FABD_HUMAN
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 03-AUG-2022, entry version 166.
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 PDBsum; 2C2N; -.
DR AlphaFoldDB; Q8IVS2; -.
DR SMR; Q8IVS2; -.
DR BioGRID; 118161; 129.
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; Q8IVS2; -.
DR PeptideAtlas; Q8IVS2; -.
DR PRIDE; Q8IVS2; -.
DR ProteomicsDB; 70755; -. [Q8IVS2-1]
DR ProteomicsDB; 70756; -. [Q8IVS2-2]
DR Antibodypedia; 27475; 227 antibodies from 22 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 CTD; 27349; -.
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; 1037268at2759; -.
DR PhylomeDB; Q8IVS2; -.
DR TreeFam; TF313401; -.
DR BioCyc; MetaCyc:HS02028-MON; -.
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; 98 hits in 1076 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 178 other tissues.
DR ExpressionAtlas; Q8IVS2; baseline and differential.
DR Genevisible; Q8IVS2; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004312; F:fatty acid synthase 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; 3.40.366.10; -; 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 Pfam; PF00698; Acyl_transf_1; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
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 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
