CAD10_HUMAN
ID CAD10_HUMAN Reviewed; 788 AA.
AC Q9Y6N8; Q9ULB3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cadherin-10;
DE AltName: Full=T2-cadherin;
DE Flags: Precursor;
GN Name=CDH10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10386616; DOI=10.1016/s0014-5793(99)00672-9;
RA Kools P., Vanhalst K., van den Eynde E., van Roy F.;
RT "The human cadherin-10 gene: complete coding sequence, predominant
RT expression in the brain, and mapping on chromosome 5p13-14.";
RL FEBS Lett. 452:328-334(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10861224; DOI=10.1042/0264-6021:3490159;
RA Shimoyama Y., Tsujimoto G., Kitajima M., Natori M.;
RT "Identification of three human type-II classic cadherins and frequent
RT heterophilic interactions between different subclasses of type-II classic
RT cadherins.";
RL Biochem. J. 349:159-167(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-371.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Also found in
CC adult and fetal kidney. Very low levels detected in prostate and fetal
CC lung. {ECO:0000269|PubMed:10386616}.
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; AF039747; AAD44017.1; -; mRNA.
DR EMBL; AB035303; BAA87417.1; -; mRNA.
DR CCDS; CCDS3892.1; -.
DR RefSeq; NP_006718.2; NM_006727.4.
DR RefSeq; XP_011512225.1; XM_011513923.2.
DR AlphaFoldDB; Q9Y6N8; -.
DR SMR; Q9Y6N8; -.
DR BioGRID; 107443; 6.
DR IntAct; Q9Y6N8; 6.
DR STRING; 9606.ENSP00000264463; -.
DR GlyGen; Q9Y6N8; 4 sites.
DR iPTMnet; Q9Y6N8; -.
DR PhosphoSitePlus; Q9Y6N8; -.
DR BioMuta; CDH10; -.
DR DMDM; 116241276; -.
DR jPOST; Q9Y6N8; -.
DR MassIVE; Q9Y6N8; -.
DR PaxDb; Q9Y6N8; -.
DR PeptideAtlas; Q9Y6N8; -.
DR PRIDE; Q9Y6N8; -.
DR ProteomicsDB; 86749; -.
DR Antibodypedia; 2223; 205 antibodies from 29 providers.
DR DNASU; 1008; -.
DR Ensembl; ENST00000264463.8; ENSP00000264463.4; ENSG00000040731.10.
DR GeneID; 1008; -.
DR KEGG; hsa:1008; -.
DR MANE-Select; ENST00000264463.8; ENSP00000264463.4; NM_006727.5; NP_006718.2.
DR CTD; 1008; -.
DR DisGeNET; 1008; -.
DR GeneCards; CDH10; -.
DR HGNC; HGNC:1749; CDH10.
DR HPA; ENSG00000040731; Group enriched (brain, prostate).
DR MIM; 604555; gene.
DR neXtProt; NX_Q9Y6N8; -.
DR OpenTargets; ENSG00000040731; -.
DR PharmGKB; PA26283; -.
DR VEuPathDB; HostDB:ENSG00000040731; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154187; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q9Y6N8; -.
DR OMA; RNGFSRH; -.
DR OrthoDB; 201053at2759; -.
DR PhylomeDB; Q9Y6N8; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; Q9Y6N8; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; Q9Y6N8; -.
DR SIGNOR; Q9Y6N8; -.
DR BioGRID-ORCS; 1008; 12 hits in 1059 CRISPR screens.
DR ChiTaRS; CDH10; human.
DR GeneWiki; CDH10; -.
DR GenomeRNAi; 1008; -.
DR Pharos; Q9Y6N8; Tbio.
DR PRO; PR:Q9Y6N8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y6N8; protein.
DR Bgee; ENSG00000040731; Expressed in Brodmann (1909) area 23 and 127 other tissues.
DR ExpressionAtlas; Q9Y6N8; baseline and differential.
DR Genevisible; Q9Y6N8; HS.
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; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0098609; P:cell-cell adhesion; NAS:UniProtKB.
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 Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..54
FT /evidence="ECO:0000255"
FT /id="PRO_0000003781"
FT CHAIN 55..788
FT /note="Cadherin-10"
FT /id="PRO_0000003782"
FT TOPO_DOM 55..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 55..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..487
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 488..606
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97326"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
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 VARIANT 371
FT /note="V -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036102"
FT VARIANT 413
FT /note="S -> F (in dbSNP:rs1395027)"
FT /id="VAR_028751"
FT CONFLICT 34
FT /note="Q -> R (in Ref. 1; AAD44017)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="V -> A (in Ref. 1; AAD44017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 788 AA; 88451 MW; E92908F9C19270B2 CRC64;
MTIHQFLLLF LFWVCLPHFC SPEIMFRRTP VPQQRILSSR VPRSDGKILH RQKRGWMWNQ
FFLLEEYTGS DYQYVGKLHS DQDKGDGSLK YILSGDGAGT LFIIDEKTGD IHATRRIDRE
EKAFYTLRAQ AINRRTLRPV EPESEFVIKI HDINDNEPTF PEEIYTASVP EMSVVGTSVV
QVTATDADDP SYGNSARVIY SILQGQPYFS VEPETGIIRT ALPNMNRENR EQYQVVIQAK
DMGGQMGGLS GTTTVNITLT DVNDNPPRFP QNTIHLRVLE SSPVGTAIGS VKATDADTGK
NAEVEYRIID GDGTDMFDIV TEKDTQEGII TVKKPLDYES RRLYTLKVEA ENTHVDPRFY
YLGPFKDTTI VKISIEDVDE PPVFSRSSYL FEVHEDIEVG TIIGTVMARD PDSISSPIRF
SLDRHTDLDR IFNIHSGNGS LYTSKPLDRE LSQWHNLTVI AAEINNPKET TRVAVFVRIL
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 NDSIAESLSS LESGTTEGDQ NYDYLREWGP RFNKLAEMYG
GGESDKDS
