ID   A0A2Y9K4F5_ENHLU        Unreviewed;       754 AA.
AC   A0A2Y9K4F5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Cadherin-12 isoform X2 {ECO:0000313|RefSeq:XP_022368161.1};
GN   Name=LOC111153436 {ECO:0000313|RefSeq:XP_022368161.1};
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_022368161.1};
RN   [1] {ECO:0000313|RefSeq:XP_022368161.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022368161.1};
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}.
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DR   RefSeq; XP_022368161.1; XM_022512453.1.
DR   AlphaFoldDB; A0A2Y9K4F5; -.
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; 4.
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; 4.
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..754
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015954322"
FT   TRANSMEM        566..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..160
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          185..229
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          230..344
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          345..449
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          449..567
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
SQ   SEQUENCE   754 AA;  83955 MW;  0C2DFA414DD66576 CRC64;
     MLTRNCLSLL LWVLFDGGLL TPLQPQPQQT LATEPTENVI HLPGRRPHFQ RVKRGWVWNQ
     FFVLEEYMGS EPQYVGKLHS DLDKGEGTVK YTLSGDGAGT VFTIDETTGD IHAIRSLDRE
     EKPFYTLRAQ AVDIETRKPL EPESEFIIKV QDINDNEPKF LDGPYIASVP EMSPVGVIRT
     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
//