ID A0A3Q7T9D2_VULVU Unreviewed; 927 AA.
AC A0A3Q7T9D2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Protocadherin gamma-B5 isoform X15 {ECO:0000313|RefSeq:XP_025873709.1};
GN Name=LOC112934395 {ECO:0000313|RefSeq:XP_025873709.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025873709.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025873709.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025873709.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025873709.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_025873709.1; XM_026017924.1.
DR AlphaFoldDB; A0A3Q7T9D2; -.
DR Proteomes; UP000286640; 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; 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:SF259; PROTOCADHERIN GAMMA-B3-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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..927
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018598095"
FT TRANSMEM 684..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..133
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 134..242
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 243..343
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 352..448
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 449..558
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 573..671
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 792..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 99896 MW; 73D3E5EFBEE8A02B CRC64;
MGSSAGERGW AERLPVLFPF LLSLFCWALS EQIRYRIPEE MPEGSVVGNL AKDLGLSVHE
LPTRQLRISL EKPYFTVSAK SGELLVSSRL DREQMCGKKS ACTLEFEAVA ENPLNFYHVS
VDVEDINDHT PKFTQTSFDL QISESTVPGT RFILEAAEDA DIGLNGLQIY KLSLSPRFSL
INKDKLDGSK YPELALGKRL DREQQSYHCL VLTALDGGDP PLSGTTELQI QVTDANDNPP
VFNQDIYRVS LPENVPPGTA VLQVSATDQD EGINSEITYS FYRTGQVFSL NSKTGEITTL
RTLDFEETKE YSIVVEGRDG GGLAAQCTVE INIQDENDNS PEVTFHSLTE MILENGPPGT
LIALIKIHDQ DSGENGEVNC RLEGEVPFQI TSSSKNSYKL VIDGTLDREQ TPEYNVTITA
TDRGKPPLSS SISITLHIAD VNDNAPVFHQ ASYVVHVAEN NPPGAPIAQV SASDPDLGPN
GRVSYSIVAS DLEPRALASY VSVSAQSGVV FAQRAFDHEQ LRAFELTLQA RDQGSPALSA
NVSLRVLVGD RNDNAPRVLY PALGPDGSAL FDTVPRAAQP GYLVTKVVAV DADSGHNAWL
SYHVLQASEP GLFSLGLRTG EVRTARALGD RDAARQRLLV AVRDGGQPPL SATATLLLVF
ADSLQEALPD VSERQAPADP QAELQFYLVV ALALISVLFL LAVILAVALR LGRSSSSTTW
GCFQPGLCVK SGPVVPPNYS EGTLPYSYNL CVAHTGKTEF NFLKCNEQLS SGQDILLCND
SSGALFPLYN TNESTSDPET LTSQAPPNTD WRFSQAQRPG TSGSQNGDET GTWPNNQFDT
EMLQAMILAS ASEAADGSST LGGGAGTMGL SARYGPQFTL QHVPDYRQNV YIPGSNATLT
NAAGKRDGKA PAGGNGSKKK SGKKEKK
//
