ID A0A3P9MV46_POERE Unreviewed; 939 AA.
AC A0A3P9MV46;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000001227.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000001227.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000001227.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain. {ECO:0000256|ARBA:ARBA00003436}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR Ensembl; ENSPRET00000001267.1; ENSPREP00000001227.1; ENSPREG00000000942.1.
DR GeneTree; ENSGT00940000164173; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000000942; Expressed in head 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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 6.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR032455; Cadherin_C.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF332; PROTOCADHERIN1-ALPHA-AV3-RELATED; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR Pfam; PF15974; Cadherin_tail; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..939
FT /note="Cadherin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018197080"
FT TRANSMEM 694..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..135
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 136..243
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 244..351
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 352..457
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 458..566
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 581..680
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 831..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 104118 MW; E1E50B2A8B841491 CRC64;
MDCFRKSRRR DGFWLAFYFA LLFLLWKEAS AQIRYSVPEE VKGGTVVGNV AKDLGLDISF
LTERRFRVVP ESKDPIFEVN QDNGALYVIS HIDREELCKD SGSCLVEQKI LVENPLEMHY
VSVEITDVND NFPSFPEKQQ TIEIAEHTLP GRRFQLHNAH DPDAGINSVR TYTLTANEYF
DINIRQSDTG MIPFLILKKS LDREQKNKHE LVVTAVDGGK PPKSGKLNII IIVLDNNDNR
PVFSQEIYQL SIEENIPLGT TVFRMNATDV DEGVNGEIEY NLGKTLLRKV FDIFELDKVK
GEIVVKGLVD YEEKNLYELD VEASDKGTPP LTGECRLILK ILDVNDNPPE IQITSLSNTV
SEDSKRGTVI SLLSFSDKDS GMNGKIIANI INDVPFELKP SYKENIYSVV VKDNLDREEV
SHYDIQIKIT DCGDPPLSTI KSIKIEVSDI NDNIPRFSYN VLQIYIPENN VAGGSIFSVS
ATDNDLNENA GISYGIHREI NENTIAAFLN INSENGEIFA LKSFDFETLK TFQFQVVATD
SGTPSLSSNV TVNVFILDQN DNAPVILYPL SSNGSXEGVE EIPRXVNAGH LVTKVRAYDA
DIGYNGWLLF SLQEVXDHSL FGLDRYTGXI RTLRSFTETD EAEHKLVILV KDNGNVSLSA
TATVIAKLVE PKEAFAASDV KSAAKDEEED NVTFYLMITL GAVSVLFIIS IIVLIAMQCS
KSTDYTSKHL QEANYDGTLC HSIQYRSGDK RYMLVGPRMS IGSTIVPGSH ANTLVLPDRR
RPSEEPKAPN SDWRYSASLR AGGVMQSSVH MEESAVMQGA QGVLVQNWPT ASSAADGEGG
EVSPPMGAGV DSNSWHFRYG PGGPGAPPQH LKPGEVPPEA FIIPGSPAII SIRQNQGGED
DKSDFITFGK KEEAKKKKKK KKEKEKKDKK DKGKDDGDE
//
