ID A0A3P8NTL4_ASTCA Unreviewed; 798 AA.
AC A0A3P8NTL4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Cadherin-7-like {ECO:0000313|Ensembl:ENSACLP00000008094.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000008094.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000008094.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000008094.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU003318};
CC Single-pass type I membrane protein {ECO:0000256|RuleBase:RU003318}.
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DR AlphaFoldDB; A0A3P8NTL4; -.
DR STRING; 8154.ENSACLP00000008094; -.
DR Ensembl; ENSACLT00000008281.1; ENSACLP00000008094.1; ENSACLG00000005506.1.
DR GeneTree; ENSGT00940000166818; -.
DR OMA; YVCEGTQ; -.
DR OrthoDB; 3667774at2759; -.
DR Proteomes; UP000265100; Chromosome 9.
DR Bgee; ENSACLG00000005506; Expressed in muscle tissue and 1 other cell type or tissue.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0060429; P:epithelium development; IEA:UniProt.
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:SF421; -; 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 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW 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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..798
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018252702"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..159
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 160..268
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 269..383
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 384..488
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 488..600
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 757..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 88948 MW; EA5B2B73A22C89C9 CRC64;
MYGWTVKMSM PSVLAVAMVF FMIPGGVLSD MRGTQGLEAQ QLAQGSTHLH RRLKRGWIWK
QLFVPEEDPT PRVIGQLKSD SDQGESSIKY ILSGEGAGDV FEINEYTGEI RTLKKLDREE
KAFYVLQAQA INRWSNEPEE PQSEFIITVQ DINDNVPQFQ NEPYVSSIPE MCPIGTTVAQ
VTATDADDPM FGNNAKLIYS ILQGEPYFSV EPKTGIIVTS WQNMDREARE QYQVVVQVKD
MLGLSGGYSS STTVTVSLTD VNDNGPTFQQ HLYTFAVPEN AAIGTTVGRI MAEDGDTGIN
AKMTYSLEGE LEESTFIIKT DPVTQEGVIL LAKPLDFEVK RRFDMTAEAV NDHVDTRFLS
LDDFTDRTTV KVIVKDEDEP PVFLSPVYEW KLPENAAVGT VVGSVSARDT DTVNNPIRYS
VDKRSDTTKA FKIDPNNGTI TVAKSLDRET AAWHNVTVEA KETTQNHLSS SVVVFIKVLD
INDNVPRLAR DYQPYICEGT QAGELIQLLS AVDPDDPVEG HHFYFSMVPE KRINPNFTIR
DNQDNTAGIV ARRSTFTRKD RTQYLLPVVV ADSGSPALSG TSTLTISVCS CQPAGHCPTG
GVEALALSMG VSLQTLLGIL FCLVTLTVLS VVMVMVRRHR RKQQEGREVE VKELELPETV
SQKVFYYGES GVGGVELDFC QPTVPMRPRP RRRERRMRRE DVRASIRMSL RESHLIGPED
EVFRQFILDR LAEADQDPYA PPFDYLQIYA YEGSGSPTGS LSSLDSSTLE SDQSVCNPRP
SLARLTPWYG AREEDTLF
//