CAD10_MOUSE
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 03-AUG-2022, entry version 151.
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}.
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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 AlphaFoldDB; P70408; -.
DR SMR; P70408; -.
DR BioGRID; 236359; 5.
DR IntAct; P70408; 4.
DR MINT; P70408; -.
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; 205 antibodies from 29 providers.
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; 3 hits in 72 CRISPR screens.
DR PRO; PR:P70408; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P70408; protein.
DR Bgee; ENSMUSG00000022321; Expressed in cortical subplate and 145 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
