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Database: UniProt
Entry: A0A452G596_CAPHI
LinkDB: A0A452G596_CAPHI
Original site: A0A452G596_CAPHI 
ID   A0A452G596_CAPHI        Unreviewed;       699 AA.
AC   A0A452G596;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=UV radiation resistance associated {ECO:0000313|Ensembl:ENSCHIP00000031753.1};
GN   Name=UVRAG {ECO:0000313|Ensembl:ENSCHIP00000031753.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000031753.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000031753.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000031753.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   EMBL; LWLT01000015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_017914818.1; XM_018059329.1.
DR   AlphaFoldDB; A0A452G596; -.
DR   STRING; 9925.ENSCHIP00000031753; -.
DR   Ensembl; ENSCHIT00000039627.1; ENSCHIP00000031753.1; ENSCHIG00000025967.1.
DR   GeneID; 102174861; -.
DR   KEGG; chx:102174861; -.
DR   CTD; 7405; -.
DR   GeneTree; ENSGT00390000012877; -.
DR   OrthoDB; 5481315at2759; -.
DR   Proteomes; UP000291000; Chromosome 15.
DR   Bgee; ENSCHIG00000025967; Expressed in cerebellum and 18 other cell types or tissues.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0070418; C:DNA-dependent protein kinase complex; IEA:Ensembl.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR   GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; IEA:Ensembl.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:0000149; F:SNARE binding; IEA:Ensembl.
DR   GO; GO:0097352; P:autophagosome maturation; IEA:Ensembl.
DR   GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
DR   GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR   GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0051684; P:maintenance of Golgi location; IEA:Ensembl.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032801; P:receptor catabolic process; IEA:Ensembl.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR   GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0035493; P:SNARE complex assembly; IEA:Ensembl.
DR   GO; GO:0007051; P:spindle organization; IEA:Ensembl.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
DR   CDD; cd00030; C2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR   PANTHER; PTHR15157; UV RADIATION RESISTANCE-ASSOCIATED GENE PROTEIN; 1.
DR   PANTHER; PTHR15157:SF5; UV RADIATION RESISTANCE-ASSOCIATED GENE PROTEIN; 1.
DR   Pfam; PF10186; ATG14; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS50004; C2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT   DOMAIN          23..149
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          237..306
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        513..555
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   699 AA;  77881 MW;  95F5537BBC4E6C92 CRC64;
     MNASASVGGP LPPPPTGPAA ALPPGSAARA LHVELPSQQR RLRHLRNIAA RNIVNRNGHQ
     LLDTYFTLHL CNTEKVFKEF YRSEVIKNSL NPTWRSLDFG IIPDRLDTSV SCFVVKIWGG
     KEDIYQLLIE WKVCLDGLKY LGQQIHARNQ NEIIFGLNDG YYGAPFEHKG YSNAQKNILL
     QVDQNCVRNS YDVFSLLRLH RAQCAIKQTQ VTVQKIGKEI EEKLRLTSTS NGLKKESECL
     QLKILVLRNE LERQKKALGR EAVLLHKEQI ALQDKGSTFS AEHLKLQLQK ESLNELRKEC
     TAKRELFLKT NAQLTIRCRQ LLSELSYIYP IDLNDHKDYF VCGVKLPNSE DFQAKDDGSI
     AVALGYTAHL VSMISFFLQV PLRYPVIHKG SRSTIKDNIN DKLTEKEREF PLYPKGGEKL
     QFDYGVYLLN KNIAQLRYQH GLGTPDLRQT LPNLKNFMEH GLMVRCDRHH TSSAIPVPKR
     QSSIFGGADV GFSGGIPSPD KGYRKRASSE NERLQYKTPP PSYNSALVQP VTPVPSTGES
     DRKTASLSSS LDTSLDLSKE NKKKGVDLGD SLNGGHMSVN TSQEQGQALS GPPATINGTL
     LPGEQASSSG AQLPGGFHPV SEAELCCTVE QAEEIIGMEA TGFTSGDQLE AFNCIPVDSA
     VAVECDEQVL GEFEEFSRRI YALNENVSSF RRPRRSSDK
//
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