CAD16_HUMAN
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 03-AUG-2022, entry version 174.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 isoforms
RT 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., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., 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., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types.
CC -!- INTERACTION:
CC O75309; Q92876: KLK6; NbExp=3; IntAct=EBI-2837263, EBI-2432309;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC 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 Name=3;
CC IsoId=O75309-3; Sequence=VSP_046027;
CC Name=4;
CC IsoId=O75309-4; Sequence=VSP_046467;
CC -!- TISSUE SPECIFICITY: Kidney specific.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
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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 AlphaFoldDB; O75309; -.
DR SMR; O75309; -.
DR BioGRID; 107449; 31.
DR IntAct; O75309; 5.
DR STRING; 9606.ENSP00000299752; -.
DR GlyGen; O75309; 6 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; O75309; -.
DR PhosphoSitePlus; O75309; -.
DR BioMuta; CDH16; -.
DR jPOST; O75309; -.
DR MassIVE; O75309; -.
DR PaxDb; O75309; -.
DR PeptideAtlas; O75309; -.
DR PRIDE; O75309; -.
DR ProteomicsDB; 41459; -.
DR ProteomicsDB; 4774; -.
DR ProteomicsDB; 49884; -. [O75309-1]
DR ProteomicsDB; 49885; -. [O75309-2]
DR Antibodypedia; 29333; 601 antibodies from 31 providers.
DR DNASU; 1014; -.
DR Ensembl; ENST00000299752.9; ENSP00000299752.4; ENSG00000166589.13. [O75309-1]
DR Ensembl; ENST00000394055.7; ENSP00000377619.3; ENSG00000166589.13. [O75309-2]
DR Ensembl; ENST00000565796.5; ENSP00000454784.1; ENSG00000166589.13. [O75309-4]
DR Ensembl; ENST00000568632.5; ENSP00000455263.1; ENSG00000166589.13. [O75309-3]
DR GeneID; 1014; -.
DR KEGG; hsa:1014; -.
DR MANE-Select; ENST00000299752.9; ENSP00000299752.4; NM_004062.4; NP_004053.1.
DR UCSC; uc002eql.3; human. [O75309-1]
DR CTD; 1014; -.
DR DisGeNET; 1014; -.
DR GeneCards; CDH16; -.
DR HGNC; HGNC:1755; CDH16.
DR HPA; ENSG00000166589; Tissue enriched (kidney).
DR MIM; 603118; gene.
DR neXtProt; NX_O75309; -.
DR OpenTargets; ENSG00000166589; -.
DR PharmGKB; PA26289; -.
DR VEuPathDB; HostDB:ENSG00000166589; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161650; -.
DR HOGENOM; CLU_016170_1_0_1; -.
DR InParanoid; O75309; -.
DR OMA; QHEYGPF; -.
DR OrthoDB; 190556at2759; -.
DR PhylomeDB; O75309; -.
DR TreeFam; TF316817; -.
DR PathwayCommons; O75309; -.
DR SignaLink; O75309; -.
DR SIGNOR; O75309; -.
DR BioGRID-ORCS; 1014; 12 hits in 1068 CRISPR screens.
DR GeneWiki; CDH16; -.
DR GenomeRNAi; 1014; -.
DR Pharos; O75309; Tbio.
DR PRO; PR:O75309; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O75309; protein.
DR Bgee; ENSG00000166589; Expressed in metanephros cortex and 86 other tissues.
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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..829
FT /note="Cadherin-16"
FT /id="PRO_0000003809"
FT TOPO_DOM 19..786
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..126
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 131..235
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 242..336
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 341..449
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 455..564
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 569..665
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 666..786
FT /note="Ectodomain G"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88338"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 121..217
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_046027"
FT VAR_SEQ 642..680
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046467"
FT VAR_SEQ 642..663
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013354"
FT VARIANT 191
FT /note="L -> F (in dbSNP:rs2271024)"
FT /id="VAR_021870"
FT VARIANT 257
FT /note="H -> Y (in dbSNP:rs2271023)"
FT /id="VAR_021871"
FT VARIANT 717
FT /note="R -> H (in dbSNP:rs34621310)"
FT /id="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
