ID A0A452GMR4_9SAUR Unreviewed; 127 AA.
AC A0A452GMR4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Fatty acid-binding protein, liver {ECO:0000256|RuleBase:RU369022};
DE Short=L-FABP {ECO:0000256|RuleBase:RU369022};
DE AltName: Full=Liver-type fatty acid-binding protein {ECO:0000256|RuleBase:RU369022};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000002941.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000002941.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Binds free fatty acids and their coenzyme A derivatives,
CC bilirubin, and some other small molecules in the cytoplasm. May be
CC involved in intracellular lipid transport.
CC {ECO:0000256|RuleBase:RU369022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369022}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000256|RuleBase:RU369022}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000256|ARBA:ARBA00008390,
CC ECO:0000256|RuleBase:RU369022}.
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DR AlphaFoldDB; A0A452GMR4; -.
DR STRING; 38772.ENSGAGP00000002941; -.
DR Ensembl; ENSGAGT00000003369.1; ENSGAGP00000002941.1; ENSGAGG00000002342.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005504; F:fatty acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015908; P:fatty acid transport; IEA:UniProtKB-UniRule.
DR CDD; cd19444; FABP1; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1.
DR PANTHER; PTHR11955:SF96; FATTY ACID-BINDING PROTEIN, LIVER; 1.
DR Pfam; PF14651; Lipocalin_7; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00214; FABP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU369022};
KW Lipid-binding {ECO:0000256|RuleBase:RU369022};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Transport {ECO:0000256|RuleBase:RU369022}.
FT DOMAIN 5..22
FT /note="Cytosolic fatty-acid binding proteins"
FT /evidence="ECO:0000259|PROSITE:PS00214"
SQ SEQUENCE 127 AA; 14034 MW; F480E5A3E11BC89C CRC64;
MSFNGKFELQ SQENFEPFMK ALCLSDELIE KGKDVKSISE IVQNGKKFKV TVTTGSKVLT
NEFTIGEEAE LETPTGEKVK AVVQMEGDNK LVTNLGKIKS VTEIKGDIVT NTLTVGDISY
TRISKRI
//
