ACO12_HUMAN
ID ACO12_HUMAN Reviewed; 555 AA.
AC Q8WYK0; B3KVK9; Q5FWE9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Acetyl-coenzyme A thioesterase {ECO:0000305};
DE EC=3.1.2.1 {ECO:0000269|PubMed:16951743};
DE AltName: Full=Acyl-CoA thioester hydrolase 12;
DE AltName: Full=Acyl-coenzyme A thioesterase 12;
DE Short=Acyl-CoA thioesterase 12;
DE AltName: Full=Cytoplasmic acetyl-CoA hydrolase 1;
DE Short=CACH-1;
DE Short=hCACH-1;
DE AltName: Full=START domain-containing protein 15;
DE Short=StARD15;
GN Name=ACOT12; Synonyms=CACH, CACH1, STARD15;
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), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=16951743;
RA Suematsu N., Isohashi F.;
RT "Molecular cloning and functional expression of human cytosolic acetyl-CoA
RT hydrolase.";
RL Acta Biochim. Pol. 53:553-561(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
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.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Chondrosarcoma;
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 [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-316 IN COMPLEX WITH COENZYME A.
RG Structural genomics consortium (SGC);
RT "Human acyl-coenzyme A thioesterase 12.";
RL Submitted (NOV-2007) to the PDB data bank.
RN [8]
RP VARIANT HIS-190.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (PubMed:16951743). Preferentially hydrolyzes acetyl-CoA
CC (PubMed:16951743). {ECO:0000269|PubMed:16951743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1;
CC Evidence={ECO:0000269|PubMed:16951743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
CC Evidence={ECO:0000305|PubMed:16951743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+);
CC Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371;
CC Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate;
CC Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC -!- ACTIVITY REGULATION: Inhibited by ADP. Active in the presence of ATP
CC (PubMed:16951743). Cold labile, it dissociates into inactive monomers
CC at low temperature (By similarity). {ECO:0000250|UniProtKB:Q99NB7,
CC ECO:0000269|PubMed:16951743}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for acetyl-CoA {ECO:0000269|PubMed:16951743};
CC Note=kcat is 7000 sec(-1) for the hydrolysis of acetyl-CoA.
CC {ECO:0000269|PubMed:16951743};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:16951743}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250|UniProtKB:Q99NB7}.
CC -!- INTERACTION:
CC Q8WYK0; Q8WYK0: ACOT12; NbExp=3; IntAct=EBI-11954993, EBI-11954993;
CC Q8WYK0; O00154-4: ACOT7; NbExp=3; IntAct=EBI-11954993, EBI-12007918;
CC Q8WYK0; P50221: MEOX1; NbExp=3; IntAct=EBI-11954993, EBI-2864512;
CC Q8WYK0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11954993, EBI-16439278;
CC Q8WYK0; P41227: NAA10; NbExp=3; IntAct=EBI-11954993, EBI-747693;
CC Q8WYK0; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-11954993, EBI-2585120;
CC Q8WYK0; Q02548: PAX5; NbExp=3; IntAct=EBI-11954993, EBI-296331;
CC Q8WYK0; P26367: PAX6; NbExp=3; IntAct=EBI-11954993, EBI-747278;
CC Q8WYK0; Q04864-2: REL; NbExp=3; IntAct=EBI-11954993, EBI-10829018;
CC Q8WYK0; Q96BR9: ZBTB8A; NbExp=4; IntAct=EBI-11954993, EBI-742740;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16951743}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WYK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WYK0-2; Sequence=VSP_055785, VSP_055786;
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DR EMBL; AB078619; BAB84022.1; -; mRNA.
DR EMBL; AK122960; BAG53821.1; -; mRNA.
DR EMBL; AC008411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95875.1; -; Genomic_DNA.
DR EMBL; BC089437; AAH89437.1; -; mRNA.
DR EMBL; BC075010; AAH75010.1; -; mRNA.
DR EMBL; BC075011; AAH75011.1; -; mRNA.
DR CCDS; CCDS4055.1; -. [Q8WYK0-1]
DR RefSeq; NP_570123.1; NM_130767.2. [Q8WYK0-1]
DR PDB; 3B7K; X-ray; 2.70 A; A/B/C=7-316.
DR PDB; 4MOB; X-ray; 2.40 A; A=7-336.
DR PDB; 4MOC; X-ray; 2.50 A; A=7-336.
DR PDBsum; 3B7K; -.
DR PDBsum; 4MOB; -.
DR PDBsum; 4MOC; -.
DR AlphaFoldDB; Q8WYK0; -.
DR SMR; Q8WYK0; -.
DR BioGRID; 126405; 15.
DR IntAct; Q8WYK0; 14.
DR STRING; 9606.ENSP00000303246; -.
DR SwissLipids; SLP:000001187; -.
DR TCDB; 9.B.371.2.1; the paai thioesterase (pte) family.
DR iPTMnet; Q8WYK0; -.
DR PhosphoSitePlus; Q8WYK0; -.
DR BioMuta; ACOT12; -.
DR DMDM; 25008183; -.
DR jPOST; Q8WYK0; -.
DR MassIVE; Q8WYK0; -.
DR PaxDb; Q8WYK0; -.
DR PeptideAtlas; Q8WYK0; -.
DR PRIDE; Q8WYK0; -.
DR ProteomicsDB; 62810; -.
DR ProteomicsDB; 75162; -. [Q8WYK0-1]
DR Antibodypedia; 24697; 177 antibodies from 24 providers.
DR DNASU; 134526; -.
DR Ensembl; ENST00000307624.8; ENSP00000303246.3; ENSG00000172497.9. [Q8WYK0-1]
DR Ensembl; ENST00000513751.1; ENSP00000421628.1; ENSG00000172497.9. [Q8WYK0-2]
DR GeneID; 134526; -.
DR KEGG; hsa:134526; -.
DR MANE-Select; ENST00000307624.8; ENSP00000303246.3; NM_130767.3; NP_570123.1.
DR UCSC; uc003khl.5; human. [Q8WYK0-1]
DR CTD; 134526; -.
DR DisGeNET; 134526; -.
DR GeneCards; ACOT12; -.
DR HGNC; HGNC:24436; ACOT12.
DR HPA; ENSG00000172497; Tissue enriched (liver).
DR MIM; 614315; gene.
DR neXtProt; NX_Q8WYK0; -.
DR OpenTargets; ENSG00000172497; -.
DR PharmGKB; PA142672657; -.
DR VEuPathDB; HostDB:ENSG00000172497; -.
DR eggNOG; KOG2763; Eukaryota.
DR GeneTree; ENSGT00940000160328; -.
DR HOGENOM; CLU_035725_0_0_1; -.
DR InParanoid; Q8WYK0; -.
DR OMA; CTVSYLN; -.
DR OrthoDB; 776852at2759; -.
DR PhylomeDB; Q8WYK0; -.
DR TreeFam; TF328368; -.
DR BRENDA; 3.1.2.1; 2681.
DR PathwayCommons; Q8WYK0; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; Q8WYK0; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 134526; 96 hits in 1062 CRISPR screens.
DR ChiTaRS; ACOT12; human.
DR EvolutionaryTrace; Q8WYK0; -.
DR GeneWiki; ACOT12; -.
DR GenomeRNAi; 134526; -.
DR Pharos; Q8WYK0; Tbio.
DR PRO; PR:Q8WYK0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8WYK0; protein.
DR Bgee; ENSG00000172497; Expressed in right lobe of liver and 65 other tissues.
DR Genevisible; Q8WYK0; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; ISS:HGNC-UCL.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:Ensembl.
DR GO; GO:0006637; P:acyl-CoA metabolic process; ISS:HGNC-UCL.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR040170; Cytosol_ACT.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR11049; PTHR11049; 1.
DR Pfam; PF03061; 4HBT; 2.
DR Pfam; PF01852; START; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Fatty acid metabolism;
KW Hydrolase; Lipid metabolism; Reference proteome; Repeat; Serine esterase.
FT CHAIN 1..555
FT /note="Acetyl-coenzyme A thioesterase"
FT /id="PRO_0000053809"
FT DOMAIN 5..117
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 179..294
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 340..549
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT BINDING 53..55
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 82..84
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 144
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 234..236
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT MOD_RES 33
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT MOD_RES 159
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT MOD_RES 228
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT VAR_SEQ 166..167
FT /note="DL -> GQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055785"
FT VAR_SEQ 168..555
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055786"
FT VARIANT 190
FT /note="L -> H (found in a clear cell renal carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064691"
FT VARIANT 230
FT /note="V -> I (in dbSNP:rs34607174)"
FT /id="VAR_048192"
FT VARIANT 403
FT /note="A -> T (in dbSNP:rs10371)"
FT /id="VAR_048193"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:4MOB"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4MOB"
FT HELIX 28..47
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 69..80
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 82..95
FT /evidence="ECO:0007829|PDB:4MOB"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 101..113
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4MOB"
FT HELIX 131..160
FT /evidence="ECO:0007829|PDB:4MOB"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4MOB"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:4MOB"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:4MOB"
FT HELIX 202..221
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 244..255
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:4MOB"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 279..291
FT /evidence="ECO:0007829|PDB:4MOB"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4MOC"
FT HELIX 308..325
FT /evidence="ECO:0007829|PDB:4MOB"
SQ SEQUENCE 555 AA; 62034 MW; 707560D55504732C CRC64;
MERPAPGEVV MSQAIQPAHA TARGELSAGQ LLKWIDTTAC LAAEKHAGVS CVTASVDDIQ
FEETARVGQV ITIKAKVTRA FSTSMEISIK VMVQDMLTGI EKLVSVAFST FVAKPVGKEK
IHLKPVTLLT EQDHVEHNLA AERRKVRLQH EDTFNNLMKE SSKFDDLIFD EEEGAVSTRG
TSVQSIELVL PPHANHHGNT FGGQIMAWME TVATISASRL CWAHPFLKSV DMFKFRGPST
VGDRLVFTAI VNNTFQTCVE VGVRVEAFDC QEWAEGRGRH INSAFLIYNA ADDKENLITF
PRIQPISKDD FRRYRGAIAR KRIRLGRKYV ISHKEEVPLC IHWDISKQAS LSDSNVEALK
KLAAKRGWEV TSTVEKIKIY TLEEHDVLSV WVEKHVGSPA HLAYRLLSDF TKRPLWDPHF
VSCEVIDWVS EDDQLYHITC PILNDDKPKD LVVLVSRRKP LKDGNTYTVA VKSVILPSVP
PSPQYIRSEI ICAGFLIHAI DSNSCIVSYF NHMSASILPY FAGNLGGWSK SIEETAASCI
QFLENPPDDG FVSTF
