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Protein

Cadherin-13

Gene

Cdh13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:99551. Cdh13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi152 – 1521R → E: Strongly inhibits dimerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 138116By similarityPRO_0000003796Add
BLAST
Chaini139 – 693555Cadherin-13PRO_0000003797Add
BLAST
Propeptidei694 – 71421Removed in mature formSequence analysisPRO_0000003798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence analysis
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence analysis
Glycosylationi500 – 5001N-linked (GlcNAc...)Sequence analysis
Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence analysis
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence analysis
Glycosylationi638 – 6381N-linked (GlcNAc...)Sequence analysis
Glycosylationi671 – 6711N-linked (GlcNAc...)Sequence analysis
Lipidationi693 – 6931GPI-anchor amidated glycineSequence analysis

Keywords - PTMi

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

Proteomic databases

MaxQBiQ9WTR5.
PaxDbiQ9WTR5.
PeptideAtlasiQ9WTR5.
PRIDEiQ9WTR5.

PTM databases

iPTMnetiQ9WTR5.
PhosphoSiteiQ9WTR5.

Expressioni

Gene expression databases

BgeeiQ9WTR5.
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

  • adiponectin binding Source: BHF-UCL
  • cadherin binding Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi198633. 2 interactions.
IntActiQ9WTR5. 1 interaction.
STRINGi10090.ENSMUSP00000113527.

Structurei

Secondary structure

1
714
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 strandi172 – 1787Combined sources
Turni179 – 1813Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi187 – 1904Combined sources
Turni192 – 1943Combined sources
Beta strandi196 – 1994Combined sources
Turni205 – 2073Combined sources
Beta strandi209 – 21810Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi224 – 23613Combined sources
Beta strandi249 – 2557Combined sources
Beta strandi263 – 2664Combined sources
Beta strandi272 – 2754Combined sources
Helixi277 – 2804Combined sources
Beta strandi282 – 29110Combined sources
Beta strandi298 – 3014Combined sources
Turni303 – 3053Combined sources
Beta strandi307 – 3104Combined sources
Helixi314 – 3163Combined sources
Helixi319 – 3213Combined sources
Beta strandi325 – 33511Combined sources
Turni339 – 3424Combined sources
Beta strandi344 – 35411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K5RX-ray2.00A/B140-355[»]
3K6FX-ray1.81A/B140-237[»]
ProteinModelPortaliQ9WTR5.
SMRiQ9WTR5. Positions 27-111, 140-680.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WTR5.

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.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiQ9WTR5.
KOiK06808.
OMAiTIATYQL.
OrthoDBiEOG7MH0XG.
TreeFamiTF316817.

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]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821L → W in BAA76677 (PubMed:10737605).Curated
Sequence conflicti371 – 3711T → R in BAA76677 (PubMed:10737605).Curated
Sequence conflicti676 – 6761R → K in BAA76677 (PubMed:10737605).Curated

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3K5RX-ray2.00A/B140-355[»]
3K6FX-ray1.81A/B140-237[»]
ProteinModelPortaliQ9WTR5.
SMRiQ9WTR5. Positions 27-111, 140-680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198633. 2 interactions.
IntActiQ9WTR5. 1 interaction.
STRINGi10090.ENSMUSP00000113527.

PTM databases

iPTMnetiQ9WTR5.
PhosphoSiteiQ9WTR5.

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.
OMAiTIATYQL.
OrthoDBiEOG7MH0XG.
TreeFamiTF316817.

Enzyme and pathway databases

ReactomeiR-MMU-418990. Adherens junctions interactions.

Miscellaneous databases

EvolutionaryTraceiQ9WTR5.
PROiQ9WTR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WTR5.
CleanExiMM_CDH13.
GenevisibleiQ9WTR5. MM.

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

« Hide 'large scale' publications
  1. "Expression of T-cadherin (CDH13, H-Cadherin) in human brain and its characteristics as a negative growth regulator of epidermal growth factor in neuroblastoma cells."
    Takeuchi T., Misaki A., Liang S.-B., Tachibana A., Hayashi N., Sonobe H., Ohtsuki Y.
    J. Neurochem. 74:1489-1497(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain and Heart.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Medulla oblongata and Spinal cord.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney and Lung.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 140-355, SUBUNIT, MUTAGENESIS OF ARG-152.

Entry informationi

Entry nameiCAD13_MOUSE
AccessioniPrimary (citable) accession number: Q9WTR5
Secondary accession number(s): Q8BG11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.