ID PROM1_HUMAN Reviewed; 865 AA. AC O43490; Q6SV49; Q6SV50; Q6SV51; Q6SV52; Q6SV53; Q96EN6; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 13-FEB-2019, entry version 169. DE RecName: Full=Prominin-1; DE AltName: Full=Antigen AC133; DE AltName: Full=Prominin-like protein 1; DE AltName: CD_antigen=CD133; DE Flags: Precursor; GN Name=PROM1; Synonyms=PROML1; ORFNames=MSTP061; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 31-42; RP 200-211; 280-291 AND 641-656. RC TISSUE=Fetal liver, and Retinoblastoma; RX PubMed=9389721; RA Miraglia S., Godfrey W., Yin A.H., Atkins K., Warnke R., Holden J.T., RA Bray R.A., Waller E.K., Buck D.W.; RT "A novel five-transmembrane hematopoietic stem cell antigen: RT isolation, characterization, and molecular cloning."; RL Blood 90:5013-5021(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND GLYCOSYLATION. RX PubMed=12042327; DOI=10.1074/jbc.M202349200; RA Yu Y., Flint A., Dvorin E.L., Bischoff J.; RT "AC133-2, a novel isoform of human AC133 stem cell antigen."; RL J. Biol. Chem. 277:20711-20716(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Lin J., Shmelkov S.V., Karajannis M.A., StClair R., Walsh K., RA Gordon R., Shido K., Lam G., Moussazadeh N., Shim W., Rafii S.; RT "Identification and functional analysis of several isoforms of RT hematopoitic stem cell surface maker prominin-1 (AC133)."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Aorta; RA Wang X.Y., Zhao B., Liu B., Xu Y.Y., Liu Y.Q., Cao H.Q., Sheng H., RA Ye J., Song L., Wei Y.J., Liu S., Liu L.S., Ding J.F., Gao R.L., RA Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP CHARACTERIZATION. RC TISSUE=Fetal liver; RX PubMed=9389720; RA Yin A.H., Miraglia S., Zanjani E.D., Almeida-Porada G., Ogawa M., RA Leary A.G., Olweus J., Kearney J., Buck D.W.; RT "AC133, a novel marker for human hematopoietic stem and progenitor RT cells."; RL Blood 90:5002-5012(1997). RN [10] RP TISSUE SPECIFICITY. RX PubMed=17874118; DOI=10.1007/s00418-007-0334-2; RA Jaszai J., Janich P., Farkas L.M., Fargeas C.A., Huttner W.B., RA Corbeil D.; RT "Differential expression of prominin-1 (CD133) and prominin-2 in major RT cephalic exocrine glands of adult mice."; RL Histochem. Cell Biol. 128:409-419(2007). RN [11] RP NOMENCLATURE OF ISOFORMS. RX PubMed=17498271; DOI=10.1111/j.1399-0039.2007.00825.x; RA Fargeas C.A., Huttner W.B., Corbeil D.; RT "Nomenclature of prominin-1 (CD133) splice variants - an update."; RL Tissue Antigens 69:602-606(2007). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=18096722; DOI=10.1634/stemcells.2007-0639; RA Huttner H.B., Janich P., Koehrmann M., Jaszai J., Siebzehnrubl F., RA Bluemcke I., Suttorp M., Gahr M., Kuhnt D., Nimsky C., Krex D., RA Schackert G., Loewenbrueck K., Reichmann H., Juettler E., Hacke W., RA Schellinger P.D., Schwab S., Wilsch-Braeuninger M., Marzesco A.M., RA Corbeil D.; RT "The stem cell marker prominin-1/CD133 on membrane particles in human RT cerebrospinal fluid offers novel approaches for studying central RT nervous system disease."; RL Stem Cells 26:698-705(2008). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=19302789; DOI=10.1016/j.febslet.2009.01.048; RA Marzesco A.M., Wilsch-Brauninger M., Dubreuil V., Janich P., RA Langenfeld K., Thiele C., Huttner W.B., Corbeil D.; RT "Release of extracellular membrane vesicles from microvilli of RT epithelial cells is enhanced by depleting membrane cholesterol."; RL FEBS Lett. 583:897-902(2009). RN [14] RP FUNCTION. RX PubMed=20818439; DOI=10.1038/onc.2010.383; RA Takenobu H., Shimozato O., Nakamura T., Ochiai H., Yamaguchi Y., RA Ohira M., Nakagawara A., Kamijo T.; RT "CD133 suppresses neuroblastoma cell differentiation via signal RT pathway modification."; RL Oncogene 30:97-105(2011). RN [15] RP INVOLVEMENT IN RP41. RX PubMed=10587575; DOI=10.1093/hmg/9.1.27; RA Maw M.A., Corbeil D., Koch J., Hellwig A., Wilson-Wheeler J.C., RA Bridges R.J., Kumaramanickavel G., John S., Nancarrow D., Roeper K., RA Weigmann A., Huttner W.B., Denton M.J.; RT "A frameshift mutation in prominin (mouse)-like 1 causes human retinal RT degeneration."; RL Hum. Mol. Genet. 9:27-34(2000). RN [16] RP INVOLVEMENT IN RP41. RX PubMed=17605048; DOI=10.1007/s00439-007-0395-2; RA Zhang Q., Zulfiqar F., Xiao X., Riazuddin S.A., Ahmad Z., Caruso R., RA MacDonald I., Sieving P., Riazuddin S., Hejtmancik J.F.; RT "Severe retinitis pigmentosa mapped to 4p15 and associated with a RT novel mutation in the PROM1 gene."; RL Hum. Genet. 122:293-299(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, RP ACETYLATION AT LYS-225; LYS-257 AND LYS-264 BY NAT8 AND NAT8B, RP MUTAGENESIS OF LYS-225; LYS-257 AND LYS-264, AND INTERACTION WITH NAT8 RP AND NAT8B. RX PubMed=24556617; DOI=10.1016/j.jmb.2014.02.012; RA Mak A.B., Pehar M., Nixon A.M., Williams R.A., Uetrecht A.C., RA Puglielli L., Moffat J.; RT "Post-translational regulation of CD133 by ATase1/ATase2-mediated RT lysine acetylation."; RL J. Mol. Biol. 426:2175-2182(2014). RN [19] RP INVOLVEMENT IN CORD12, INVOLVEMENT IN STGD4, INVOLVEMENT IN MCDR2, RP VARIANT CORD12/STGD4/MCDR2 CYS-373, INTERACTION WITH CDHR1 AND ACTIN, RP AND CHARACTERIZATION OF VARIANT CORD12/STGD4/MCDR2 CYS-373. RX PubMed=18654668; DOI=10.1172/JCI35891; RA Yang Z., Chen Y., Lillo C., Chien J., Yu Z., Michaelides M., Klein M., RA Howes K.A., Li Y., Kaminoh Y., Chen H., Zhao C., Chen Y., RA Al-Sheikh Y.T., Karan G., Corbeil D., Escher P., Kamaya S., Li C., RA Johnson S., Frederick J.M., Zhao Y., Wang C., Cameron D.J., RA Huttner W.B., Schorderet D.F., Munier F.L., Moore A.T., Birch D.G., RA Baehr W., Hunt D.M., Williams D.S., Zhang K.; RT "Mutant prominin 1 found in patients with macular degeneration RT disrupts photoreceptor disk morphogenesis in mice."; RL J. Clin. Invest. 118:2908-2916(2008). CC -!- FUNCTION: May play a role in cell differentiation, proliferation CC and apoptosis (PubMed:24556617). Binds cholesterol in cholesterol- CC containing plasma membrane microdomains and may play a role in the CC organization of the apical plasma membrane in epithelial cells. CC During early retinal development acts as a key regulator of disk CC morphogenesis. Involved in regulation of MAPK and Akt signaling CC pathways. In neuroblastoma cells suppresses cell differentiation CC such as neurite outgrowth in a RET-dependent manner CC (PubMed:20818439). {ECO:0000269|PubMed:20818439, CC ECO:0000269|PubMed:24556617}. CC -!- SUBUNIT: Interacts with CDHR1 and with actin filaments. Interacts CC with NAT8 and NAT8B. {ECO:0000269|PubMed:18654668, CC ECO:0000269|PubMed:24556617}. CC -!- INTERACTION: CC Q8VHP6:Cdhr1 (xeno); NbExp=3; IntAct=EBI-3447549, EBI-4395045; CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. Cell projection, microvillus CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC Cell projection, cilium, photoreceptor outer segment CC {ECO:0000250}. Endoplasmic reticulum. Endoplasmic reticulum-Golgi CC intermediate compartment. Note=Found in extracellular membrane CC particles in various body fluids such as cerebrospinal fluid, CC saliva, seminal fluid and urine. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=AC133-1, S2; CC IsoId=O43490-1; Sequence=Displayed; CC Name=2; Synonyms=AC133-2, S1; CC IsoId=O43490-2; Sequence=VSP_039069; CC Name=3; Synonyms=S3; CC IsoId=O43490-3; Sequence=VSP_040000, VSP_040002, VSP_040004; CC Name=4; Synonyms=S10; CC IsoId=O43490-4; Sequence=VSP_040000, VSP_040003; CC Name=5; Synonyms=S7; CC IsoId=O43490-5; Sequence=VSP_040000, VSP_040001; CC Name=6; Synonyms=S11; CC IsoId=O43490-6; Sequence=VSP_040001; CC Name=7; Synonyms=S12; CC IsoId=O43490-7; Sequence=VSP_040003; CC -!- TISSUE SPECIFICITY: Isoform 1 is selectively expressed on CD34 CC hematopoietic stem and progenitor cells in adult and fetal bone CC marrow, fetal liver, cord blood and adult peripheral blood. CC Isoform 1 is not detected on other blood cells. Isoform 1 is also CC expressed in a number of non-lymphoid tissues including retina, CC pancreas, placenta, kidney, liver, lung, brain and heart. Found in CC saliva within small membrane particles. Isoform 2 is predominantly CC expressed in fetal liver, skeletal muscle, kidney, and heart as CC well as adult pancreas, kidney, liver, lung, and placenta. Isoform CC 2 is highly expressed in fetal liver, low in bone marrow, and CC barely detectable in peripheral blood. Isoform 2 is expressed on CC hematopoietic stem cells and in epidermal basal cells (at protein CC level). Expressed in adult retina by rod and cone photoreceptor CC cells (at protein level). {ECO:0000269|PubMed:12042327, CC ECO:0000269|PubMed:17874118}. CC -!- PTM: Isoform 1 and isoform 2 are glycosylated. CC {ECO:0000269|PubMed:12042327}. CC -!- PTM: Acetylation at Lys-225, Lys-257 and Lys-264 by NAT8 and NAT8B CC may control PROM1 protein expression and its function in cell CC apoptosis. {ECO:0000269|PubMed:24556617}. CC -!- DISEASE: Retinitis pigmentosa 41 (RP41) [MIM:612095]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. CC Retinitis pigmentosa is characterized by retinal pigment deposits CC visible on fundus examination and primary loss of rod CC photoreceptor cells followed by secondary loss of cone CC photoreceptors. Patients typically have night vision blindness and CC loss of midperipheral visual field. As their condition progresses, CC they lose their far peripheral visual field and eventually central CC vision as well. {ECO:0000269|PubMed:10587575, CC ECO:0000269|PubMed:17605048}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Cone-rod dystrophy 12 (CORD12) [MIM:612657]: An inherited CC retinal dystrophy characterized by retinal pigment deposits CC visible on fundus examination, predominantly in the macular CC region, and initial loss of cone photoreceptors followed by rod CC degeneration. This leads to decreased visual acuity and CC sensitivity in the central visual field, followed by loss of CC peripheral vision. Severe loss of vision occurs earlier than in CC retinitis pigmentosa, due to cone photoreceptors degenerating at a CC higher rate than rod photoreceptors. CC {ECO:0000269|PubMed:18654668}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Stargardt disease 4 (STGD4) [MIM:603786]: A common CC hereditary macular degeneration. It is characterized by decreased CC central vision, atrophy of the macula and underlying retinal CC pigment epithelium, and frequent presence of prominent flecks in CC the posterior pole of the retina. {ECO:0000269|PubMed:18654668}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Retinal macular dystrophy 2 (MCDR2) [MIM:608051]: A CC bull's-eye macular dystrophy characterized by bilateral annular CC atrophy of retinal pigment epithelium at the macula. CC {ECO:0000269|PubMed:18654668}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Is used as marker for hematopoietic stem and CC progenitor cells (HSPC) for somatic stem cell isolation. CC -!- SIMILARITY: Belongs to the prominin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Mutations of the PROM1 gene; Note=Retina CC International's Scientific Newsletter; CC URL="http://www.retina-international.org/files/sci-news/promlmut.htm"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF027208; AAB92514.1; -; mRNA. DR EMBL; AF507034; AAM33415.1; -; mRNA. DR EMBL; AY449689; AAS19705.1; -; mRNA. DR EMBL; AY449690; AAS19706.1; -; mRNA. DR EMBL; AY449691; AAS19707.1; -; mRNA. DR EMBL; AY449692; AAS19708.1; -; mRNA. DR EMBL; AY449693; AAS19709.1; -; mRNA. DR EMBL; AF117225; AAO15307.1; -; mRNA. DR EMBL; AK027422; BAG51317.1; -; mRNA. DR EMBL; AC005598; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108063; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471069; EAW92750.1; -; Genomic_DNA. DR EMBL; BC012089; AAH12089.1; -; mRNA. DR CCDS; CCDS47029.1; -. [O43490-1] DR CCDS; CCDS54746.1; -. [O43490-2] DR CCDS; CCDS54747.1; -. [O43490-6] DR CCDS; CCDS54748.1; -. [O43490-7] DR PIR; T09050; T09050. DR RefSeq; NP_001139319.1; NM_001145847.1. [O43490-2] DR RefSeq; NP_001139320.1; NM_001145848.1. [O43490-2] DR RefSeq; NP_001139321.1; NM_001145849.1. [O43490-7] DR RefSeq; NP_001139322.1; NM_001145850.1. [O43490-6] DR RefSeq; NP_001139323.1; NM_001145851.1. [O43490-4] DR RefSeq; NP_001139324.1; NM_001145852.1. [O43490-5] DR RefSeq; NP_006008.1; NM_006017.2. [O43490-1] DR RefSeq; XP_005248252.1; XM_005248195.4. [O43490-4] DR RefSeq; XP_005248253.1; XM_005248196.4. [O43490-5] DR RefSeq; XP_011512192.1; XM_011513890.1. [O43490-1] DR RefSeq; XP_011512194.1; XM_011513892.2. [O43490-1] DR RefSeq; XP_011512195.1; XM_011513893.2. [O43490-1] DR RefSeq; XP_011512196.1; XM_011513894.2. [O43490-1] DR RefSeq; XP_011512197.1; XM_011513895.2. [O43490-1] DR RefSeq; XP_011512198.1; XM_011513896.2. [O43490-1] DR RefSeq; XP_011512199.1; XM_011513897.2. [O43490-1] DR RefSeq; XP_011512201.2; XM_011513899.2. DR RefSeq; XP_011512202.1; XM_011513900.2. [O43490-7] DR RefSeq; XP_011512204.1; XM_011513902.2. [O43490-6] DR RefSeq; XP_016864288.1; XM_017008799.1. [O43490-2] DR RefSeq; XP_016864291.1; XM_017008802.1. [O43490-6] DR RefSeq; XP_016864292.1; XM_017008803.1. [O43490-5] DR RefSeq; XP_016864293.1; XM_017008804.1. [O43490-5] DR RefSeq; XP_016864294.1; XM_017008805.1. [O43490-5] DR UniGene; Hs.614734; -. DR ProteinModelPortal; O43490; -. DR SMR; O43490; -. DR BioGrid; 114369; 9. DR IntAct; O43490; 4. DR STRING; 9606.ENSP00000415481; -. DR GlyConnect; 1642; -. DR iPTMnet; O43490; -. DR PhosphoSitePlus; O43490; -. DR BioMuta; PROM1; -. DR EPD; O43490; -. DR jPOST; O43490; -. DR MaxQB; O43490; -. DR PaxDb; O43490; -. DR PeptideAtlas; O43490; -. DR PRIDE; O43490; -. DR ProteomicsDB; 48967; -. DR ProteomicsDB; 48968; -. [O43490-2] DR ProteomicsDB; 48969; -. [O43490-3] DR ProteomicsDB; 48970; -. [O43490-4] DR ProteomicsDB; 48971; -. [O43490-5] DR ProteomicsDB; 48972; -. [O43490-6] DR ProteomicsDB; 48973; -. [O43490-7] DR DNASU; 8842; -. DR Ensembl; ENST00000447510; ENSP00000415481; ENSG00000007062. [O43490-1] DR Ensembl; ENST00000505450; ENSP00000426090; ENSG00000007062. [O43490-2] DR Ensembl; ENST00000508167; ENSP00000427346; ENSG00000007062. [O43490-2] DR Ensembl; ENST00000510224; ENSP00000426809; ENSG00000007062. [O43490-1] DR Ensembl; ENST00000539194; ENSP00000443620; ENSG00000007062. [O43490-6] DR Ensembl; ENST00000540805; ENSP00000438045; ENSG00000007062. [O43490-7] DR GeneID; 8842; -. DR KEGG; hsa:8842; -. DR UCSC; uc003goo.2; human. [O43490-1] DR CTD; 8842; -. DR DisGeNET; 8842; -. DR EuPathDB; HostDB:ENSG00000007062.11; -. DR GeneCards; PROM1; -. DR GeneReviews; PROM1; -. DR H-InvDB; HIX0004116; -. DR HGNC; HGNC:9454; PROM1. DR HPA; CAB011525; -. DR HPA; HPA004922; -. DR HPA; HPA031053; -. DR MalaCards; PROM1; -. DR MIM; 603786; phenotype. DR MIM; 604365; gene. DR MIM; 608051; phenotype. DR MIM; 612095; phenotype. DR MIM; 612657; phenotype. DR neXtProt; NX_O43490; -. DR OpenTargets; ENSG00000007062; -. DR Orphanet; 1872; Cone rod dystrophy. DR Orphanet; 319640; Retinal macular dystrophy type 2. DR Orphanet; 791; Retinitis pigmentosa. DR Orphanet; 827; Stargardt disease. DR PharmGKB; PA33807; -. DR eggNOG; KOG4331; Eukaryota. DR eggNOG; ENOG410XRG0; LUCA. DR GeneTree; ENSGT00530000063586; -. DR HOGENOM; HOG000115704; -. DR HOVERGEN; HBG053690; -. DR InParanoid; O43490; -. DR KO; K06532; -. DR OMA; HLYGIHN; -. DR OrthoDB; 704215at2759; -. DR PhylomeDB; O43490; -. DR TreeFam; TF324631; -. DR SIGNOR; O43490; -. DR ChiTaRS; PROM1; human. DR GeneWiki; CD133; -. DR GenomeRNAi; 8842; -. DR PRO; PR:O43490; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000007062; Expressed in 189 organ(s), highest expression level in bronchial epithelial cell. DR ExpressionAtlas; O43490; baseline and differential. DR Genevisible; O43490; HS. DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005902; C:microvillus; IBA:GO_Central. DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB. DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0071914; C:prominosome; IBA:GO_Central. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0042805; F:actinin binding; IDA:BHF-UCL. DR GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL. DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central. DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IMP:BHF-UCL. DR GO; GO:0072139; P:glomerular parietal epithelial cell differentiation; IMP:UniProtKB. DR GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; IMP:UniProtKB. DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:BHF-UCL. DR GO; GO:2000768; P:positive regulation of nephron tubule epithelial cell differentiation; IMP:UniProtKB. DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB. DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:BHF-UCL. DR InterPro; IPR008795; Prominin. DR PANTHER; PTHR22730; PTHR22730; 1. DR Pfam; PF05478; Prominin; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell membrane; Cell projection; KW Cilium; Complete proteome; Cone-rod dystrophy; KW Direct protein sequencing; Disease mutation; Endoplasmic reticulum; KW Glycoprotein; Membrane; Phosphoprotein; Polymorphism; KW Reference proteome; Retinitis pigmentosa; Signal; Stargardt disease; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 865 Prominin-1. FT /FTId=PRO_0000025813. FT TOPO_DOM 20 108 Extracellular. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TOPO_DOM 130 157 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TOPO_DOM 179 433 Extracellular. {ECO:0000255}. FT TRANSMEM 434 454 Helical. {ECO:0000255}. FT TOPO_DOM 455 486 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 487 507 Helical. {ECO:0000255}. FT TOPO_DOM 508 792 Extracellular. {ECO:0000255}. FT TRANSMEM 793 813 Helical. {ECO:0000255}. FT TOPO_DOM 814 865 Cytoplasmic. {ECO:0000255}. FT MOD_RES 225 225 N6-acetyllysine. FT {ECO:0000269|PubMed:24556617}. FT MOD_RES 257 257 N6-acetyllysine. FT {ECO:0000269|PubMed:24556617}. FT MOD_RES 264 264 N6-acetyllysine. FT {ECO:0000269|PubMed:24556617}. FT MOD_RES 863 863 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT CARBOHYD 220 220 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 274 274 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 395 395 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 414 414 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 548 548 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 580 580 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 729 729 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 730 730 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 92 100 Missing (in isoform 2). FT {ECO:0000303|PubMed:12042327, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.4}. FT /FTId=VSP_039069. FT VAR_SEQ 93 101 Missing (in isoform 3, isoform 4 and FT isoform 5). {ECO:0000303|Ref.3}. FT /FTId=VSP_040000. FT VAR_SEQ 831 861 Missing (in isoform 5 and isoform 6). FT {ECO:0000305}. FT /FTId=VSP_040001. FT VAR_SEQ 831 839 VETIPMKNM -> SSWVTSVQC (in isoform 3). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_040002. FT VAR_SEQ 839 861 Missing (in isoform 4 and isoform 7). FT {ECO:0000305}. FT /FTId=VSP_040003. FT VAR_SEQ 840 865 Missing (in isoform 3). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_040004. FT VARIANT 31 31 A -> G. FT /FTId=VAR_010382. FT VARIANT 31 31 A -> S. FT /FTId=VAR_010383. FT VARIANT 373 373 R -> C (in CORD12, STGD4 and MCDR2; FT affects the interaction with actin; FT dbSNP:rs137853006). FT {ECO:0000269|PubMed:18654668}. FT /FTId=VAR_057961. FT MUTAGEN 225 225 K->Q: Loss of acetylation; when FT associated with Q-257 and Q-264. FT {ECO:0000269|PubMed:24556617}. FT MUTAGEN 225 225 K->R: Loss of expression of the protein FT in part due to proteasomal degradation; FT when associated with Q-257 and Q-264. FT {ECO:0000269|PubMed:24556617}. FT MUTAGEN 257 257 K->Q: Loss of acetylation; when FT associated with Q-225 and Q-264. FT {ECO:0000269|PubMed:24556617}. FT MUTAGEN 257 257 K->R: Loss of expression of the protein FT in part due to proteasomal degradation; FT when associated with Q-225 and Q-264. FT {ECO:0000269|PubMed:24556617}. FT MUTAGEN 264 264 K->Q: Loss of acetylation; when FT associated with Q-225 and Q-257. FT {ECO:0000269|PubMed:24556617}. FT MUTAGEN 264 264 K->R: Loss of expression of the protein FT in part due to proteasomal degradation; FT when associated with Q-225 and Q-257. FT {ECO:0000269|PubMed:24556617}. FT CONFLICT 200 200 D -> A (in Ref. 1; AA sequence). FT {ECO:0000305}. FT CONFLICT 200 200 D -> P (in Ref. 1; AA sequence). FT {ECO:0000305}. FT CONFLICT 284 284 S -> D (in Ref. 1; AA sequence). FT {ECO:0000305}. FT CONFLICT 288 288 S -> R (in Ref. 1; AA sequence). FT {ECO:0000305}. SQ SEQUENCE 865 AA; 97202 MW; D21CBC05ADB2DEDF CRC64; MALVLGSLLL LGLCGNSFSG GQPSSTDAPK AWNYELPATN YETQDSHKAG PIGILFELVH IFLYVVQPRD FPEDTLRKFL QKAYESKIDY DKPETVILGL KIVYYEAGII LCCVLGLLFI ILMPLVGYFF CMCRCCNKCG GEMHQRQKEN GPFLRKCFAI SLLVICIIIS IGIFYGFVAN HQVRTRIKRS RKLADSNFKD LRTLLNETPE QIKYILAQYN TTKDKAFTDL NSINSVLGGG ILDRLRPNII PVLDEIKSMA TAIKETKEAL ENMNSTLKSL HQQSTQLSSS LTSVKTSLRS SLNDPLCLVH PSSETCNSIR LSLSQLNSNP ELRQLPPVDA ELDNVNNVLR TDLDGLVQQG YQSLNDIPDR VQRQTTTVVA GIKRVLNSIG SDIDNVTQRL PIQDILSAFS VYVNNTESYI HRNLPTLEEY DSYWWLGGLV ICSLLTLIVI FYYLGLLCGV CGYDRHATPT TRGCVSNTGG VFLMVGVGLS FLFCWILMII VVLTFVFGAN VEKLICEPYT SKELFRVLDT PYLLNEDWEY YLSGKLFNKS KMKLTFEQVY SDCKKNRGTY GTLHLQNSFN ISEHLNINEH TGSISSELES LKVNLNIFLL GAAGRKNLQD FAACGIDRMN YDSYLAQTGK SPAGVNLLSF AYDLEAKANS LPPGNLRNSL KRDAQTIKTI HQQRVLPIEQ SLSTLYQSVK ILQRTGNGLL ERVTRILASL DFAQNFITNN TSSVIIEETK KYGRTIIGYF EHYLQWIEFS ISEKVASCKP VATALDTAVD VFLCSYIIDP LNLFWFGIGK ATVFLLPALI FAVKLAKYYR RMDSEDVYDD VETIPMKNME NGNNGYHKDH VYGIHNPVMT SPSQH //