ID   FABD_HUMAN              Reviewed;         390 AA.
AC   Q8IVS2; B0QY72; O95510; O95511;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Malonyl-CoA-acyl carrier protein transacylase, mitochondrial {ECO:0000305};
DE            Short=MCT;
DE            EC=2.3.1.39 {ECO:0000269|PubMed:12882974};
DE   AltName: Full=Mitochondrial malonyl CoA:ACP acyltransferase;
DE   AltName: Full=Mitochondrial malonyltransferase;
DE   AltName: Full=[Acyl-carrier-protein] malonyltransferase;
DE   Flags: Precursor;
GN   Name=MCAT {ECO:0000312|HGNC:HGNC:29622}; Synonyms=MT;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=12529303; DOI=10.1101/gr.695703;
RA   Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA   Bye J.M., Beare D.M., Dunham I.;
RT   "Reevaluating human gene annotation: a second-generation analysis of
RT   chromosome 22.";
RL   Genome Res. 13:27-36(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Caudate nucleus;
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=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   GLY-303.
RC   TISSUE=Testis;
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   FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=12882974; DOI=10.1074/jbc.m306121200;
RA   Zhang L., Joshi A.K., Smith S.;
RT   "Cloning, expression, characterization, and interaction of two components
RT   of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl
RT   carrier protein.";
RL   J. Biol. Chem. 278:40067-40074(2003).
RN   [7]
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   [8]
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   [9]
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   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 60-375.
RG   Structural genomics consortium (SGC);
RT   "Structure of human mitochondrial malonyltransferase.";
RL   Submitted (SEP-2005) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the transfer of a malonyl moiety from malonyl-CoA
CC       to the free thiol group of the phosphopantetheine arm of the
CC       mitochondrial ACP protein (NDUFAB1). This suggests the existence of the
CC       biosynthesis of fatty acids in mitochondria.
CC       {ECO:0000269|PubMed:12882974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000269|PubMed:12882974};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC         Evidence={ECO:0000305|PubMed:12882974};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12882974}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IVS2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IVS2-2; Sequence=VSP_010517, VSP_010518;
CC   -!- SIMILARITY: Belongs to the type II malonyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL359401; CAB94789.1; -; mRNA.
DR   EMBL; AL359403; CAB94790.1; -; mRNA.
DR   EMBL; AK314059; BAG36765.1; -; mRNA.
DR   EMBL; AL022237; CAQ07851.1; -; Genomic_DNA.
DR   EMBL; AL022237; CAA18261.1; -; Genomic_DNA.
DR   EMBL; CH471138; EAW73286.1; -; Genomic_DNA.
DR   EMBL; BC030985; AAH30985.1; -; mRNA.
DR   EMBL; BC042195; AAH42195.2; -; mRNA.
DR   CCDS; CCDS14045.1; -. [Q8IVS2-2]
DR   CCDS; CCDS33660.1; -. [Q8IVS2-1]
DR   RefSeq; NP_055322.1; NM_014507.3. [Q8IVS2-2]
DR   RefSeq; NP_775738.3; NM_173467.4. [Q8IVS2-1]
DR   PDB; 2C2N; X-ray; 1.55 A; A/B=60-375.
DR   PDB; 8CSP; EM; 2.66 A; 8=1-390.
DR   PDB; 8CSQ; EM; 2.54 A; 8=1-390.
DR   PDB; 8CSR; EM; 2.54 A; 8=1-390.
DR   PDB; 8CSS; EM; 2.36 A; 8=1-390.
DR   PDBsum; 2C2N; -.
DR   PDBsum; 8CSP; -.
DR   PDBsum; 8CSQ; -.
DR   PDBsum; 8CSR; -.
DR   PDBsum; 8CSS; -.
DR   AlphaFoldDB; Q8IVS2; -.
DR   EMDB; EMD-26966; -.
DR   EMDB; EMD-26967; -.
DR   EMDB; EMD-26968; -.
DR   EMDB; EMD-26969; -.
DR   SMR; Q8IVS2; -.
DR   BioGRID; 118161; 139.
DR   IntAct; Q8IVS2; 23.
DR   MINT; Q8IVS2; -.
DR   STRING; 9606.ENSP00000290429; -.
DR   DrugBank; DB07344; 3,6,9,12,15-PENTAOXAHEPTADECAN-1-OL.
DR   SwissLipids; SLP:000001251; -.
DR   GlyGen; Q8IVS2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8IVS2; -.
DR   PhosphoSitePlus; Q8IVS2; -.
DR   SwissPalm; Q8IVS2; -.
DR   BioMuta; MCAT; -.
DR   DMDM; 48428076; -.
DR   EPD; Q8IVS2; -.
DR   jPOST; Q8IVS2; -.
DR   MassIVE; Q8IVS2; -.
DR   MaxQB; Q8IVS2; -.
DR   PaxDb; 9606-ENSP00000290429; -.
DR   PeptideAtlas; Q8IVS2; -.
DR   ProteomicsDB; 70755; -. [Q8IVS2-1]
DR   ProteomicsDB; 70756; -. [Q8IVS2-2]
DR   Pumba; Q8IVS2; -.
DR   Antibodypedia; 27475; 254 antibodies from 23 providers.
DR   DNASU; 27349; -.
DR   Ensembl; ENST00000290429.11; ENSP00000290429.5; ENSG00000100294.13. [Q8IVS2-1]
DR   Ensembl; ENST00000327555.5; ENSP00000331306.5; ENSG00000100294.13. [Q8IVS2-2]
DR   GeneID; 27349; -.
DR   KEGG; hsa:27349; -.
DR   MANE-Select; ENST00000290429.11; ENSP00000290429.5; NM_173467.5; NP_775738.3.
DR   UCSC; uc003bdl.2; human. [Q8IVS2-1]
DR   AGR; HGNC:29622; -.
DR   DisGeNET; 27349; -.
DR   GeneCards; MCAT; -.
DR   HGNC; HGNC:29622; MCAT.
DR   HPA; ENSG00000100294; Low tissue specificity.
DR   MalaCards; MCAT; -.
DR   MIM; 614479; gene.
DR   neXtProt; NX_Q8IVS2; -.
DR   OpenTargets; ENSG00000100294; -.
DR   Orphanet; 98676; Autosomal recessive isolated optic atrophy.
DR   PharmGKB; PA162395058; -.
DR   VEuPathDB; HostDB:ENSG00000100294; -.
DR   eggNOG; KOG2926; Eukaryota.
DR   GeneTree; ENSGT00390000013715; -.
DR   HOGENOM; CLU_030558_2_1_1; -.
DR   InParanoid; Q8IVS2; -.
DR   OMA; AANYNCP; -.
DR   OrthoDB; 2265421at2759; -.
DR   PhylomeDB; Q8IVS2; -.
DR   TreeFam; TF313401; -.
DR   BioCyc; MetaCyc:HS02028-MONOMER; -.
DR   BRENDA; 2.3.1.39; 2681.
DR   PathwayCommons; Q8IVS2; -.
DR   Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   SignaLink; Q8IVS2; -.
DR   SIGNOR; Q8IVS2; -.
DR   UniPathway; UPA00094; -.
DR   BioGRID-ORCS; 27349; 110 hits in 1157 CRISPR screens.
DR   ChiTaRS; MCAT; human.
DR   EvolutionaryTrace; Q8IVS2; -.
DR   GeneWiki; MCAT_(gene); -.
DR   GenomeRNAi; 27349; -.
DR   Pharos; Q8IVS2; Tbio.
DR   PRO; PR:Q8IVS2; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q8IVS2; Protein.
DR   Bgee; ENSG00000100294; Expressed in mucosa of transverse colon and 180 other cell types or tissues.
DR   ExpressionAtlas; Q8IVS2; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; TAS:Reactome.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   PANTHER; PTHR47170; MALONYL-COA ACP TRANSACYLASE, ACP-BINDING; 1.
DR   PANTHER; PTHR47170:SF2; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   Genevisible; Q8IVS2; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..390
FT                   /note="Malonyl-CoA-acyl carrier protein transacylase,
FT                   mitochondrial"
FT                   /id="PRO_0000000589"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250"
FT   MOD_RES         314
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R3F5"
FT   VAR_SEQ         172..180
FT                   /note="LYAVKIRAE -> STVSPEEFL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12529303,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010517"
FT   VAR_SEQ         181..390
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12529303,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010518"
FT   VARIANT         303
FT                   /note="A -> G (in dbSNP:rs13815)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_048183"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   TURN            75..83
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           87..98
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           102..108
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           111..115
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           117..138
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           140..144
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           155..162
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           168..187
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          191..197
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           204..217
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          225..232
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          235..241
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           242..250
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           275..286
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   TURN            300..302
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          303..305
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           309..311
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           312..319
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           326..333
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          344..352
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           353..361
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   HELIX           363..366
FT                   /evidence="ECO:0007829|PDB:2C2N"
FT   STRAND          369..372
FT                   /evidence="ECO:0007829|PDB:2C2N"
SQ   SEQUENCE   390 AA;  42962 MW;  5CAF7AE9DFF36A21 CRC64;
     MSVRVARVAW VRGLGASYRR GASSFPVPPP GAQGVAELLR DATGAEEEAP WAATERRMPG
     QCSVLLFPGQ GSQVVGMGRG LLNYPRVREL YAAARRVLGY DLLELSLHGP QETLDRTVHC
     QPAIFVASLA AVEKLHHLQP SVIENCVAAA GFSVGEFAAL VFAGAMEFAE GLYAVKIRAE
     AMQEASEAVP SGMLSVLGQP QSKFNFACLE AREHCKSLGI ENPVCEVSNY LFPDCRVISG
     HQEALRFLQK NSSKFHFRRT RMLPVSGAFH TRLMEPAVEP LTQALKAVDI KKPLVSVYSN
     VHAHRYRHPG HIHKLLAQQL VSPVKWEQTM HAIYERKKGR GFPQTFEVGP GRQLGAILKS
     CNMQAWKSYS AVDVLQTLEH VDLDPQEPPR
//