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 12-AUG-2020, entry version 107. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; 117 antibodies. DR DNASU; 646480; -. DR Ensembl; ENST00000379071; ENSP00000368362; ENSG00000205186. DR GeneID; 646480; -. DR KEGG; hsa:646480; -. DR UCSC; uc011lfo.3; human. DR CTD; 646480; -. DR DisGeNET; 646480; -. DR EuPathDB; HostDB:ENSG00000205186.2; -. 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 eggNOG; KOG4015; Eukaryota. DR GeneTree; ENSGT00940000161845; -. DR HOGENOM; CLU_113772_0_0_1; -. DR InParanoid; Q0Z7S8; -. DR OMA; GGSMIHV; -. DR OrthoDB; 1417203at2759; -. DR PhylomeDB; Q0Z7S8; -. DR TreeFam; TF316894; -. DR PathwayCommons; Q0Z7S8; -. DR Reactome; R-HSA-163560; Triglyceride catabolism. DR BioGRID-ORCS; 646480; 0 hits in 99 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 46 other tissues. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0001675; P:acrosome assembly; IEA:Ensembl. DR GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome. 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:0000244|PDB:4A60" FT STRAND 7..16 FT /evidence="ECO:0000244|PDB:4A60" FT HELIX 17..24 FT /evidence="ECO:0000244|PDB:4A60" FT HELIX 28..34 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 40..46 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 49..56 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 59..65 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 71..74 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 80..88 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 91..98 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 101..110 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 113..120 FT /evidence="ECO:0000244|PDB:4A60" FT STRAND 123..130 FT /evidence="ECO:0000244|PDB:4A60" SQ SEQUENCE 132 AA; 15093 MW; B189DA5EB0B234FA CRC64; MVEPFLGTWK LVSSENFEDY MKELGVNFAA RNMAGLVKPT VTISVDGKMM TIRTESSFQD TKISFKLGEE FDETTADNRK VKSTITLENG SMIHVQKWLG KETTIKRKIV DEKMVVECKM NNIVSTRIYE KV //