CAD13_CHICK
ID CAD13_CHICK Reviewed; 712 AA.
AC P33150; Q91353;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cadherin-13;
DE AltName: Full=Truncated cadherin;
DE Short=T-cad;
DE Short=T-cadherin;
DE Flags: Precursor;
GN Name=CDH13;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Embryonic brain;
RX PubMed=1654948; DOI=10.1016/0896-6273(91)90291-7;
RA Ranscht B., Dours-Zimmermann M.T.;
RT "T-cadherin, a novel cadherin cell adhesion molecule in the nervous system
RT lacks the conserved cytoplasmic region.";
RL Neuron 7:391-402(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8315665; DOI=10.1002/jnr.490340610;
RA Sacristan M.P., Vestal D.J., Dours-Zimmermann M.T., Ranscht B.;
RT "T-cadherin 2: molecular characterization, function in cell adhesion, and
RT coexpression with T-cadherin and N-cadherin.";
RL J. Neurosci. Res. 34:664-680(1993).
RN [3]
RP CHARACTERIZATION.
RX PubMed=1400585; DOI=10.1083/jcb.119.2.451;
RA Vestal D.J., Ranscht B.;
RT "Glycosyl phosphatidylinositol-anchored T-cadherin mediates calcium-
RT dependent, homophilic cell adhesion.";
RL J. Cell Biol. 119:451-461(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 140-355, AND SUBUNIT.
RX PubMed=20190755; DOI=10.1038/nsmb.1781;
RA Ciatto C., Bahna F., Zampieri N., VanSteenhouse H.C., Katsamba P.S.,
RA Ahlsen G., Harrison O.J., Brasch J., Jin X., Posy S., Vendome J.,
RA Ranscht B., Jessell T.M., Honig B., Shapiro L.;
RT "T-cadherin structures reveal a novel adhesive binding mechanism.";
RL Nat. Struct. Mol. Biol. 17:339-347(2010).
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.
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:0000269|PubMed:20190755}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=T-Cad1;
CC IsoId=P33150-1; Sequence=Displayed;
CC Name=2; Synonyms=T-Cad2;
CC IsoId=P33150-2; Sequence=VSP_000642;
CC -!- TISSUE SPECIFICITY: Neural tissues. Also found in muscles; kidney and
CC retina.
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; M81779; AAA49079.1; -; mRNA.
DR EMBL; S62757; AAB27242.1; -; mRNA.
DR PIR; I51206; I51206.
DR PIR; JU0279; IJMSCT.
DR RefSeq; NP_001001760.1; NM_001001760.1. [P33150-2]
DR RefSeq; XP_015148010.1; XM_015292524.1. [P33150-1]
DR PDB; 3K5S; X-ray; 2.90 A; A/B=140-355.
DR PDB; 3K6I; X-ray; 1.13 A; A=140-237.
DR PDBsum; 3K5S; -.
DR PDBsum; 3K6I; -.
DR AlphaFoldDB; P33150; -.
DR SMR; P33150; -.
DR DIP; DIP-58996N; -.
DR STRING; 9031.ENSGALP00000008794; -.
DR PaxDb; P33150; -.
DR Ensembl; ENSGALT00000008808; ENSGALP00000008794; ENSGALG00000005483. [P33150-1]
DR GeneID; 414849; -.
DR KEGG; gga:414849; -.
DR CTD; 1012; -.
DR VEuPathDB; HostDB:geneid_414849; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155218; -.
DR InParanoid; P33150; -.
DR OMA; VCTCKKS; -.
DR OrthoDB; 215774at2759; -.
DR PhylomeDB; P33150; -.
DR Reactome; R-GGA-418990; Adherens junctions interactions.
DR EvolutionaryTrace; P33150; -.
DR PRO; PR:P33150; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000005483; Expressed in colon and 12 other tissues.
DR ExpressionAtlas; P33150; baseline and differential.
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:0009986; C:cell surface; IDA:AgBase.
DR GO; GO:0099512; C:supramolecular fiber; IDA:AgBase.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
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_0000003802"
FT CHAIN 139..693
FT /note="Cadherin-13"
FT /id="PRO_0000003803"
FT PROPEP 694..712
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003804"
FT DOMAIN 143..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 586..680
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT LIPID 693
FT /note="GPI-anchor amidated aspartate"
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 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 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 712
FT /note="L -> KSFPYV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8315665"
FT /id="VSP_000642"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:3K6I"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3K6I"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:3K6I"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 224..236
FT /evidence="ECO:0007829|PDB:3K6I"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:3K5S"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:3K5S"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:3K5S"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:3K5S"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3K5S"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:3K5S"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3K5S"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:3K5S"
FT STRAND 319..335
FT /evidence="ECO:0007829|PDB:3K5S"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3K5S"
FT STRAND 344..354
FT /evidence="ECO:0007829|PDB:3K5S"
SQ SEQUENCE 712 AA; 78381 MW; 572F5576E0D231B1 CRC64;
MQHKTQLTLS FLLSQVLLLA CAEDLECTPG FQQKVFYIEQ PFEFTEDQPI LNLVFDDCKG
NNKLNFEVSN PDFKVEHDGS LVALKNVSEA GRALFVHARS EHAEDMAEIL IVGADEKHDA
LKEIFKIEGN LGIPRQKRAI LATPILIPEN QRPPFPRSVG KVIRSEGTEG AKFRLSGKGV
DQDPKGIFRI NEISGDVSVT RPLDREAIAN YELEVEVTDL SGKIIDGPVR LDISVIDQND
NRPMFKEGPY VGHVMEGSPT GTTVMRMTAF DADDPSTDNA LLRYNILKQT PTKPSPNMFY
IDPEKGDIVT VVSPVLLDRE TMETPKYELV IEAKDMGGHD VGLTGTATAT ILIDDKNDHP
PEFTKKEFQA TVKEGVTGVI VNLTVGDRDD PATGAWRAVY TIINGNPGQS FEIHTNPQTN
EGMLSVVKPL DYEISAFHTL LIKVENEDPL IPDIAYGPSS TATVQITVED VNEGPVFHPN
PMTVTKQENI PIGSIVLTVN ATDPDTLQHQ TIRYSVYKDP ASWLEINPTN GTVATTAVLD
RESPHVQDNK YTALFLAIDS GNPPATGTGT LHITLEDVND NVPSLYPTLA KVCDDAKDLR
VVVLGASDKD LHPNTDPFKF ELSKQSGPEK LWRINKLNNT HAQVVLLQNL KKANYNIPIS
VTDSGKPPLT NNTELKLQVC SCKKSRMDCS ASDALHISMT LILLSLFSLF CL
