ID MFA3L_HUMAN Reviewed; 409 AA. AC O75121; A8K1X6; D3DP35; Q4W5N7; Q4W5N9; Q6TNA8; Q9BVE1; Q9BXK0; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 3. DT 13-FEB-2019, entry version 153. DE RecName: Full=Microfibrillar-associated protein 3-like; DE AltName: Full=Testis development protein NYD-SP9 {ECO:0000303|Ref.1}; DE Flags: Precursor; GN Name=MFAP3L; Synonyms=KIAA0626; ORFNames=HSD-39, HSD39; 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 2), AND TISSUE SPECIFICITY. RC TISSUE=Testis; RA Xiao J.H., Yin L.L., Li J.M., Zhu H., Zhou Z.M., Zhao B.G., Sha J.H.; RT "Molecular cloning, identification and characteristics of NYD-SP9: RT gene coding protein kinase presumably involved in spermatogenesis."; RL Chin. Sci. Bull. 47:896-901(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RA Yang C.B., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.; RT "A new spermatogenesis-related gene."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; 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 [5] 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 [6] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Testis; 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 [8] RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-287, AND FUNCTION. RX PubMed=24735981; DOI=10.1016/j.bbadis.2014.04.006; RA Lou X., Kang B., Zhang J., Hao C., Tian X., Li W., Xu N., Lu Y., RA Liu S.; RT "MFAP3L activation promotes colorectal cancer cell invasion and RT metastasis."; RL Biochim. Biophys. Acta 1842:1423-1432(2014). CC -!- FUNCTION: May participate in the nuclear signaling of EGFR and CC MAPK1/ERK2. May a have a role in metastasis. CC {ECO:0000269|PubMed:24735981}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24735981}; CC Single-pass type I membrane protein {ECO:0000305}. Nucleus CC {ECO:0000269|PubMed:24735981}. Cytoplasm CC {ECO:0000269|PubMed:24735981}. Note=Mainly localized in the CC nucleus (PubMed:24735981). {ECO:0000269|PubMed:24735981}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O75121-1; Sequence=Displayed; CC Name=2; CC IsoId=O75121-2; Sequence=VSP_011100; CC Name=3; CC IsoId=O75121-3; Sequence=VSP_014094, VSP_014095; CC -!- TISSUE SPECIFICITY: Highly expressed in testis. CC {ECO:0000269|Ref.1}. CC -!- CAUTION: Protein kinase activity is reported (PubMed:24735981). CC However, no protein kinase domain is detected by any prediction CC method (PROSITE, Pfam). Its enzyme activity is therefore unsure. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA31601.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; 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; AF327560; AAK15700.1; -; mRNA. DR EMBL; AY391838; AAS55434.1; -; mRNA. DR EMBL; AB014526; BAA31601.2; ALT_INIT; mRNA. DR EMBL; AK290041; BAF82730.1; -; mRNA. DR EMBL; AC084866; AAY41028.1; -; Genomic_DNA. DR EMBL; AC084866; AAY41029.1; -; Genomic_DNA. DR EMBL; CH471056; EAX04773.1; -; Genomic_DNA. DR EMBL; CH471056; EAX04774.1; -; Genomic_DNA. DR EMBL; CH471056; EAX04775.1; -; Genomic_DNA. DR EMBL; BC001279; AAH01279.1; -; mRNA. DR EMBL; BC066912; AAH66912.1; -; mRNA. DR CCDS; CCDS34103.1; -. [O75121-1] DR CCDS; CCDS43281.1; -. [O75121-2] DR RefSeq; NP_001009554.1; NM_001009554.3. [O75121-2] DR RefSeq; NP_001288576.1; NM_001301647.1. [O75121-2] DR RefSeq; NP_001288577.1; NM_001301648.1. [O75121-2] DR RefSeq; NP_067679.6; NM_021647.7. [O75121-1] DR RefSeq; XP_005263425.1; XM_005263368.3. [O75121-2] DR RefSeq; XP_016864357.1; XM_017008868.1. [O75121-1] DR RefSeq; XP_016864358.1; XM_017008869.1. [O75121-1] DR RefSeq; XP_016864359.1; XM_017008870.1. [O75121-1] DR RefSeq; XP_016864360.1; XM_017008871.1. [O75121-1] DR UniGene; Hs.593942; -. DR UniGene; Hs.733667; -. DR ProteinModelPortal; O75121; -. DR iPTMnet; O75121; -. DR PhosphoSitePlus; O75121; -. DR BioMuta; MFAP3L; -. DR EPD; O75121; -. DR jPOST; O75121; -. DR MaxQB; O75121; -. DR PaxDb; O75121; -. DR PeptideAtlas; O75121; -. DR PRIDE; O75121; -. DR ProteomicsDB; 49774; -. DR ProteomicsDB; 49775; -. [O75121-2] DR ProteomicsDB; 49776; -. [O75121-3] DR Ensembl; ENST00000361618; ENSP00000354583; ENSG00000198948. [O75121-1] DR Ensembl; ENST00000393702; ENSP00000377305; ENSG00000198948. [O75121-3] DR Ensembl; ENST00000393704; ENSP00000377307; ENSG00000198948. [O75121-2] DR Ensembl; ENST00000506110; ENSP00000422571; ENSG00000198948. [O75121-3] DR GeneID; 9848; -. DR KEGG; hsa:9848; -. DR UCSC; uc003isn.4; human. [O75121-1] DR CTD; 9848; -. DR DisGeNET; 9848; -. DR EuPathDB; HostDB:ENSG00000198948.11; -. DR GeneCards; MFAP3L; -. DR H-InvDB; HIX0004635; -. DR HGNC; HGNC:29083; MFAP3L. DR HPA; HPA017986; -. DR neXtProt; NX_O75121; -. DR OpenTargets; ENSG00000198948; -. DR PharmGKB; PA134974574; -. DR eggNOG; ENOG410IE5Z; Eukaryota. DR eggNOG; ENOG410XPPH; LUCA. DR GeneTree; ENSGT00390000011576; -. DR HOVERGEN; HBG052463; -. DR InParanoid; O75121; -. DR OMA; KWYNSVG; -. DR OrthoDB; 1154642at2759; -. DR PhylomeDB; O75121; -. DR TreeFam; TF333205; -. DR ChiTaRS; MFAP3L; human. DR GenomeRNAi; 9848; -. DR PRO; PR:O75121; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000198948; Expressed in 210 organ(s), highest expression level in sperm. DR ExpressionAtlas; O75121; baseline and differential. DR Genevisible; O75121; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR039696; MFAP3-like. DR PANTHER; PTHR14340; PTHR14340; 1. DR Pfam; PF07679; I-set; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00408; IGc2; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; KW Nucleus; Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 28 {ECO:0000255}. FT CHAIN 29 409 Microfibrillar-associated protein 3-like. FT /FTId=PRO_0000014869. FT TOPO_DOM 29 149 Extracellular. {ECO:0000255}. FT TRANSMEM 150 172 Helical. {ECO:0000255}. FT TOPO_DOM 173 409 Cytoplasmic. {ECO:0000255}. FT DOMAIN 47 141 Ig-like C2-type. FT MOD_RES 287 287 Phosphotyrosine; by EGFR. FT {ECO:0000269|PubMed:24735981}. FT MOD_RES 298 298 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9D3X9}. FT MOD_RES 303 303 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9D3X9}. FT MOD_RES 306 306 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9D3X9}. FT MOD_RES 307 307 Phosphoserine. FT {ECO:0000250|UniProtKB:Q6AYP2}. FT CARBOHYD 33 33 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 37 37 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 67 67 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 111 111 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 135 135 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 68 125 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VAR_SEQ 1 103 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.1}. FT /FTId=VSP_011100. FT VAR_SEQ 101 102 KW -> RL (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_014094. FT VAR_SEQ 103 409 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_014095. FT CONFLICT 362 362 D -> N (in Ref. 2; AAS55434). FT {ECO:0000305}. SQ SEQUENCE 409 AA; 45380 MW; 47965B61C0F8A3AA CRC64; MDRLKSHLTV CFLPSVPFLI LVSTLATAKS VTNSTLNGTN VVLGSVPVII ARTDHIIVKE GNSALINCSV YGIPDPQFKW YNSIGKLLKE EEDEKERGGG KWQMHDSGLL NITKVSFSDR GKYTCVASNI YGTVNNTVTL RVIFTSGDMG VYYMVVCLVA FTIVMVLNIT RLCMMSSHLK KTEKAINEFF RTEGAEKLQK AFEIAKRIPI ITSAKTLELA KVTQFKTMEF ARYIEELARS VPLPPLIMNC RTIMEEIMEV VGLEEQGQNF VRHTPEGQEA ADRDEVYTIP NSLKRSDSPA ADSDASSLHE QPQQIAIKVS VHPQSKKEHA DDQEGGQFEV KDVEETELSA EHSPETAEPS TDVTSTELTS EEPTPVEVPD KVLPPAYLEA TEPAVTHDKN TCIIYESHV //