ID Q6FGL7_HUMAN Unreviewed; 127 AA. AC Q6FGL7; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 02-SEP-2026, entry version 157. 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}; DE Flags: Fragment; GN Name=FABP1 {ECO:0000313|EMBL:CAG46887.1}; GN ORFNames=hCG_32947 {ECO:0000313|EMBL:EAW77076.1}; 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 {ECO:0000313|EMBL:CAG46887.1}; RN [1] {ECO:0000313|EMBL:EAW77076.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:CAG46887.1} RP NUCLEOTIDE SEQUENCE. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EAW77076.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton 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 -!- FUNCTION: Binds free fatty acids and their coenzyme A derivatives, CC bilirubin, and some other small molecules in the cytoplasm. Involved in CC intracellular lipid transport. {ECO:0000256|RuleBase:RU369022}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC 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}. 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; CR542090; CAG46887.1; -; mRNA. DR EMBL; CH471215; EAW77076.1; -; Genomic_DNA. DR RefSeq; NP_001434.1; NM_001443.3. DR AlphaFoldDB; Q6FGL7; -. DR SMR; Q6FGL7; -. DR Antibodypedia; 3707; 737 antibodies from 43 providers. DR DNASU; 2168; -. DR GeneID; 2168; -. DR KEGG; hsa:2168; -. DR UCSC; uc002sst.3; human. DR ClinPGx; PA27956; -. DR CTD; 2168; -. DR DisGeNET; 2168; -. DR VEuPathDB; HostDB:ENSG00000163586; -. DR HOGENOM; CLU_113772_4_2_1; -. DR OMA; GKYQVQT; -. DR OrthoDB; 9971011at2759; -. DR BioGRID-ORCS; 2168; 8 hits in 1149 CRISPR screens. DR ChiTaRS; FABP1; human. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0015485; F:cholesterol binding; IEA:Ensembl. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0005504; F:fatty acid binding; IEA:UniProtKB-UniRule. DR GO; GO:0120013; F:lipid transfer activity; IEA:Ensembl. DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IEA:Ensembl. DR GO; GO:0015908; P:fatty acid transport; IEA:UniProtKB-UniRule. DR CDD; cd19444; FABP1; 1. DR FunFam; 2.40.128.20:FF:000006; Fatty acid-binding protein, liver; 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 Pfam; PF14651; Lipocalin_7; 1. DR PRINTS; PR00178; FATTYACIDBP. DR SUPFAM; SSF50814; Lipocalins; 1. DR PROSITE; PS00214; FABP; 1. PE 2: Evidence at transcript level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369022}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121, KW ECO:0000256|RuleBase:RU369022}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU369022}. FT DOMAIN 5..22 FT /note="Cytosolic fatty-acid binding proteins" FT /evidence="ECO:0000259|PROSITE:PS00214" FT NON_TER 127 FT /evidence="ECO:0000313|EMBL:CAG46887.1" SQ SEQUENCE 127 AA; 14208 MW; 065DCEFB08DAB6B6 CRC64; MSFSGKYQLQ SQENFEAFMK AIGLPEELIQ KGKDIKGVSE IVQNGKHFKF TITAGSKVIQ NEFTVGEECE LETMTGEKVK TVVQLEGDNK LVTTFKNIKS VTELNGDIIT NTMTLGDIVF KRISKRI //