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Protein

Cadherin-13

Gene

Cdh13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-418990 Adherens junctions interactions

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-13
Alternative name(s):
Heart cadherin
Short name:
H-cadherin
Truncated cadherin
Short name:
T-cad
Short name:
T-cadherin
Gene namesi
Name:Cdh13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:99551 Cdh13

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi152R → E: Strongly inhibits dimerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000000379623 – 138By similarityAdd BLAST116
ChainiPRO_0000003797139 – 693Cadherin-13Add BLAST555
PropeptideiPRO_0000003798694 – 714Removed in mature formSequence analysisAdd BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi382N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi489N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi500N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi530N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi598N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi638N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi671N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi693GPI-anchor amidated glycineSequence analysis1

Keywords - PTMi

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

Proteomic databases

MaxQBiQ9WTR5
PaxDbiQ9WTR5
PeptideAtlasiQ9WTR5
PRIDEiQ9WTR5

PTM databases

iPTMnetiQ9WTR5
PhosphoSitePlusiQ9WTR5

Expressioni

Gene expression databases

BgeeiENSMUSG00000031841 Expressed in 269 organ(s), highest expression level in heart
CleanExiMM_CDH13
GenevisibleiQ9WTR5 MM

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198633, 2 interactors
IntActiQ9WTR5, 2 interactors
STRINGi10090.ENSMUSP00000113527

Structurei

Secondary structure

1714
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9WTR5
SMRiQ9WTR5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WTR5

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini143 – 245Cadherin 1PROSITE-ProRule annotationAdd BLAST103
Domaini246 – 363Cadherin 2PROSITE-ProRule annotationAdd BLAST118
Domaini364 – 477Cadherin 3PROSITE-ProRule annotationAdd BLAST114
Domaini478 – 585Cadherin 4PROSITE-ProRule annotationAdd BLAST108
Domaini586 – 680Cadherin 5PROSITE-ProRule annotationAdd BLAST95

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
GeneTreeiENSGT00760000118906
HOGENOMiHOG000231254
HOVERGENiHBG106438
InParanoidiQ9WTR5
KOiK06808
OMAiKANYHLP
OrthoDBiEOG091G02OG
TreeFamiTF316817

Family and domain databases

InterProiView protein in InterPro
IPR002126 Cadherin
IPR015919 Cadherin-like
IPR020894 Cadherin_CS
IPR014868 Cadherin_pro_dom
IPR033216 CDH13
PANTHERiPTHR24027:SF80 PTHR24027:SF80, 1 hit
PfamiView protein in Pfam
PF00028 Cadherin, 5 hits
PF08758 Cadherin_pro, 1 hit
PRINTSiPR00205 CADHERIN
SMARTiView protein in SMART
SM00112 CA, 5 hits
SM01055 Cadherin_pro, 1 hit
SUPFAMiSSF49313 SSF49313, 6 hits
PROSITEiView protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 5 hits

Sequencei

Sequence statusi: Complete.

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

Q9WTR5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQPRTPLTLC VLLSQVLLVT SADDLECTPG FQRKVLHIHQ PAEFIEDQPV
60 70 80 90 100
LNLTFNDCKG NEKLHYEVSS PHFKVNSDGT LVALRNITAV GRTLFVHART
110 120 130 140 150
PHAEDMAELV IVGGKDIQGS LQDIFKFART SPVPRQKRSI VVSPILIPEN
160 170 180 190 200
QRQPFPRDVG KVVDSDRPEG SKFRLTGKGV DQDPKGTFRI NENTGSVSVT
210 220 230 240 250
RTLDRETIAT YQLYVETTDA SGKTLEGPVP LEVIVIDQND NRPIFREGPY
260 270 280 290 300
IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY
310 320 330 340 350
IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT
360 370 380 390 400
IVIDDKNDHS PKFTKKEFQA TVEEGAVGVI VNLTVEDKDD PTTGAWRAAY
410 420 430 440 450
TIINGNPGQS FEIHTNPQTN EGMLSVVKPL DYEISAFHTL LIKVENEDPL
460 470 480 490 500
VPDVSYGPSS TATVHITVLD VNEGPVFYPD PMMVTKQENI SVGSVLLTVN
510 520 530 540 550
ATDPDSLQHQ TIRYSIYKDP AGWLSINPIN GTVDTTAVLD RESPFVHNSV
560 570 580 590 600
YTALFLAIDS GNPPATGTGT LLITLEDIND NAPVIYPTVA EVCDDARNLS
610 620 630 640 650
VVILGASDKD LHPNTDPFKF EIHKQTVPDK VWKISKINNT HALVSLLQNL
660 670 680 690 700
NKANYNLPIM VTDSGKPPMT NITDLRVQVC SCKNSKVDCN GAGALHLSLS
710
LLLLFSLLSL LSGL
Length:714
Mass (Da):78,186
Last modified:July 27, 2011 - v2
Checksum:iD6EE6573B2B23204
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti282L → W in BAA76677 (PubMed:10737605).Curated1
Sequence conflicti371T → R in BAA76677 (PubMed:10737605).Curated1
Sequence conflicti676R → K in BAA76677 (PubMed:10737605).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022100 mRNA Translation: BAA76677.1
AK039438 mRNA Translation: BAC30347.1
AK048724 mRNA Translation: BAC33435.1
AK134649 mRNA Translation: BAE22225.1
CH466525 Genomic DNA Translation: EDL11590.1
CCDSiCCDS52682.1
RefSeqiNP_062681.2, NM_019707.5
UniGeneiMm.334841

Genome annotation databases

EnsembliENSMUST00000117160; ENSMUSP00000113527; ENSMUSG00000031841
GeneIDi12554
KEGGimmu:12554
UCSCiuc009npl.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022100 mRNA Translation: BAA76677.1
AK039438 mRNA Translation: BAC30347.1
AK048724 mRNA Translation: BAC33435.1
AK134649 mRNA Translation: BAE22225.1
CH466525 Genomic DNA Translation: EDL11590.1
CCDSiCCDS52682.1
RefSeqiNP_062681.2, NM_019707.5
UniGeneiMm.334841

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K5RX-ray2.00A/B140-355[»]
3K6FX-ray1.81A/B140-237[»]
ProteinModelPortaliQ9WTR5
SMRiQ9WTR5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198633, 2 interactors
IntActiQ9WTR5, 2 interactors
STRINGi10090.ENSMUSP00000113527

PTM databases

iPTMnetiQ9WTR5
PhosphoSitePlusiQ9WTR5

Proteomic databases

MaxQBiQ9WTR5
PaxDbiQ9WTR5
PeptideAtlasiQ9WTR5
PRIDEiQ9WTR5

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000117160; ENSMUSP00000113527; ENSMUSG00000031841
GeneIDi12554
KEGGimmu:12554
UCSCiuc009npl.1 mouse

Organism-specific databases

CTDi1012
MGIiMGI:99551 Cdh13

Phylogenomic databases

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
GeneTreeiENSGT00760000118906
HOGENOMiHOG000231254
HOVERGENiHBG106438
InParanoidiQ9WTR5
KOiK06808
OMAiKANYHLP
OrthoDBiEOG091G02OG
TreeFamiTF316817

Enzyme and pathway databases

ReactomeiR-MMU-418990 Adherens junctions interactions

Miscellaneous databases

EvolutionaryTraceiQ9WTR5
PROiPR:Q9WTR5
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031841 Expressed in 269 organ(s), highest expression level in heart
CleanExiMM_CDH13
GenevisibleiQ9WTR5 MM

Family and domain databases

InterProiView protein in InterPro
IPR002126 Cadherin
IPR015919 Cadherin-like
IPR020894 Cadherin_CS
IPR014868 Cadherin_pro_dom
IPR033216 CDH13
PANTHERiPTHR24027:SF80 PTHR24027:SF80, 1 hit
PfamiView protein in Pfam
PF00028 Cadherin, 5 hits
PF08758 Cadherin_pro, 1 hit
PRINTSiPR00205 CADHERIN
SMARTiView protein in SMART
SM00112 CA, 5 hits
SM01055 Cadherin_pro, 1 hit
SUPFAMiSSF49313 SSF49313, 6 hits
PROSITEiView protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 5 hits
ProtoNetiSearch...

Entry informationi

Entry nameiCAD13_MOUSE
AccessioniPrimary (citable) accession number: Q9WTR5
Secondary accession number(s): Q8BG11
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: September 12, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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