ID CAD10_MOUSE Reviewed; 788 AA. AC P70408; Q3UUB3; Q80WS7; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 08-MAY-2019, entry version 134. DE RecName: Full=Cadherin-10; DE AltName: Full=T2-cadherin; DE Flags: Precursor; GN Name=Cdh10; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 516-788, AND DEVELOPMENTAL STAGE. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=8879495; DOI=10.1095/biolreprod55.4.822; RA Munro S.B., Blaschuk O.W.; RT "A comprehensive survey of the cadherins expressed in the testes of RT fetal, immature, and adult mice utilizing the polymerase chain RT reaction."; RL Biol. Reprod. 55:822-827(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 732-771. RC STRAIN=CBA/J; TISSUE=Thymocyte; RX PubMed=8620560; DOI=10.1006/cimm.1996.0123; RA Munro S.B., Duclos A.J., Jackson A.R., Baines M.G., Blaschuk O.W.; RT "Characterization of cadherins expressed by murine thymocytes."; RL Cell. Immunol. 169:309-312(1996). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. CC They preferentially interact with themselves in a homophilic CC manner in connecting cells; cadherins may thus contribute to the CC sorting of heterogeneous cell types. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC type I membrane protein {ECO:0000305}. CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of testicular CC development with highest levels found in fetal gonad. CC {ECO:0000269|PubMed:8879495}. CC -!- DOMAIN: Three calcium ions are usually bound at the interface of CC each cadherin domain and rigidify the connections, imparting a CC strong curvature to the full-length ectodomain. {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK138606; BAE23714.1; -; mRNA. DR EMBL; BC052056; AAH52056.1; -; mRNA. DR EMBL; BC062962; AAH62962.1; -; mRNA. DR EMBL; U69137; AAB87708.1; -; mRNA. DR CCDS; CCDS37047.1; -. DR RefSeq; NP_001303687.1; NM_001316758.1. DR RefSeq; NP_033995.1; NM_009865.3. DR PDB; 6CG6; X-ray; 2.71 A; A=55-261. DR PDBsum; 6CG6; -. DR SMR; P70408; -. DR BioGrid; 236359; 4. DR IntAct; P70408; 3. DR STRING; 10090.ENSMUSP00000042199; -. DR iPTMnet; P70408; -. DR PhosphoSitePlus; P70408; -. DR MaxQB; P70408; -. DR PaxDb; P70408; -. DR PeptideAtlas; P70408; -. DR PRIDE; P70408; -. DR Ensembl; ENSMUST00000040562; ENSMUSP00000042199; ENSMUSG00000022321. DR Ensembl; ENSMUST00000166873; ENSMUSP00000128782; ENSMUSG00000022321. DR GeneID; 320873; -. DR KEGG; mmu:320873; -. DR UCSC; uc007vik.1; mouse. DR CTD; 1008; -. DR MGI; MGI:107436; Cdh10. DR eggNOG; KOG3594; Eukaryota. DR eggNOG; ENOG410XQHI; LUCA. DR GeneTree; ENSGT00940000154187; -. DR HOGENOM; HOG000231252; -. DR InParanoid; P70408; -. DR KO; K06802; -. DR OMA; LWVCLPH; -. DR OrthoDB; 201053at2759; -. DR TreeFam; TF329887; -. DR Reactome; R-MMU-418990; Adherens junctions interactions. DR PRO; PR:P70408; -. DR Proteomes; UP000000589; Chromosome 15. DR Bgee; ENSMUSG00000022321; Expressed in 166 organ(s), highest expression level in retina. DR ExpressionAtlas; P70408; baseline and differential. DR Genevisible; P70408; MM. DR GO; GO:0016342; C:catenin complex; IBA:GO_Central. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005913; C:cell-cell adherens junction; IBA:GO_Central. DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI. DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. 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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central. DR Gene3D; 4.10.900.10; -; 1. DR InterPro; IPR039808; Cadherin. DR InterPro; IPR002126; Cadherin-like_dom. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR020894; Cadherin_CS. DR InterPro; IPR000233; Cadherin_cytoplasmic-dom. DR InterPro; IPR027397; Catenin_binding_dom_sf. DR PANTHER; PTHR24027; PTHR24027; 1. DR Pfam; PF00028; Cadherin; 5. DR Pfam; PF01049; Cadherin_C; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 5. DR SUPFAM; SSF49313; SSF49313; 5. 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; Complete proteome; Glycoprotein; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 22 {ECO:0000255}. FT PROPEP 23 54 {ECO:0000255}. FT /FTId=PRO_0000269662. FT CHAIN 55 788 Cadherin-10. FT /FTId=PRO_0000126646. FT TOPO_DOM 23 613 Extracellular. {ECO:0000255}. FT TRANSMEM 614 634 Helical. {ECO:0000255}. FT TOPO_DOM 635 788 Cytoplasmic. {ECO:0000255}. FT DOMAIN 56 160 Cadherin 1. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 161 269 Cadherin 2. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 270 384 Cadherin 3. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 385 489 Cadherin 4. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 489 603 Cadherin 5. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT MOD_RES 784 784 Phosphoserine. FT {ECO:0000244|PubMed:16452087, FT ECO:0000244|PubMed:21183079}. FT CARBOHYD 256 256 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 456 456 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 534 534 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CONFLICT 142 142 P -> S (in Ref. 2; AAH52056/AAH62962). FT {ECO:0000305}. FT CONFLICT 518 525 PLGGQKFF -> VDRRSFS (in Ref. 3; FT AAB87708). {ECO:0000305}. FT CONFLICT 549 549 T -> A (in Ref. 3; AAB87708). FT {ECO:0000305}. FT CONFLICT 607 610 AGLS -> WPH (in Ref. 3; AAB87708). FT {ECO:0000305}. FT CONFLICT 635 639 Missing (in Ref. 3; AAB87708). FT {ECO:0000305}. FT CONFLICT 699 699 Missing (in Ref. 3; AAB87708). FT {ECO:0000305}. FT CONFLICT 706 706 D -> G (in Ref. 3; AAB87708). FT {ECO:0000305}. FT CONFLICT 773 773 N -> K (in Ref. 3; AAB87708). FT {ECO:0000305}. FT CONFLICT 788 788 A -> S (in Ref. 3; AAB87708). FT {ECO:0000305}. FT STRAND 60 66 {ECO:0000244|PDB:6CG6}. FT STRAND 73 77 {ECO:0000244|PDB:6CG6}. FT STRAND 85 87 {ECO:0000244|PDB:6CG6}. FT STRAND 89 95 {ECO:0000244|PDB:6CG6}. FT TURN 99 101 {ECO:0000244|PDB:6CG6}. FT STRAND 102 104 {ECO:0000244|PDB:6CG6}. FT TURN 106 108 {ECO:0000244|PDB:6CG6}. FT STRAND 110 113 {ECO:0000244|PDB:6CG6}. FT TURN 119 121 {ECO:0000244|PDB:6CG6}. FT STRAND 124 133 {ECO:0000244|PDB:6CG6}. FT TURN 134 136 {ECO:0000244|PDB:6CG6}. FT STRAND 139 141 {ECO:0000244|PDB:6CG6}. FT STRAND 144 151 {ECO:0000244|PDB:6CG6}. FT STRAND 163 170 {ECO:0000244|PDB:6CG6}. FT STRAND 178 181 {ECO:0000244|PDB:6CG6}. FT STRAND 199 205 {ECO:0000244|PDB:6CG6}. FT TURN 206 208 {ECO:0000244|PDB:6CG6}. FT STRAND 209 211 {ECO:0000244|PDB:6CG6}. FT TURN 213 215 {ECO:0000244|PDB:6CG6}. FT STRAND 217 220 {ECO:0000244|PDB:6CG6}. FT TURN 227 229 {ECO:0000244|PDB:6CG6}. FT STRAND 232 241 {ECO:0000244|PDB:6CG6}. FT TURN 242 244 {ECO:0000244|PDB:6CG6}. FT STRAND 250 260 {ECO:0000244|PDB:6CG6}. SQ SEQUENCE 788 AA; 88312 MW; 4066D21DBB038AE1 CRC64; MTIYQFLRLF VLWACLPHFC CPELTFRRTP GIQQMTAESR APRSDGKILH RQKRGWMWNQ FFLLEEYTGS DYQYVGKLHS DQDKGDGSLK YILSGDGAGT LFIIDEKTGD IHATRRIDRE EKAFYTLRAQ AINRRTLRPV EPESEFVIKI HDINDNEPTF PEEIYTASVP EMSVVGTSVV QVTATDADDP SYGNSARVIY SILQGQPYFS VEPETGIIRT ALPNMNRENK EQYQVVIQAK DMGGQMGGLS GTTTVNITLT DVNDNPPRFP QNTIHLRVLE SSPVGTAVGS VKATDADTGK NAEVDYRIID GDGTDMFDII TEKDTQEGII TVKKPLDYEN RRLYTLKVEA ENTHVDPRFY YLGPFKDTTI VKISIEDVDE PPVFSRSSYL FEVHEDIEVG TIIGTVMARD PDSTSSPIRF TLDRHTDLDR IFNIHSGNGS LYTSKPLDRE LSQWHNLTVI AAEINNPKET TRVSVFVRIL DVNDNAPQFA VFYDTFVCEN ARPGQLIQTI SAVDKDDPLG GQKFFFSLAA VNPNFTVQDN EDNTARILTR KNGFNRHEIS TYLLPVVISD NDYPIQSSTG TLTIRVCACD SQGNMQSCSA EALLLPAGLS TGALIAILLC IIILLVIVVL FAALKRQRKK EPLILSKEDI RDNIVSYNDE GGGEEDTQAF DIGTLRNPAA IEEKKLRRDI IPETLFIPRR TPTAPDNTDV RDFINERLKE HDLDPTAPPY DSLATYAYEG NDSVAESLSS LESGTTEGDQ NYDYLREWGP RFNKLAEMYG GGESDKDA //