THIK_HUMAN
ID THIK_HUMAN Reviewed; 424 AA.
AC P09110; G5E935; Q96CA6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=3-ketoacyl-CoA thiolase, peroxisomal {ECO:0000305};
DE EC=2.3.1.16 {ECO:0000305|PubMed:2882519};
DE AltName: Full=Acetyl-CoA C-myristoyltransferase;
DE EC=2.3.1.155 {ECO:0000305|PubMed:2882519};
DE AltName: Full=Acetyl-CoA acyltransferase;
DE EC=2.3.1.9 {ECO:0000250|UniProtKB:P21775};
DE AltName: Full=Beta-ketothiolase;
DE AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase {ECO:0000303|PubMed:2882519};
DE Flags: Precursor;
GN Name=ACAA1 {ECO:0000312|HGNC:HGNC:82}; Synonyms=ACAA, PTHIO;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3194209; DOI=10.1093/nar/16.21.10369;
RA Bout A., Teunissen Y., Hashimoto T., Benne R., Tager J.M.;
RT "Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase.";
RL Nucleic Acids Res. 16:10369-10369(1988).
RN [2]
RP SEQUENCE REVISION TO 285-287.
RA Bout A.;
RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=2726492; DOI=10.1093/nar/17.9.3588;
RA Fairbairn L.J., Tanner M.J.A.;
RT "Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA
RT thiolase.";
RL Nucleic Acids Res. 17:3588-3588(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1679347; DOI=10.1016/0167-4781(91)90035-k;
RA Bout A., Franse M.M., Collins J., Blonden L., Tager J.M., Benne R.;
RT "Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA
RT thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient
RT patient.";
RL Biochim. Biophys. Acta 1090:43-51(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-387.
RC TISSUE=Lymph, Ovary, and Pancreas;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=2882519; DOI=10.1073/pnas.84.8.2494;
RA Schram A.W., Goldfischer S., van Roermund C.W., Brouwer-Kelder E.M.,
RA Collins J., Hashimoto T., Heymans H.S., van den Bosch H., Schutgens R.B.,
RA Tager J.M.;
RT "Human peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2494-2496(1987).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11734571;
RA Ferdinandusse S., Denis S., Mooijer P.A., Zhang Z., Reddy J.K.,
RA Spector A.A., Wanders R.J.;
RT "Identification of the peroxisomal beta-oxidation enzymes involved in the
RT biosynthesis of docosahexaenoic acid.";
RL J. Lipid Res. 42:1987-1995(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND THR-60, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER CYS-26, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 28-424, AND SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human peroxisomal acetyl-COA acyl transferase 1
RT (ACAA1).";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Responsible for the thiolytic cleavage of straight chain 3-
CC keto fatty acyl-CoAs (3-oxoacyl-CoAs) (Probable). Plays an important
CC role in fatty acid peroxisomal beta-oxidation (Probable). Catalyzes the
CC cleavage of short, medium, long, and very long straight chain 3-
CC oxoacyl-CoAs (Probable). {ECO:0000305|PubMed:11734571,
CC ECO:0000305|PubMed:2882519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155;
CC Evidence={ECO:0000305|PubMed:2882519};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000305|PubMed:2882519};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:62619, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA +
CC tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC Evidence={ECO:0000250|UniProtKB:P21775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + CoA =
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + acetyl-CoA;
CC Xref=Rhea:RHEA:39131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74298, ChEBI:CHEBI:74304;
CC Evidence={ECO:0000305|PubMed:11734571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39132;
CC Evidence={ECO:0000305|PubMed:11734571};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:11734571, ECO:0000305|PubMed:2882519}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.14}.
CC -!- INTERACTION:
CC P09110; Q9BSK4: FEM1A; NbExp=3; IntAct=EBI-3926709, EBI-2515349;
CC P09110; Q12800: TFCP2; NbExp=3; IntAct=EBI-3926709, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P21775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P09110-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09110-2; Sequence=VSP_046195, VSP_046196;
CC -!- INDUCTION: Peroxisomal thiolase is markedly induced (at the level of
CC transcription) by various hypolipidemic compounds in parallel with the
CC other two enzymes of the peroxisomal beta-oxidation system.
CC {ECO:0000250|UniProtKB:P21775}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; X12966; CAA31412.1; -; mRNA.
DR EMBL; X14813; CAA32918.1; -; mRNA.
DR EMBL; X65140; CAA46270.1; -; Genomic_DNA.
DR EMBL; X65148; CAA46271.1; -; Genomic_DNA.
DR EMBL; AP006309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64516.1; -; Genomic_DNA.
DR EMBL; BC000635; AAH00635.1; -; mRNA.
DR EMBL; BC011977; AAH11977.1; -; mRNA.
DR EMBL; BC014474; AAH14474.1; -; mRNA.
DR CCDS; CCDS2673.1; -. [P09110-1]
DR CCDS; CCDS46794.1; -. [P09110-2]
DR PIR; S17515; XUHUAB.
DR RefSeq; NP_001123882.1; NM_001130410.1. [P09110-2]
DR RefSeq; NP_001598.1; NM_001607.3. [P09110-1]
DR PDB; 2IIK; X-ray; 2.55 A; A/B=30-423.
DR PDBsum; 2IIK; -.
DR AlphaFoldDB; P09110; -.
DR SMR; P09110; -.
DR BioGRID; 106548; 85.
DR IntAct; P09110; 17.
DR MINT; P09110; -.
DR STRING; 9606.ENSP00000333664; -.
DR CarbonylDB; P09110; -.
DR iPTMnet; P09110; -.
DR MetOSite; P09110; -.
DR PhosphoSitePlus; P09110; -.
DR SwissPalm; P09110; -.
DR BioMuta; ACAA1; -.
DR DMDM; 135751; -.
DR REPRODUCTION-2DPAGE; IPI00012828; -.
DR UCD-2DPAGE; P09110; -.
DR EPD; P09110; -.
DR jPOST; P09110; -.
DR MassIVE; P09110; -.
DR MaxQB; P09110; -.
DR PaxDb; P09110; -.
DR PeptideAtlas; P09110; -.
DR PRIDE; P09110; -.
DR ProteomicsDB; 33816; -.
DR ProteomicsDB; 52200; -. [P09110-1]
DR Antibodypedia; 1631; 334 antibodies from 33 providers.
DR DNASU; 30; -.
DR Ensembl; ENST00000301810.11; ENSP00000301810.7; ENSG00000060971.19. [P09110-2]
DR Ensembl; ENST00000333167.13; ENSP00000333664.8; ENSG00000060971.19. [P09110-1]
DR GeneID; 30; -.
DR KEGG; hsa:30; -.
DR MANE-Select; ENST00000333167.13; ENSP00000333664.8; NM_001607.4; NP_001598.1.
DR UCSC; uc003cht.4; human. [P09110-1]
DR CTD; 30; -.
DR DisGeNET; 30; -.
DR GeneCards; ACAA1; -.
DR HGNC; HGNC:82; ACAA1.
DR HPA; ENSG00000060971; Group enriched (kidney, liver).
DR MIM; 604054; gene.
DR neXtProt; NX_P09110; -.
DR OpenTargets; ENSG00000060971; -.
DR PharmGKB; PA24419; -.
DR VEuPathDB; HostDB:ENSG00000060971; -.
DR eggNOG; KOG1389; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR InParanoid; P09110; -.
DR OMA; DYYWGMG; -.
DR PhylomeDB; P09110; -.
DR TreeFam; TF332308; -.
DR BioCyc; MetaCyc:HS00752-MON; -.
DR PathwayCommons; P09110; -.
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR Reactome; R-HSA-9033500; TYSND1 cleaves peroxisomal proteins.
DR SignaLink; P09110; -.
DR UniPathway; UPA00661; -.
DR BioGRID-ORCS; 30; 19 hits in 1087 CRISPR screens.
DR ChiTaRS; ACAA1; human.
DR EvolutionaryTrace; P09110; -.
DR GeneWiki; ACAA1; -.
DR GenomeRNAi; 30; -.
DR Pharos; P09110; Tbio.
DR PRO; PR:P09110; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P09110; protein.
DR Bgee; ENSG00000060971; Expressed in jejunal mucosa and 204 other tissues.
DR ExpressionAtlas; P09110; baseline and differential.
DR Genevisible; P09110; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0008775; F:acetate CoA-transferase activity; EXP:Reactome.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IMP:UniProtKB.
DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
DR GO; GO:0008206; P:bile acid metabolic process; IMP:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:UniProtKB.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Fatty acid metabolism;
KW Lipid metabolism; Peroxisome; Phosphoprotein; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Peroxisome"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 27..424
FT /note="3-ketoacyl-CoA thiolase, peroxisomal"
FT /id="PRO_0000034067"
FT ACT_SITE 123
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 408
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 149..181
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046195"
FT VAR_SEQ 272..331
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046196"
FT VARIANT 172
FT /note="E -> D (in dbSNP:rs156265)"
FT /id="VAR_011904"
FT VARIANT 387
FT /note="V -> A (in dbSNP:rs2229528)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_069148"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:2IIK"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2IIK"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:2IIK"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 196..216
FT /evidence="ECO:0007829|PDB:2IIK"
FT TURN 217..222
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:2IIK"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:2IIK"
FT HELIX 382..397
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 401..409
FT /evidence="ECO:0007829|PDB:2IIK"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:2IIK"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:2IIK"
SQ SEQUENCE 424 AA; 44292 MW; 71B2BBAFA06AE412 CRC64;
MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR AGRGGFKDTT
PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM ARIAQFLSDI PETVPLSTVN
RQCSSGLQAV ASIAGGIRNG SYDIGMACGV ESMSLADRGN PGNITSRLME KEKARDCLIP
MGITSENVAE RFGISREKQD TFALASQQKA ARAQSKGCFQ AEIVPVTTTV HDDKGTKRSI
TVTQDEGIRP STTMEGLAKL KPAFKKDGST TAGNSSQVSD GAAAILLARR SKAEELGLPI
LGVLRSYAVV GVPPDIMGIG PAYAIPVALQ KAGLTVSDVD IFEINEAFAS QAAYCVEKLR
LPPEKVNPLG GAVALGHPLG CTGARQVITL LNELKRRGKR AYGVVSMCIG TGMGAAAVFE
YPGN
