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Database: UniProt
Entry: F1SK35_PIG
LinkDB: F1SK35_PIG
Original site: F1SK35_PIG 
ID   F1SK35_PIG              Unreviewed;       317 AA.
AC   F1SK35;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Retinaldehyde-binding protein 1 {ECO:0000313|EMBL:HCZ81532.1, ECO:0000313|Ensembl:ENSSSCP00000002009.3};
GN   Name=RLBP1 {ECO:0000313|Ensembl:ENSSSCP00000002009.3,
GN   ECO:0000313|VGNC:VGNC:92327};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000002009.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000002009.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000002009.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HCZ81532.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000002009.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; DQIR01026057; HCZ81532.1; -; Transcribed_RNA.
DR   PaxDb; 9823-ENSSSCP00000002009; -.
DR   Ensembl; ENSSSCT00000002058.4; ENSSSCP00000002009.3; ENSSSCG00000001836.5.
DR   VGNC; VGNC:92327; RLBP1.
DR   eggNOG; KOG1471; Eukaryota.
DR   GeneTree; ENSGT00940000160026; -.
DR   HOGENOM; CLU_046597_4_0_1; -.
DR   Proteomes; UP000008227; Chromosome 7.
DR   Bgee; ENSSSCG00000001836; Expressed in hypothalamus and 45 other cell types or tissues.
DR   CDD; cd00170; SEC14; 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:SF200; RETINALDEHYDE-BINDING PROTEIN 1; 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   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1SK35};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   DOMAIN          136..297
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   COILED          45..75
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   317 AA;  36568 MW;  FF0BF03B02B4C43B CRC64;
     MSEGAGTFRM VPEEEQELRA QLERLTTKDH GPVFGQCSQL PRHTLQKAKD ELNEREETRE
     EVVRELQELV QAEAASGQEL AVAVAERVQG KDSAFFLRFI RARKFHVGRA YELLRGYVNF
     RLQYPELFDS LSLEAIRCTV EAGYPGVLST RDKYGRVVML FNIENWDAEE ITFDEILQAY
     CFILEKLLEN EETQINGFCI IENFKGFTMQ QAAGLRASDL RKMVDMLQDS FPARFKAIHF
     IHQPWYFTTT YNVVKPFLKS KLLQRVFVHG EDLSDFFQEF DEDILPSDFG GTLPKYDGKV
     VAEQLFGPRA QAENTAF
//
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