ID   Q8R490_RAT              Unreviewed;       714 AA.
AC   Q8R490; A6IZI0;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   SubName: Full=Cadherin 13 {ECO:0000313|EMBL:AAH85699.1, ECO:0000313|Ensembl:ENSRNOP00000068368.1};
DE   SubName: Full=T-cadherin {ECO:0000313|EMBL:AAM14607.1};
GN   Name=Cdh13 {ECO:0000313|EMBL:AAH85699.1,
GN   ECO:0000313|Ensembl:ENSRNOP00000068368.1, ECO:0000313|RGD:619745};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000068368.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|EMBL:AAM14607.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Heart {ECO:0000313|EMBL:AAM14607.1};
RA   Niermann T., Schmutz S.;
RT   "Cloning of rat T-cadherin.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAH85699.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAH85699.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000068368.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068368.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [4] {ECO:0007829|PubMed:24090084}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24090084;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
RN   [5] {ECO:0000313|Ensembl:ENSRNOP00000068368.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068368.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; BC085699; AAH85699.1; -; mRNA.
DR   EMBL; AF494095; AAM14607.1; -; mRNA.
DR   RefSeq; NP_620244.1; NM_138889.2.
DR   IntAct; Q8R490; 1.
DR   STRING; 10116.ENSRNOP00000068368; -.
DR   PaxDb; 10116-ENSRNOP00000068368; -.
DR   Ensembl; ENSRNOT00000077053.3; ENSRNOP00000068368.1; ENSRNOG00000014371.9.
DR   GeneID; 192248; -.
DR   KEGG; rno:192248; -.
DR   UCSC; RGD:619745; rat.
DR   AGR; RGD:619745; -.
DR   CTD; 1012; -.
DR   RGD; 619745; Cdh13.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000155218; -.
DR   OrthoDB; 5306553at2759; -.
DR   Reactome; R-RNO-418990; Adherens junctions interactions.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000014371; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0005901; C:caveola; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0055100; F:adiponectin binding; ISO:RGD.
DR   GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0071813; F:lipoprotein particle binding; ISO:RGD.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:RGD.
DR   GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; TAS:RGD.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR   GO; GO:0043616; P:keratinocyte proliferation; ISO:RGD.
DR   GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
DR   GO; GO:0051668; P:localization within membrane; ISO:RGD.
DR   GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; ISO:RGD.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:RGD.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR   GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR   GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:RGD.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0016601; P:Rac protein signal transduction; ISO:RGD.
DR   GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
DR   GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR   GO; GO:0002040; P:sprouting angiogenesis; ISO:RGD.
DR   CDD; cd11304; Cadherin_repeat; 5.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
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   PANTHER; PTHR24027:SF80; CADHERIN-13; 1.
DR   PANTHER; PTHR24027; CADHERIN-23; 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; Cadherin-like; 6.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..714
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015099339"
FT   DOMAIN          147..245
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          246..363
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          364..477
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          478..585
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          584..695
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          156..185
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"
SQ   SEQUENCE   714 AA;  78086 MW;  7E56142B8162F864 CRC64;
     MQPRTPLTLC VLLSQVLLVT SAGDLDCTPG FQQKVLHIHQ PAEFIEDQPV LNLTFSDCKG
     NKKLHYEVSS PYFKVNSDGT LVAVRNITAV GRTLFVHART PHAEDMAELV IVGGKDIQGS
     LQDIFKFART SPVPRQKRSI VVSPILIPEN QRQPFPRDVG KVVDSDRPEG SKFRLTGKGV
     DQDPKGTFRI NENTGSVSVT RTLDRETIAT YQLFVETTDA SGRTLEGPVP LEVIVIDQND
     NRPIFREGPY IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY
     IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT IVIDDKNDHS
     PKFTKKEFQA TVEEGAVGVI VNLTVEDKDD PATGAWRAAY TIINGNPGQS FEIHTNPQTN
     EGMLSVVKPL DYEISAFHTL LIKVENEDPL VPDVSYGPSS TATVHITVLD VNEGPVFYPD
     PMMVTKQENI SVGSVLLTVN ATDPDSLQHQ TIRYSVYKDP AGWLSINPIN GTVDTTAVLD
     RESPFVHNSV YTALFLAIDS GNPPATGTGT LMITLEDVND NAPVIYPTVA EVCDDARNLS
     VVILGASDKD LHPNTDPFKF EIHKQTVPDK VWKISKINNT HALVSLLQNL NKANYNLPIM
     VTDSGKPPMT NITDLRVQVC SCKNSKVDCN AAGTLHLSLS LLLLFSLLSL LSGL
//