ID G1STX1_RABIT Unreviewed; 794 AA.
AC G1STX1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Cadherin 12 {ECO:0000313|Ensembl:ENSOCUP00000006773.2};
GN Name=CDH12 {ECO:0000313|Ensembl:ENSOCUP00000006773.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000006773.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000006773.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000006773.2,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000006773.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000006773.2};
RG Ensembl;
RL Submitted (JUL-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 EMBL; AAGW02030117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02030126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017200150.1; XM_017344661.1.
DR AlphaFoldDB; G1STX1; -.
DR SMR; G1STX1; -.
DR STRING; 9986.ENSOCUP00000006773; -.
DR PaxDb; 9986-ENSOCUP00000006773; -.
DR Ensembl; ENSOCUT00000007835.4; ENSOCUP00000006773.2; ENSOCUG00000007832.4.
DR GeneID; 100340496; -.
DR KEGG; ocu:100340496; -.
DR CTD; 1010; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154187; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; G1STX1; -.
DR OMA; FTRHRPP; -.
DR OrthoDB; 3667774at2759; -.
DR TreeFam; TF329887; -.
DR Proteomes; UP000001811; Chromosome 11.
DR Bgee; ENSOCUG00000007832; Expressed in frontal cortex and 3 other cell types or tissues.
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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
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_5003423007"
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; 88386 MW; 086AA1D4C67615B6 CRC64;
MLTRNCLSLL LWVLFDGGLL TPLQPQPRQT LTTEPRENVL RLPGRRLHFQ RVKRGWVWNQ
FFVLEEYMGA EPQYVGKLHS DLDKGEGTVK YTLSGDGAGT VFTIDETTGD IHAIRSLDRE
EKPFYTLRAQ AVDIETRKPL EPESEFIIKV QDINDNEPRF LDGPYVASVP EMSPVGAYVL
QVKATDADDP TYGNSARVVY SILQGQPYFS IDPKTGVIRT ALPNMDREVK EQYQVLIQAK
DMGGQLGGLA GTTIVNITLT DVNDNPPRFP KSIFHLKVPE SSPVGSAVGR IRAVDPDFGQ
NAEIEYNIVP GDGGNLFDII TDEETQEGVI KLKKPLDFET KKAYTFKVEA SNLHLDHRFH
SAGPFKDTAT VKISVLDVDE PPVFSKPLYT MEVYEDTPVG TIIGAVTAQD LDVGSSAVRY
FIDWKSDGDS YFTIDGTEGT IATNELLDRE STAQYNFSII ASKVSNPLLT SKVNIVINVL
DVNEFPPEIS VPYETAVCEN AKPGQIIQIV SAADRDLSPA GQQFSFRLSP EAAIKPNFTV
RDFRNNTAGI ETRRNGYSRR QQELYFLPVV IEDSSYPIQS STNTMTIRVC RCDSDGTILS
CNVEAIFLPV GLSTGALIAI LLCIVILLAI VVLYVALRRQ KKKDTLMTSK EDIRDNVIHY
DDEGGGEEDT QAFDIGALRN PKVIEENKIR RDIKPDTFCL PRQRPPVEDN TDIRDFINQR
LQENDVDPAA PPYDSLATYA YEGSGSVAES LSSIDSLTTE ADQDYDYLTG WGPRFKVLAD
MFGEEESYNP DKVT
//