ID A0A091DA05_FUKDA Unreviewed; 327 AA.
AC A0A091DA05;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Clavesin-2 {ECO:0000256|ARBA:ARBA00013642};
DE AltName: Full=Retinaldehyde-binding protein 1-like 2 {ECO:0000256|ARBA:ARBA00031836};
GN ORFNames=H920_11293 {ECO:0000313|EMBL:KFO27298.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27298.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO27298.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO27298.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000256|ARBA:ARBA00004132}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004220}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000256|ARBA:ARBA00004150}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004150}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
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DR EMBL; KN122940; KFO27298.1; -; Genomic_DNA.
DR RefSeq; XP_010636542.1; XM_010638240.1.
DR AlphaFoldDB; A0A091DA05; -.
DR STRING; 885580.ENSFDAP00000010469; -.
DR Ensembl; ENSFDAT00000023335; ENSFDAP00000010469; ENSFDAG00000018221.
DR GeneID; 104872090; -.
DR CTD; 134829; -.
DR eggNOG; KOG1471; Eukaryota.
DR OMA; QNERLCD; -.
DR OrthoDB; 2943211at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 1.20.5.1200; Alpha-tocopherol transfer; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR PANTHER; PTHR10174; ALPHA-TOCOPHEROL TRANSFER PROTEIN-RELATED; 1.
DR PANTHER; PTHR10174:SF73; CLAVESIN-2; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR PRINTS; PR00180; CRETINALDHBP.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 4: Predicted;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 96..257
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 272..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 37753 MW; 6290919C1D7B18B6 CRC64;
MTHLQAGLSP ETLEKARLEL NENPDTLHQD IQEVRDMVIT RPDIGFLRTD DAFILRFLRA
RKFHHFEAFR LLAQYFEYRQ QNLDMFKSFK ATDPGIKQAL KDGFPGGLAN LDHYGRKILV
LFAANWDQSR YTLVDILRAI LLSLEAMIED PELQVNGFVL IIDWSNFTFK QASKLTPSML
RLAIEGLQDS FPARFGGIHF VNQPWYIHAL YTVIRPFLKE KTRKRIFLHG NNLNSLHQLI
HPEILPSEFG GMLPPYDMGT WARTLLDHEY DEDSEHSADP YGTPAKEVEK GLSPKSMKRS
QSVLDPTVLM HMDKSEEENM QPLLSLD
//
