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Protein

Cadherin-13

Gene

CDH13

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May act as a negative regulator of neural cell growth.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-13
Alternative name(s):
Truncated cadherin
Short name:
T-cad
Short name:
T-cadherin
Gene namesi
Name:CDH13
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 138116By similarityPRO_0000003802Add
BLAST
Chaini139 – 693555Cadherin-13PRO_0000003803Add
BLAST
Propeptidei694 – 71219Removed in mature formSequence analysisPRO_0000003804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence analysis
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence analysis
Glycosylationi500 – 5001N-linked (GlcNAc...)Sequence analysis
Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence analysis
Glycosylationi638 – 6381N-linked (GlcNAc...)Sequence analysis
Glycosylationi671 – 6711N-linked (GlcNAc...)Sequence analysis
Lipidationi693 – 6931GPI-anchor amidated aspartateSequence analysis

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP33150.

Expressioni

Tissue specificityi

Neural tissues. Also found in muscles; kidney and retina.

Interactioni

Subunit structurei

By contrast to classical cadherins, homodimerization in trans is not mediated by cadherin EC1 domain strand-swapping, but instead through a homophilic adhesive interface which joins two elongated EC1-EC2 domains through a region near their Ca2+-binding sites to form a tetrahedral, X-like shape.1 Publication

Protein-protein interaction databases

DIPiDIP-58996N.
STRINGi9031.ENSGALP00000038306.

Structurei

Secondary structure

1
712
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi145 – 1484Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi169 – 17810Combined sources
Turni179 – 1813Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi187 – 1904Combined sources
Turni192 – 1943Combined sources
Beta strandi196 – 1994Combined sources
Turni205 – 2073Combined sources
Beta strandi210 – 21910Combined sources
Beta strandi224 – 23613Combined sources
Beta strandi250 – 2578Combined sources
Beta strandi263 – 2664Combined sources
Beta strandi277 – 2804Combined sources
Beta strandi283 – 2908Combined sources
Beta strandi299 – 3013Combined sources
Turni303 – 3053Combined sources
Beta strandi307 – 3104Combined sources
Beta strandi314 – 3174Combined sources
Beta strandi319 – 33517Combined sources
Helixi336 – 3383Combined sources
Beta strandi344 – 35411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K5SX-ray2.90A/B140-355[»]
3K6IX-ray1.13A140-237[»]
ProteinModelPortaliP33150.
SMRiP33150. Positions 139-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33150.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 245103Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini246 – 363118Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 477114Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini478 – 585108Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini586 – 68095Cadherin 5PROSITE-ProRule annotationAdd
BLAST

Domaini

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.By similarity

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP33150.
KOiK06808.
PhylomeDBiP33150.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR014868. Cadherin_pro_dom.
IPR033216. CDH13.
[Graphical view]
PANTHERiPTHR24027:SF80. PTHR24027:SF80. 1 hit.
PfamiPF00028. Cadherin. 5 hits.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P33150-1) [UniParc]FASTAAdd to basket

Also known as: T-Cad1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQHKTQLTLS FLLSQVLLLA CAEDLECTPG FQQKVFYIEQ PFEFTEDQPI
60 70 80 90 100
LNLVFDDCKG NNKLNFEVSN PDFKVEHDGS LVALKNVSEA GRALFVHARS
110 120 130 140 150
EHAEDMAEIL IVGADEKHDA LKEIFKIEGN LGIPRQKRAI LATPILIPEN
160 170 180 190 200
QRPPFPRSVG KVIRSEGTEG AKFRLSGKGV DQDPKGIFRI NEISGDVSVT
210 220 230 240 250
RPLDREAIAN YELEVEVTDL SGKIIDGPVR LDISVIDQND NRPMFKEGPY
260 270 280 290 300
VGHVMEGSPT GTTVMRMTAF DADDPSTDNA LLRYNILKQT PTKPSPNMFY
310 320 330 340 350
IDPEKGDIVT VVSPVLLDRE TMETPKYELV IEAKDMGGHD VGLTGTATAT
360 370 380 390 400
ILIDDKNDHP PEFTKKEFQA TVKEGVTGVI VNLTVGDRDD PATGAWRAVY
410 420 430 440 450
TIINGNPGQS FEIHTNPQTN EGMLSVVKPL DYEISAFHTL LIKVENEDPL
460 470 480 490 500
IPDIAYGPSS TATVQITVED VNEGPVFHPN PMTVTKQENI PIGSIVLTVN
510 520 530 540 550
ATDPDTLQHQ TIRYSVYKDP ASWLEINPTN GTVATTAVLD RESPHVQDNK
560 570 580 590 600
YTALFLAIDS GNPPATGTGT LHITLEDVND NVPSLYPTLA KVCDDAKDLR
610 620 630 640 650
VVVLGASDKD LHPNTDPFKF ELSKQSGPEK LWRINKLNNT HAQVVLLQNL
660 670 680 690 700
KKANYNIPIS VTDSGKPPLT NNTELKLQVC SCKKSRMDCS ASDALHISMT
710
LILLSLFSLF CL
Length:712
Mass (Da):78,381
Last modified:October 1, 1993 - v1
Checksum:i572F5576E0D231B1
GO
Isoform 2 (identifier: P33150-2) [UniParc]FASTAAdd to basket

Also known as: T-Cad2

The sequence of this isoform differs from the canonical sequence as follows:
     712-712: L → KSFPYV

Show »
Length:717
Mass (Da):78,990
Checksum:i36F9EB2591333F55
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei712 – 7121L → KSFPYV in isoform 2. 1 PublicationVSP_000642

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81779 mRNA. Translation: AAA49079.1.
S62757 mRNA. Translation: AAB27242.1.
PIRiI51206.
JU0279. IJMSCT.
RefSeqiNP_001001760.1. NM_001001760.1. [P33150-2]
XP_015148010.1. XM_015292524.1. [P33150-1]
UniGeneiGga.24273.

Genome annotation databases

GeneIDi414849.
KEGGigga:414849.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81779 mRNA. Translation: AAA49079.1.
S62757 mRNA. Translation: AAB27242.1.
PIRiI51206.
JU0279. IJMSCT.
RefSeqiNP_001001760.1. NM_001001760.1. [P33150-2]
XP_015148010.1. XM_015292524.1. [P33150-1]
UniGeneiGga.24273.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K5SX-ray2.90A/B140-355[»]
3K6IX-ray1.13A140-237[»]
ProteinModelPortaliP33150.
SMRiP33150. Positions 139-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58996N.
STRINGi9031.ENSGALP00000038306.

Proteomic databases

PaxDbiP33150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi414849.
KEGGigga:414849.

Organism-specific databases

CTDi1012.

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP33150.
KOiK06808.
PhylomeDBiP33150.

Miscellaneous databases

EvolutionaryTraceiP33150.
PROiP33150.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR014868. Cadherin_pro_dom.
IPR033216. CDH13.
[Graphical view]
PANTHERiPTHR24027:SF80. PTHR24027:SF80. 1 hit.
PfamiPF00028. Cadherin. 5 hits.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region."
    Ranscht B., Dours-Zimmermann M.T.
    Neuron 7:391-402(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Embryonic brain.
  2. "T-cadherin 2: molecular characterization, function in cell adhesion, and coexpression with T-cadherin and N-cadherin."
    Sacristan M.P., Vestal D.J., Dours-Zimmermann M.T., Ranscht B.
    J. Neurosci. Res. 34:664-680(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Glycosyl phosphatidylinositol-anchored T-cadherin mediates calcium-dependent, homophilic cell adhesion."
    Vestal D.J., Ranscht B.
    J. Cell Biol. 119:451-461(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 140-355, SUBUNIT.

Entry informationi

Entry nameiCAD13_CHICK
AccessioniPrimary (citable) accession number: P33150
Secondary accession number(s): Q91353
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.