CAD13_PONAB
ID CAD13_PONAB Reviewed; 713 AA.
AC Q5R5W6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Cadherin-13;
DE Flags: Precursor;
GN Name=CDH13;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860736; CAH92850.1; -; mRNA.
DR RefSeq; NP_001126665.1; NM_001133193.1.
DR AlphaFoldDB; Q5R5W6; -.
DR BMRB; Q5R5W6; -.
DR SMR; Q5R5W6; -.
DR STRING; 9601.ENSPPYP00000008568; -.
DR GeneID; 100173665; -.
DR KEGG; pon:100173665; -.
DR CTD; 1012; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q5R5W6; -.
DR OrthoDB; 215774at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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_0000003799"
FT CHAIN 139..690
FT /note="Cadherin-13"
FT /id="PRO_0000003800"
FT PROPEP 691..713
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003801"
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..690
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT LIPID 690
FT /note="GPI-anchor amidated asparagine"
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; 78266 MW; A47C72F82AA617E3 CRC64;
MQPRTPLVLC VLLSQVLLLT SAEDLDCIPG FQQKVFHINQ PAEFIEDQSI LNLTFSDCKG
NDKLRYEVSS PYFKVNSDGG LVALRNITAV GKTLFVHART PHAEDMAELV IVGGKDIQGS
LQDIFKFART SPVPRQKRSI VVSPILIPEN QRQPFPRDVG KVVDSDRPER SKFRLTGKGV
DQEPKGIFRI NENTGSVSVT RTLDREVIAV YQLFVETTDV NGKTLEGPVP LEVIVIDQND
NRPIFREGPY IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY
IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT IMIDDKNDHS
PKFTKKEFQA TVEEGAVGVI VNLTVEDKDD PTTGAWRAAY TIINGNPGQS FEIHTNPQTN
EGMLSVVKPL GYEISAFHTL LIKVENEDPL VPDVSYGPSS TATVHITVLD VNEGPVFYPD
PMMVTRQENI SVGSVLLTVN ATDPDSLQHQ TIRYSVYKDP AGWLNINPIN GTVDTTAVLD
RESPFVDNSV YTALFLAIDS GNPPATGTGT LLITLEDVND NAPFIYPTVA EVCDDAKNLS
VVILGASDKD LHPNTDPFKF EIHKQAVPDK VWKISKINNT HALVSLLQNL NKANYNLPIM
VTDSGKPPMT NITDLRVQVC SCRNSKVDSN AVGALRFSLP SLLLLSLFSL ACL
