ID D3YYT0_MOUSE Unreviewed; 849 AA.
AC D3YYT0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Cadherin-2 {ECO:0000256|ARBA:ARBA00021703};
DE AltName: Full=Neural cadherin {ECO:0000256|ARBA:ARBA00031121};
GN Name=Cdh2 {ECO:0000313|Ensembl:ENSMUSP00000111516.2,
GN ECO:0000313|MGI:MGI:88355};
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 {ECO:0000313|Ensembl:ENSMUSP00000111516.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000111516.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000111516.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000111516.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000111516.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004135}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; D3YYT0; -.
DR SMR; D3YYT0; -.
DR jPOST; D3YYT0; -.
DR MaxQB; D3YYT0; -.
DR PeptideAtlas; D3YYT0; -.
DR ProteomicsDB; 322825; -.
DR Antibodypedia; 4558; 1940 antibodies from 53 providers.
DR Ensembl; ENSMUST00000115850.2; ENSMUSP00000111516.2; ENSMUSG00000024304.15.
DR AGR; MGI:88355; -.
DR MGI; MGI:88355; Cdh2.
DR VEuPathDB; HostDB:ENSMUSG00000024304; -.
DR GeneTree; ENSGT00940000155981; -.
DR HOGENOM; CLU_005284_2_0_1; -.
DR ChiTaRS; Cdh2; mouse.
DR Proteomes; UP000000589; Chromosome 18.
DR Bgee; ENSMUSG00000024304; Expressed in median eminence of neurohypophysis and 309 other cell types or tissues.
DR ExpressionAtlas; D3YYT0; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 4.
DR Gene3D; 2.60.40.60; Cadherins; 6.
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; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027:SF79; CADHERIN-2; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01820; DESMOCOLLIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|MaxQB:D3YYT0,
KW ECO:0007829|PeptideAtlas:D3YYT0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 667..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 103..210
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 211..325
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 326..440
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 441..548
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 547..653
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 806..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 93857 MW; 6C663C9F3CEC0B65 CRC64;
MKFSNCNRKR KVQYESSEPA DFKVDEDGTV YAVRSFPLTA EQAKFLIYAQ DKETQEKWQV
AVNLSREPTL TEEPMKEPHE IEEIVFPRQL AKHSGALQRQ KRDWVIPPIN LPENSRGPFP
QELVRIRSDR DKNLSLRYSV TGPGADQPPT GIFIINPISG QLSVTKPLDR ELIARFHLRA
HAVDINGNQV ENPIDIVINV IDMNDNRPEF LHQVWNGSVP EGSKPGTYVM TVTAIDADDP
NALNGMLRYR ILSQAPSTPS PNMFTINNET GDIITVAAGL DREKVQQYTL IIQATDMEGN
PTYGLSNTAT AVITVTDVND NPPEFTAMTF YGEVPENRVD VIVANLTVTD KDQPHTPAWN
AAYRISGGDP TGRFAILTDP NSNDGLVTVV KPIDFETNRM FVLTVAAENQ VPLAKGIQHP
PQSTATVSVT VIDVNENPYF APNPKIIRQE EGLHAGTMLT TLTAQDPDRY MQQNIRYTKL
SDPANWLKID PVNGQITTIA VLDRESPNVK NNIYNATFLA SDNGIPPMSG TGTLQIYLLD
INDNAPQVLP QEAETCETPE PNSINITALD YDIDPNAGPF AFDLPLSPVT IKRNWTINRL
NGDFAQLNLK IKFLEAGIYE VPIIITDSGN PPKSNISILR VKVCQCDSNG DCTDVDRIVG
AGLGTGAIIA ILLCIIILLI LVLMFVVWMK RRDKERQAKQ LLIDPEDDVR DNILKYDEEG
GGEEDQDYDL SQLQQPDTVE PDAIKPVGIR RLDERPIHAE PQYPVRSAAP HPGDIGDFIN
EGLKAADNDP TAPPYDSLLV FDYEGSGSTA GSLSSLNSSS SGGDQDYDYL NDWGPRFKKL
ADMYGGGDD
//
