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 29-SEP-2021, entry version 148. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., 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 [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 project: RT 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 fetal, RT immature, and adult mice utilizing the polymerase chain 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 BY RP 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., 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 BY RP 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 expression."; RL Cell 143:1174-1189(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. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of testicular development CC with highest levels found in fetal gonad. {ECO:0000269|PubMed:8879495}. 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}. 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; 5. DR IntAct; P70408; 3. DR STRING; 10090.ENSMUSP00000042199; -. DR GlyConnect; 2163; 8 N-Linked glycans (2 sites). DR GlyGen; P70408; 4 sites, 8 N-linked glycans (2 sites). DR iPTMnet; P70408; -. DR PhosphoSitePlus; P70408; -. DR MaxQB; P70408; -. DR PaxDb; P70408; -. DR PeptideAtlas; P70408; -. DR PRIDE; P70408; -. DR ProteomicsDB; 265492; -. DR Antibodypedia; 2223; 201 antibodies. 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 VEuPathDB; HostDB:ENSMUSG00000022321; -. DR eggNOG; KOG3594; Eukaryota. DR GeneTree; ENSGT00940000154187; -. DR HOGENOM; CLU_005284_3_1_1; -. DR InParanoid; P70408; -. DR OMA; RNGFSRH; -. DR OrthoDB; 201053at2759; -. DR PhylomeDB; P70408; -. DR TreeFam; TF329887; -. DR Reactome; R-MMU-418990; Adherens junctions interactions. DR BioGRID-ORCS; 320873; 0 hits in 62 CRISPR screens. DR PRO; PR:P70408; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; P70408; protein. DR Bgee; ENSMUSG00000022321; Expressed in retina and 196 other tissues. DR ExpressionAtlas; P70408; baseline and differential. DR Genevisible; P70408; MM. DR GO; GO:0005912; C:adherens junction; IBA:GO_Central. DR GO; GO:0016342; C:catenin complex; 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:0045296; F:cadherin binding; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; 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:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; 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; IEA:InterPro. 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-bd_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; Glycoprotein; Membrane; Metal-binding; KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..54 FT /evidence="ECO:0000255" FT /id="PRO_0000269662" FT CHAIN 55..788 FT /note="Cadherin-10" FT /id="PRO_0000126646" FT TOPO_DOM 23..613 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 614..634 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 635..788 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 56..160 FT /note="Cadherin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 161..269 FT /note="Cadherin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 270..384 FT /note="Cadherin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 385..489 FT /note="Cadherin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 489..603 FT /note="Cadherin 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT MOD_RES 784 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT CARBOHYD 256 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 456 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 534 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 142 FT /note="P -> S (in Ref. 2; AAH52056/AAH62962)" FT /evidence="ECO:0000305" FT CONFLICT 518..525 FT /note="PLGGQKFF -> VDRRSFS (in Ref. 3; AAB87708)" FT /evidence="ECO:0000305" FT CONFLICT 549 FT /note="T -> A (in Ref. 3; AAB87708)" FT /evidence="ECO:0000305" FT CONFLICT 607..610 FT /note="AGLS -> WPH (in Ref. 3; AAB87708)" FT /evidence="ECO:0000305" FT CONFLICT 635..639 FT /note="Missing (in Ref. 3; AAB87708)" FT /evidence="ECO:0000305" FT CONFLICT 699 FT /note="Missing (in Ref. 3; AAB87708)" FT /evidence="ECO:0000305" FT CONFLICT 706 FT /note="D -> G (in Ref. 3; AAB87708)" FT /evidence="ECO:0000305" FT CONFLICT 773 FT /note="N -> K (in Ref. 3; AAB87708)" FT /evidence="ECO:0000305" FT CONFLICT 788 FT /note="A -> S (in Ref. 3; AAB87708)" FT /evidence="ECO:0000305" FT STRAND 60..66 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 73..77 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 89..95 FT /evidence="ECO:0007829|PDB:6CG6" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:6CG6" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:6CG6" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 124..133 FT /evidence="ECO:0007829|PDB:6CG6" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 144..151 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 163..170 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 199..205 FT /evidence="ECO:0007829|PDB:6CG6" FT TURN 206..208 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:6CG6" FT TURN 213..215 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 217..220 FT /evidence="ECO:0007829|PDB:6CG6" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 232..241 FT /evidence="ECO:0007829|PDB:6CG6" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:6CG6" FT STRAND 250..260 FT /evidence="ECO:0007829|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 //