ID   FABP4_HUMAN             Reviewed;         132 AA.
AC   P15090; Q6IBA1;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-JAN-2012, entry version 123.
DE   RecName: Full=Fatty acid-binding protein, adipocyte;
DE   AltName: Full=Adipocyte lipid-binding protein;
DE            Short=ALBP;
DE   AltName: Full=Adipocyte-type fatty acid-binding protein;
DE            Short=A-FABP;
DE            Short=AFABP;
DE   AltName: Full=Fatty acid-binding protein 4;
GN   Name=FABP4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90105397; PubMed=2481498; DOI=10.1021/bi00448a003;
RA   Baxa C.A., Sha R.S., Buelt M.K., Smith A.J., Matarese V.,
RA   Chinander L.L., Boundy K.L., Bernlohr D.A.;
RT   "Human adipocyte lipid-binding protein: purification of the protein
RT   and cloning of its complementary DNA.";
RL   Biochemistry 28:8683-8690(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Urinary bladder;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-23.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYNTHETIC
RP   INHIBITOR.
RX   PubMed=15357969; DOI=10.1016/j.bmcl.2004.06.057;
RA   Lehmann F., Haile S., Axen E., Medina C., Uppenberg J., Svensson S.,
RA   Lundbaeck T., Rondahl L., Barf T.;
RT   "Discovery of inhibitors of human adipocyte fatty acid-binding
RT   protein, a potential type 2 diabetes target.";
RL   Bioorg. Med. Chem. Lett. 14:4445-4448(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID,
RP   SUBUNIT, PARTIAL PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX   PubMed=17077479; DOI=10.1107/S1744309106038656;
RA   Marr E., Tardie M., Carty M., Brown Phillips T., Wang I.-K.,
RA   Soeller W., Qiu X., Karam G.;
RT   "Expression, purification, crystallization and structure of human
RT   adipocyte lipid-binding protein (aP2).";
RL   Acta Crystallogr. F 62:1058-1060(2006).
CC   -!- FUNCTION: Lipid transport protein in adipocytes. Binds both long
CC       chain fatty acids and retinoic acid. Delivers long-chain fatty
CC       acids and retinoic acid to their cognate receptors in the nucleus
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with PPARG (By similarity). Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Depending on the
CC       nature of the ligand, a conformation change exposes a nuclear
CC       localization motif and the protein is transported into the
CC       nucleus. Subject to constitutive nuclear export (By similarity).
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates
CC       hydrophobic ligands in its interior.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family.
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DR   EMBL; J02874; AAA51689.1; -; mRNA.
DR   EMBL; BT006809; AAP35455.1; -; mRNA.
DR   EMBL; CR456903; CAG33184.1; -; mRNA.
DR   EMBL; CH471068; EAW87092.1; -; Genomic_DNA.
DR   EMBL; BC003672; AAH03672.1; -; mRNA.
DR   IPI; IPI00215746; -.
DR   PIR; A33363; FZHUF.
DR   RefSeq; NP_001433.1; NM_001442.2.
DR   UniGene; Hs.391561; -.
DR   PDB; 1TOU; X-ray; 2.00 A; A=2-131.
DR   PDB; 1TOW; X-ray; 2.00 A; A=2-132.
DR   PDB; 2HNX; X-ray; 1.50 A; A=1-132.
DR   PDB; 2NNQ; X-ray; 1.80 A; A=2-131.
DR   PDB; 3FR2; X-ray; 2.20 A; A=2-132.
DR   PDB; 3FR4; X-ray; 2.16 A; A=1-132.
DR   PDB; 3FR5; X-ray; 2.20 A; A=2-132.
DR   PDB; 3P6C; X-ray; 1.25 A; A=1-132.
DR   PDB; 3P6D; X-ray; 1.06 A; A=1-132.
DR   PDB; 3P6E; X-ray; 1.08 A; A=1-132.
DR   PDB; 3P6F; X-ray; 1.20 A; A=1-132.
DR   PDB; 3P6G; X-ray; 1.20 A; A=1-132.
DR   PDB; 3P6H; X-ray; 1.15 A; A=1-132.
DR   PDB; 3Q6L; X-ray; 1.40 A; A=1-132.
DR   PDB; 3RZY; X-ray; 1.08 A; A=1-132.
DR   PDBsum; 1TOU; -.
DR   PDBsum; 1TOW; -.
DR   PDBsum; 2HNX; -.
DR   PDBsum; 2NNQ; -.
DR   PDBsum; 3FR2; -.
DR   PDBsum; 3FR4; -.
DR   PDBsum; 3FR5; -.
DR   PDBsum; 3P6C; -.
DR   PDBsum; 3P6D; -.
DR   PDBsum; 3P6E; -.
DR   PDBsum; 3P6F; -.
DR   PDBsum; 3P6G; -.
DR   PDBsum; 3P6H; -.
DR   PDBsum; 3Q6L; -.
DR   PDBsum; 3RZY; -.
DR   ProteinModelPortal; P15090; -.
DR   SMR; P15090; 1-132.
DR   IntAct; P15090; 2.
DR   MINT; MINT-1398507; -.
DR   STRING; P15090; -.
DR   PhosphoSite; P15090; -.
DR   DMDM; 119781; -.
DR   UCD-2DPAGE; P15090; -.
DR   PeptideAtlas; P15090; -.
DR   PRIDE; P15090; -.
DR   Ensembl; ENST00000256104; ENSP00000256104; ENSG00000170323.
DR   GeneID; 2167; -.
DR   KEGG; hsa:2167; -.
DR   UCSC; uc003ycd.2; human.
DR   CTD; 2167; -.
DR   GeneCards; GC08M082390; -.
DR   H-InvDB; HIX0201305; -.
DR   HGNC; HGNC:3559; FABP4.
DR   HPA; CAB024961; -.
DR   HPA; HPA002188; -.
DR   MIM; 600434; gene.
DR   neXtProt; NX_P15090; -.
DR   PharmGKB; PA27960; -.
DR   GeneTree; ENSGT00560000076791; -.
DR   HOGENOM; HBG714759; -.
DR   HOVERGEN; HBG005633; -.
DR   InParanoid; P15090; -.
DR   OMA; GQEFDEI; -.
DR   OrthoDB; EOG4QC16R; -.
DR   PhylomeDB; P15090; -.
DR   Reactome; REACT_111045; Developmental Biology.
DR   Reactome; REACT_22258; Metabolism of lipids and lipoproteins.
DR   NextBio; 8751; -.
DR   ArrayExpress; P15090; -.
DR   Bgee; P15090; -.
DR   CleanEx; HS_FABP4; -.
DR   Genevestigator; P15090; -.
DR   GermOnline; ENSG00000170323; Homo sapiens.
DR   GO; GO:0005811; C:lipid particle; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005625; C:soluble fraction; TAS:ProtInc.
DR   GO; GO:0005504; F:fatty acid binding; TAS:ProtInc.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR011038; Calycin-like.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   Gene3D; G3DSA:2.40.128.20; Calycin; 1.
DR   KO; K08753; -.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Calycin; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Lipid-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    132       Fatty acid-binding protein, adipocyte.
FT                                /FTId=PRO_0000067366.
FT   REGION      127    129       Fatty acid binding.
FT   MOTIF        22     32       Nuclear localization signal (By
FT                                similarity).
FT   MOD_RES      20     20       Phosphotyrosine; by Tyr-kinases (By
FT                                similarity).
FT   VARIANT      23     23       E -> D (in a breast cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036320.
FT   STRAND        7     16
FT   HELIX        17     24
FT   HELIX        28     36
FT   STRAND       40     46
FT   STRAND       49     55
FT   STRAND       61     66
FT   STRAND       71     74
FT   STRAND       80     88
FT   STRAND       91     98
FT   STRAND      101    110
FT   STRAND      113    120
FT   STRAND      123    131
SQ   SEQUENCE   132 AA;  14719 MW;  819D788FF4BF7235 CRC64;
     MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIKSESTFKN
     TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG KSTTIKRKRE DDKLVVECVM
     KGVTSTRVYE RA
//