CAD13_MOUSE
ID CAD13_MOUSE Reviewed; 714 AA.
AC Q9WTR5; Q8BG11;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cadherin-13;
DE AltName: Full=Heart cadherin;
DE Short=H-cadherin;
DE AltName: Full=Truncated cadherin;
DE Short=T-cad;
DE Short=T-cadherin;
DE Flags: Precursor;
GN Name=Cdh13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain, and Heart;
RX PubMed=10737605; DOI=10.1046/j.1471-4159.2000.0741489.x;
RA Takeuchi T., Misaki A., Liang S.-B., Tachibana A., Hayashi N., Sonobe H.,
RA Ohtsuki Y.;
RT "Expression of T-cadherin (CDH13, H-Cadherin) in human brain and its
RT characteristics as a negative growth regulator of epidermal growth factor
RT in neuroblastoma cells.";
RL J. Neurochem. 74:1489-1497(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Medulla oblongata, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 140-355, SUBUNIT, AND MUTAGENESIS
RP OF ARG-152.
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 {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; AB022100; BAA76677.1; -; mRNA.
DR EMBL; AK039438; BAC30347.1; -; mRNA.
DR EMBL; AK048724; BAC33435.1; -; mRNA.
DR EMBL; AK134649; BAE22225.1; -; mRNA.
DR EMBL; CH466525; EDL11590.1; -; Genomic_DNA.
DR CCDS; CCDS52682.1; -.
DR RefSeq; NP_062681.2; NM_019707.5.
DR PDB; 3K5R; X-ray; 2.00 A; A/B=140-355.
DR PDB; 3K6F; X-ray; 1.81 A; A/B=140-237.
DR PDBsum; 3K5R; -.
DR PDBsum; 3K6F; -.
DR AlphaFoldDB; Q9WTR5; -.
DR SMR; Q9WTR5; -.
DR BioGRID; 198633; 2.
DR IntAct; Q9WTR5; 2.
DR STRING; 10090.ENSMUSP00000113527; -.
DR GlyConnect; 2166; 21 N-Linked glycans (4 sites).
DR GlyGen; Q9WTR5; 8 sites, 20 N-linked glycans (4 sites).
DR iPTMnet; Q9WTR5; -.
DR PhosphoSitePlus; Q9WTR5; -.
DR CPTAC; non-CPTAC-3381; -.
DR MaxQB; Q9WTR5; -.
DR PaxDb; Q9WTR5; -.
DR PeptideAtlas; Q9WTR5; -.
DR PRIDE; Q9WTR5; -.
DR ProteomicsDB; 265416; -.
DR Antibodypedia; 667; 644 antibodies from 42 providers.
DR DNASU; 12554; -.
DR Ensembl; ENSMUST00000117160; ENSMUSP00000113527; ENSMUSG00000031841.
DR GeneID; 12554; -.
DR KEGG; mmu:12554; -.
DR UCSC; uc009npl.1; mouse.
DR CTD; 1012; -.
DR MGI; MGI:99551; Cdh13.
DR VEuPathDB; HostDB:ENSMUSG00000031841; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155218; -.
DR HOGENOM; CLU_005284_5_1_1; -.
DR InParanoid; Q9WTR5; -.
DR OMA; VCTCKKS; -.
DR OrthoDB; 215774at2759; -.
DR PhylomeDB; Q9WTR5; -.
DR TreeFam; TF316817; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 12554; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Cdh13; mouse.
DR EvolutionaryTrace; Q9WTR5; -.
DR PRO; PR:Q9WTR5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9WTR5; protein.
DR Bgee; ENSMUSG00000031841; Expressed in cortical plate and 240 other tissues.
DR Genevisible; Q9WTR5; MM.
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:0005901; C:caveola; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0055100; F:adiponectin binding; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0071813; F:lipoprotein particle binding; ISO:MGI.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0043542; P:endothelial cell migration; ISO:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; ISO:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:MGI.
DR GO; GO:0051668; P:localization within membrane; ISO:MGI.
DR GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR GO; GO:0002040; P:sprouting angiogenesis; ISO:MGI.
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; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..138
FT /evidence="ECO:0000250"
FT /id="PRO_0000003796"
FT CHAIN 139..693
FT /note="Cadherin-13"
FT /id="PRO_0000003797"
FT PROPEP 694..714
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003798"
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 REGION 156..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 693
FT /note="GPI-anchor amidated glycine"
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"
FT MUTAGEN 152
FT /note="R->E: Strongly inhibits dimerization."
FT /evidence="ECO:0000269|PubMed:20190755"
FT CONFLICT 282
FT /note="L -> W (in Ref. 1; BAA76677)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="T -> R (in Ref. 1; BAA76677)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="R -> K (in Ref. 1; BAA76677)"
FT /evidence="ECO:0000305"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:3K6F"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3K6F"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:3K6F"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3K5R"
FT STRAND 224..236
FT /evidence="ECO:0007829|PDB:3K6F"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:3K5R"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:3K5R"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3K5R"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3K5R"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:3K5R"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:3K5R"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:3K5R"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3K5R"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:3K5R"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:3K5R"
FT STRAND 325..335
FT /evidence="ECO:0007829|PDB:3K5R"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:3K5R"
FT STRAND 344..354
FT /evidence="ECO:0007829|PDB:3K5R"
SQ SEQUENCE 714 AA; 78186 MW; D6EE6573B2B23204 CRC64;
MQPRTPLTLC VLLSQVLLVT SADDLECTPG FQRKVLHIHQ PAEFIEDQPV LNLTFNDCKG
NEKLHYEVSS PHFKVNSDGT LVALRNITAV GRTLFVHART PHAEDMAELV IVGGKDIQGS
LQDIFKFART SPVPRQKRSI VVSPILIPEN QRQPFPRDVG KVVDSDRPEG SKFRLTGKGV
DQDPKGTFRI NENTGSVSVT RTLDRETIAT YQLYVETTDA SGKTLEGPVP LEVIVIDQND
NRPIFREGPY IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY
IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT IVIDDKNDHS
PKFTKKEFQA TVEEGAVGVI VNLTVEDKDD PTTGAWRAAY TIINGNPGQS FEIHTNPQTN
EGMLSVVKPL DYEISAFHTL LIKVENEDPL VPDVSYGPSS TATVHITVLD VNEGPVFYPD
PMMVTKQENI SVGSVLLTVN ATDPDSLQHQ TIRYSIYKDP AGWLSINPIN GTVDTTAVLD
RESPFVHNSV YTALFLAIDS GNPPATGTGT LLITLEDIND NAPVIYPTVA EVCDDARNLS
VVILGASDKD LHPNTDPFKF EIHKQTVPDK VWKISKINNT HALVSLLQNL NKANYNLPIM
VTDSGKPPMT NITDLRVQVC SCKNSKVDCN GAGALHLSLS LLLLFSLLSL LSGL
