ID   CAD13_BOVIN             Reviewed;         713 AA.
AC   Q3B7N0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Cadherin-13;
DE   Flags: Precursor;
GN   Name=CDH13;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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. May act as a negative regulator of neural
CC       cell growth (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: By contrast to classical cadherins, homodimerization in trans
CC       is not mediated by cadherin EC1 domain strand-swapping, but instead
CC       through a homophilic adhesive interface which joins two elongated EC1-
CC       EC2 domains through a region near their Ca2+-binding sites to form a
CC       tetrahedral, X-like shape. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
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; BC107535; AAI07536.1; -; mRNA.
DR   RefSeq; NP_001030354.1; NM_001035277.2.
DR   AlphaFoldDB; Q3B7N0; -.
DR   SMR; Q3B7N0; -.
DR   STRING; 9913.ENSBTAP00000051651; -.
DR   PaxDb; Q3B7N0; -.
DR   PeptideAtlas; Q3B7N0; -.
DR   PRIDE; Q3B7N0; -.
DR   GeneID; 512302; -.
DR   KEGG; bta:512302; -.
DR   CTD; 1012; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; Q3B7N0; -.
DR   OrthoDB; 215774at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR014868; Cadherin_pro_dom.
DR   InterPro; IPR033216; CDH13.
DR   PANTHER; PTHR24027; PTHR24027; 1.
DR   PANTHER; PTHR24027:SF80; PTHR24027:SF80; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08758; Cadherin_pro; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SMART; SM01055; Cadherin_pro; 1.
DR   SUPFAM; SSF49313; SSF49313; 6.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW   Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..138
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000246164"
FT   CHAIN           139..693
FT                   /note="Cadherin-13"
FT                   /id="PRO_0000246165"
FT   PROPEP          694..713
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000246166"
FT   DOMAIN          139..245
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          246..363
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          364..477
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          478..585
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          584..694
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          156..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           693
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        598
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        638
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        671
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   713 AA;  78197 MW;  E2AFE2C6919A5EC5 CRC64;
     MQPATPLVLC VLLSQVLLLT SAEDLDCTPG FQQKVFHIDQ PAEFIEDQAI LNLTFSDCKG
     NDKLHYEVSS PYFRVNTDGS LVALRNITAV GKTLFVHART PHAEDMAELV IVGGKDIQGS
     LQDIFKFART SPVPRQKRSI VVSPILIPEN QRQPFPRDVG KVVDSDRPEG SKFRLTGKGV
     DQEPKGIFRI NENTGSVSVT RNLDRETIAT YQLFVETVDV NGRTLEGPVP LEVIVIDQND
     NRPIFREGPY IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY
     IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT IMIDDKNDHS
     PKFTKKEFQA TVEEGAMGVI VNLTVEDKDD PTTGAWRAAY TIINGNPGQS FEIHTNPQTN
     EGMLSVVKPL DYEISAFHTL LIKVENEDPL VPDVSYGSSS TATVHITVLD ANESPVFYPD
     PMMVTKQENI SVGSVLLTVN ATDPDSLQRQ TIRYSVYKDP AGWLNINPIN GTVDTTALLD
     RESPFVHNSV YTALFLATDS GNPPATGTGT LLITLEDVND NAPFIYPTVA EVCDDAKNLS
     VVILGATDKD LHPNTDPFKF EIHKQTVPDK VWKISKINNT HALVSLLQNL NKANYHLPIM
     VTDSGKPPMT NITDLRVQVC SCKNSKVDCN AAGAPHFSAA TALLLSLFSL ARL