FABP9_HUMAN
ID FABP9_HUMAN Reviewed; 132 AA.
AC Q0Z7S8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Fatty acid-binding protein 9;
DE AltName: Full=Testis lipid-binding protein;
DE Short=TLBP;
DE AltName: Full=Testis-type fatty acid-binding protein;
DE Short=T-FABP;
GN Name=FABP9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pouresmaeili F., Rabbani H., Jeddi Tehrani M., Kalili T.;
RT "Cloning of a novel human testis-specific gene.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; DQ821473; ABG49443.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW87091.1; -; Genomic_DNA.
DR RefSeq; NP_001073995.1; NM_001080526.1.
DR PDB; 4A60; X-ray; 1.53 A; A=1-132.
DR PDBsum; 4A60; -.
DR AlphaFoldDB; Q0Z7S8; -.
DR SMR; Q0Z7S8; -.
DR STRING; 9606.ENSP00000368362; -.
DR ChEMBL; CHEMBL3826865; -.
DR iPTMnet; Q0Z7S8; -.
DR PhosphoSitePlus; Q0Z7S8; -.
DR BioMuta; FABP9; -.
DR DMDM; 121948152; -.
DR MassIVE; Q0Z7S8; -.
DR PaxDb; Q0Z7S8; -.
DR PeptideAtlas; Q0Z7S8; -.
DR PRIDE; Q0Z7S8; -.
DR ProteomicsDB; 58847; -.
DR Antibodypedia; 59079; 120 antibodies from 13 providers.
DR DNASU; 646480; -.
DR Ensembl; ENST00000379071.4; ENSP00000368362.2; ENSG00000205186.4.
DR GeneID; 646480; -.
DR KEGG; hsa:646480; -.
DR MANE-Select; ENST00000379071.4; ENSP00000368362.2; NM_001080526.2; NP_001073995.1.
DR UCSC; uc011lfo.3; human.
DR CTD; 646480; -.
DR DisGeNET; 646480; -.
DR GeneCards; FABP9; -.
DR HGNC; HGNC:3563; FABP9.
DR HPA; ENSG00000205186; Tissue enriched (skin).
DR neXtProt; NX_Q0Z7S8; -.
DR OpenTargets; ENSG00000205186; -.
DR PharmGKB; PA27964; -.
DR VEuPathDB; HostDB:ENSG00000205186; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000161845; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; Q0Z7S8; -.
DR OMA; KMMTIRT; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; Q0Z7S8; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; Q0Z7S8; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR BioGRID-ORCS; 646480; 4 hits in 249 CRISPR screens.
DR GenomeRNAi; 646480; -.
DR Pharos; Q0Z7S8; Tbio.
DR PRO; PR:Q0Z7S8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q0Z7S8; protein.
DR Bgee; ENSG00000205186; Expressed in subcutaneous adipose tissue and 45 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0001675; P:acrosome assembly; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..132
FT /note="Fatty acid-binding protein 9"
FT /id="PRO_0000317292"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55054"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55054"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55054"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55054"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:4A60"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:4A60"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:4A60"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:4A60"
SQ SEQUENCE 132 AA; 15093 MW; B189DA5EB0B234FA CRC64;
MVEPFLGTWK LVSSENFEDY MKELGVNFAA RNMAGLVKPT VTISVDGKMM TIRTESSFQD
TKISFKLGEE FDETTADNRK VKSTITLENG SMIHVQKWLG KETTIKRKIV DEKMVVECKM
NNIVSTRIYE KV
