ID CAD16_HUMAN Reviewed; 829 AA. AC O75309; B4DPA8; H3BPD3; Q6UW93; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 13-FEB-2019, entry version 157. DE RecName: Full=Cadherin-16; DE AltName: Full=Kidney-specific cadherin; DE Short=Ksp-cadherin; DE Flags: Precursor; GN Name=CDH16; ORFNames=UNQ695/PRO1340; 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). RX PubMed=9721215; DOI=10.1006/geno.1998.5402; RA Thomson R.B., Ward D.C., Quaggin S.E., Igarashi P., Muckler Z.E., RA Aronson P.S.; RT "cDNA cloning and chromosomal localization of the human and mouse RT isoforms of Ksp-cadherin."; RL Genomics 51:445-451(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Kidney; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Kidney; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Spleen; 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). CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. CC They preferentially interact with themselves in a homophilic CC manner in connecting cells; cadherins may thus contribute to the CC sorting of heterogeneous cell types. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC type I membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O75309-1; Sequence=Displayed; CC Name=2; CC IsoId=O75309-2; Sequence=VSP_013354; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=O75309-3; Sequence=VSP_046027; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=O75309-4; Sequence=VSP_046467; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Kidney specific. CC -!- DOMAIN: Three calcium ions are usually bound at the interface of CC each cadherin domain and rigidify the connections, imparting a CC strong curvature to the full-length ectodomain. {ECO:0000250}. 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; AF016272; AAC34255.1; -; mRNA. DR EMBL; AY358911; AAQ89270.1; -; mRNA. DR EMBL; AK225544; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK298255; BAG60520.1; -; mRNA. DR EMBL; AC009084; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC027912; AAH27912.1; -; mRNA. DR CCDS; CCDS10823.1; -. [O75309-1] DR CCDS; CCDS56002.1; -. [O75309-2] DR CCDS; CCDS58471.1; -. [O75309-4] DR CCDS; CCDS58472.1; -. [O75309-3] DR RefSeq; NP_001191673.1; NM_001204744.1. [O75309-2] DR RefSeq; NP_001191674.1; NM_001204745.1. [O75309-4] DR RefSeq; NP_001191675.1; NM_001204746.1. [O75309-3] DR RefSeq; NP_004053.1; NM_004062.3. [O75309-1] DR UniGene; Hs.513660; -. DR ProteinModelPortal; O75309; -. DR BioGrid; 107449; 3. DR IntAct; O75309; 3. DR STRING; 9606.ENSP00000299752; -. DR iPTMnet; O75309; -. DR PhosphoSitePlus; O75309; -. DR BioMuta; CDH16; -. DR jPOST; O75309; -. DR PaxDb; O75309; -. DR PeptideAtlas; O75309; -. DR PRIDE; O75309; -. DR ProteomicsDB; 49884; -. DR ProteomicsDB; 49885; -. [O75309-2] DR DNASU; 1014; -. DR Ensembl; ENST00000299752; ENSP00000299752; ENSG00000166589. [O75309-1] DR Ensembl; ENST00000394055; ENSP00000377619; ENSG00000166589. [O75309-2] DR Ensembl; ENST00000565796; ENSP00000454784; ENSG00000166589. [O75309-4] DR Ensembl; ENST00000568632; ENSP00000455263; ENSG00000166589. [O75309-3] DR GeneID; 1014; -. DR KEGG; hsa:1014; -. DR UCSC; uc002eql.3; human. [O75309-1] DR CTD; 1014; -. DR DisGeNET; 1014; -. DR EuPathDB; HostDB:ENSG00000166589.12; -. DR GeneCards; CDH16; -. DR HGNC; HGNC:1755; CDH16. DR HPA; CAB013526; -. DR HPA; HPA036260; -. DR MIM; 603118; gene. DR neXtProt; NX_O75309; -. DR OpenTargets; ENSG00000166589; -. DR PharmGKB; PA26289; -. DR eggNOG; KOG3594; Eukaryota. DR eggNOG; ENOG410XQHI; LUCA. DR GeneTree; ENSGT00940000161650; -. DR HOGENOM; HOG000231613; -. DR HOVERGEN; HBG050766; -. DR InParanoid; O75309; -. DR KO; K06810; -. DR OMA; HHIAQVH; -. DR OrthoDB; 190556at2759; -. DR PhylomeDB; O75309; -. DR TreeFam; TF316817; -. DR GeneWiki; CDH16; -. DR GenomeRNAi; 1014; -. DR PRO; PR:O75309; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000166589; Expressed in 57 organ(s), highest expression level in adult mammalian kidney. DR ExpressionAtlas; O75309; baseline and differential. DR Genevisible; O75309; HS. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro. DR InterPro; IPR030721; Cadherin-16. DR InterPro; IPR002126; Cadherin-like_dom. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR020894; Cadherin_CS. DR PANTHER; PTHR24028:SF1; PTHR24028:SF1; 1. DR Pfam; PF00028; Cadherin; 4. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 6. DR SUPFAM; SSF49313; SSF49313; 6. DR PROSITE; PS00232; CADHERIN_1; 2. DR PROSITE; PS50268; CADHERIN_2; 5. PE 2: Evidence at transcript level; KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; KW Complete proteome; Glycoprotein; Membrane; Metal-binding; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 829 Cadherin-16. FT /FTId=PRO_0000003809. FT TOPO_DOM 19 786 Extracellular. {ECO:0000255}. FT TRANSMEM 787 807 Helical. {ECO:0000255}. FT TOPO_DOM 808 829 Cytoplasmic. {ECO:0000255}. FT DOMAIN 25 126 Cadherin 1. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 131 235 Cadherin 2. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 242 336 Cadherin 3. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 341 449 Cadherin 4. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 455 564 Cadherin 5. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 569 665 Cadherin 6. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT REGION 666 786 Ectodomain G. FT MOD_RES 822 822 Phosphoserine. FT {ECO:0000250|UniProtKB:O88338}. FT CARBOHYD 517 517 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 602 602 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 722 722 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 121 217 Missing (in isoform 3). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_046027. FT VAR_SEQ 642 680 Missing (in isoform 4). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_046467. FT VAR_SEQ 642 663 Missing (in isoform 2). FT {ECO:0000303|PubMed:12975309}. FT /FTId=VSP_013354. FT VARIANT 191 191 L -> F (in dbSNP:rs2271024). FT /FTId=VAR_021870. FT VARIANT 257 257 H -> Y (in dbSNP:rs2271023). FT /FTId=VAR_021871. FT VARIANT 717 717 R -> H (in dbSNP:rs34621310). FT /FTId=VAR_061058. SQ SEQUENCE 829 AA; 89923 MW; 41966915E4BFC891 CRC64; MVPAWLWLLC VSVPQALPKA QPAELSVEVP ENYGGNFPLY LTKLPLPREG AEGQIVLSGD SGKATEGPFA MDPDSGFLLV TRALDREEQA EYQLQVTLEM QDGHVLWGPQ PVLVHVKDEN DQVPHFSQAI YRARLSRGTR PGIPFLFLEA SDRDEPGTAN SDLRFHILSQ APAQPSPDMF QLEPRLGALA LSPKGSTSLD HALERTYQLL VQVKDMGDQA SGHQATATVE VSIIESTWVS LEPIHLAENL KVLYPHHMAQ VHWSGGDVHY HLESHPPGPF EVNAEGNLYV TRELDREAQA EYLLQVRAQN SHGEDYAAPL ELHVLVMDEN DNVPICPPRD PTVSIPELSP PGTEVTRLSA EDADAPGSPN SHVVYQLLSP EPEDGVEGRA FQVDPTSGSV TLGVLPLRAG QNILLLVLAM DLAGAEGGFS STCEVEVAVT DINDHAPEFI TSQIGPISLP EDVEPGTLVA MLTAIDADLE PAFRLMDFAI ERGDTEGTFG LDWEPDSGHV RLRLCKNLSY EAAPSHEVVV VVQSVAKLVG PGPGPGATAT VTVLVERVMP PPKLDQESYE ASVPISAPAG SFLLTIQPSD PISRTLRFSL VNDSEGWLCI EKFSGEVHTA QSLQGAQPGD TYTVLVEAQD TDEPRLSASA PLVIHFLKAP PAPALTLAPV PSQYLCTPRQ DHGLIVSGPS KDPDLASGHG PYSFTLGPNP TVQRDWRLQT LNGSHAYLTL ALHWVEPREH IIPVVVSHNA QMWQLLVRVI VCRCNVEGQC MRKVGRMKGM PTKLSAVGIL VGTLVAIGIF LILIFTHWTM SRKKDPDQPA DSVPLKATV //