ID CAD12_MOUSE Reviewed; 794 AA.
AC Q5RJH3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 130.
DE RecName: Full=Cadherin-12;
DE Flags: Precursor;
GN Name=Cdh12;
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=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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; BC086655; AAH86655.1; -; mRNA.
DR CCDS; CCDS27396.1; -.
DR RefSeq; NP_001008420.1; NM_001008420.2.
DR RefSeq; XP_011243643.1; XM_011245341.2.
DR RefSeq; XP_011243644.1; XM_011245342.2.
DR RefSeq; XP_011243645.1; XM_011245343.2.
DR RefSeq; XP_011243646.1; XM_011245344.2.
DR RefSeq; XP_011243647.1; XM_011245345.2.
DR RefSeq; XP_011243649.1; XM_011245347.2.
DR RefSeq; XP_017172034.1; XM_017316545.1.
DR RefSeq; XP_017172035.1; XM_017316546.1.
DR AlphaFoldDB; Q5RJH3; -.
DR SMR; Q5RJH3; -.
DR STRING; 10090.ENSMUSP00000153750; -.
DR GlyConnect; 2165; 2 N-Linked glycans (1 site).
DR GlyCosmos; Q5RJH3; 4 sites, 2 glycans.
DR GlyGen; Q5RJH3; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q5RJH3; -.
DR PhosphoSitePlus; Q5RJH3; -.
DR PaxDb; 10090-ENSMUSP00000074632; -.
DR ProteomicsDB; 281740; -.
DR Antibodypedia; 22634; 313 antibodies from 28 providers.
DR DNASU; 215654; -.
DR Ensembl; ENSMUST00000075132.8; ENSMUSP00000074632.7; ENSMUSG00000040452.10.
DR Ensembl; ENSMUST00000227496.2; ENSMUSP00000153750.2; ENSMUSG00000040452.10.
DR GeneID; 215654; -.
DR KEGG; mmu:215654; -.
DR UCSC; uc007vip.1; mouse.
DR AGR; MGI:109503; -.
DR CTD; 1010; -.
DR MGI; MGI:109503; Cdh12.
DR VEuPathDB; HostDB:ENSMUSG00000040452; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154187; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q5RJH3; -.
DR OMA; FTRHRPP; -.
DR OrthoDB; 3667774at2759; -.
DR PhylomeDB; Q5RJH3; -.
DR TreeFam; TF329887; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 215654; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Cdh12; mouse.
DR PRO; PR:Q5RJH3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q5RJH3; Protein.
DR Bgee; ENSMUSG00000040452; Expressed in pyramidal layer of CA1 and 64 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: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: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; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 5.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 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_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027:SF96; CADHERIN-12; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript 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..23
FT /evidence="ECO:0000255"
FT PROPEP 24..54
FT /evidence="ECO:0000255"
FT /id="PRO_0000320094"
FT CHAIN 55..794
FT /note="Cadherin-12"
FT /id="PRO_0000320095"
FT TOPO_DOM 55..609
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..794
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..609
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97326"
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 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 794 AA; 88468 MW; 963DE4B1CB3088DF CRC64;
MLTRNSLYLL LWILFDGGLL TPLQPQPQQT LATEPKENVI HLSGRRSHFQ RVKRGWVWNQ
FFVLEEYMGS EPQYVGKLHS DLDKGEGTVK YTLSGDGAGT VFTIDETTGD IHAIRSLDRE
EKPFYTLRAQ AVDIETRKPL EPESEFIIKV QDINDNEPKF LDGPYVASVP EMSPVGAYVL
QVKATDADDP TYGNSARVVY SILQGQPYFS IDPKTGVIRT ALPNMDREVK EQYQVLIQAK
DMGGQLGGLA GTTVVNITLT DVNDNPPRFP KSIFHLKVPE SSPVGSAIGR IRAVDPDFGK
NAEIEYNIVP GDGGNLFDIV TDEDTQEGII KLKKPLDFET KKAYTFKVEA SNLHLDHRFH
SAGPFKDTAT VKISVLDVDE PPVFSKPLYT MEVYEDTPVG TIIGAVTAQD LDVGSSAVRY
FIDWKSDGES YFTIDGTEGT IATNELLDRE NMAQYNFSII ASKVSNPLLT SKVNILINVL
DVNEFPPEIS VPYETAVCEN AKPGQIIQIV GAVDRDLSPA GQQFSFRLAP EAVIKPNFTV
HDFRNNTAGI ETRRNGYSRR QQELYFLPIV IEDSSYPVQS STNTMTIRVC RCDSDGTILS
CNVEAIFLPV GLSTGALIAI LLCMVILLAI VVLYVALRRQ RKKDTLMTSK EDIRDNVIHY
DDEGGGEEDT QAFDIGALRN PKVIEENKIR RDIKPDSLCL SRQRPQVEDN TDIRDFIHRR
LQENDADPAA PPYDSLATYA YEGNGSVAES LSSIDSLTTE ADQDYDYLSD WGPRFKVLAD
MFGEEESYNP DNVT
//
