ID A0A2Y9KFH1_ENHLU Unreviewed; 794 AA.
AC A0A2Y9KFH1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cadherin-12 isoform X1 {ECO:0000313|RefSeq:XP_022368160.1};
GN Name=LOC111153436 {ECO:0000313|RefSeq:XP_022368160.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022368160.1};
RN [1] {ECO:0000313|RefSeq:XP_022368160.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022368160.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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 RefSeq; XP_022368160.1; XM_022512452.1.
DR AlphaFoldDB; A0A2Y9KFH1; -.
DR STRING; 391180.A0A2Y9KFH1; -.
DR KEGG; elk:111153436; -.
DR OrthoDB; 3667774at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005886; C:plasma membrane; 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; 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; 1.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 4: Predicted;
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..794
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016160781"
FT TRANSMEM 606..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..160
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 161..269
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 270..384
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 385..489
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 489..607
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 794 AA; 88287 MW; 3134E9383B9B727C CRC64;
MLTRNCLSLL LWVLFDGGLL TPLQPQPQQT LATEPTENVI HLPGRRPHFQ RVKRGWVWNQ
FFVLEEYMGS EPQYVGKLHS DLDKGEGTVK YTLSGDGAGT VFTIDETTGD IHAIRSLDRE
EKPFYTLRAQ AVDIETRKPL EPESEFIIKV QDINDNEPKF LDGPYIASVP EMSPVGAYVL
QVKATDADDP TYGNSARVVY SILQGQPYFS IDPKTGVIRT ALPNMDREVK EQYQVLIQAK
DMGGQLGGLA GTTVVNITLT DVNDNPPRFP KSIFHLKVPE SSPIGSAIGR IRAVDPDFGQ
NAEIEYNIVP GDGGNLFDIV TDEDTQEGVI KLKKPLDFET KKAYTFKVEA SNVHLDHRFH
SVGPFKDTAT VKISVLDVEE PPVFSKPLYT MEVYEDTPIG TIIGAVTAQD LDVGSSAVRY
FIDWKSDGDS YFTIDGTEGT IATNELLDRE STAQYNFSII ASKVSNPLLS SKVNILINVL
DVNEFPPEIS VPYDTAVCEN AKPGQIIQIV SAADRDLSPA GQRFSFRLSP EAAIKPNFTV
HDFRNNTAGI ETRRNGYSRR QQELYFLPVV IEDSSYPVQS STNTMTIRVC RCDSDGTILS
CNVEAIFLPV GLSTGALIAI LLCIVILLAI VVLYVALRRQ KKKDTLMTSK EDIRDNVIHY
DDEGGGEEDT QAFDIGALRN PKVIEDNKIR RDIKPDSLCL PRQRPPVEDN TDIRDFINQR
LQENDVDPTA PPYDSLATYA YEGNGSVADS LSSIDSLTTE ADQDYDYLTD WGPRFKVLAD
MFGEEESYNP DKVT
//