Q8IVS2 (FABD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
Short name=MCT
EC=2.3.1.39

Alternative name(s):
Mitochondrial malonyl CoA:ACP acyltransferase
Mitochondrial malonyltransferase
[Acyl-carrier-protein] malonyltransferase

Gene names

Name:	MCAT
Synonyms:	MT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias. Ref.4
Catalytic activity	Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein]. Ref.4
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subcellular location	Mitochondrion Ref.4.
Sequence similarities	Belongs to the type II malonyltransferase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from direct assay Ref.4. Source: UniProtKB
Cellular_component	mitochondrion Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	[acyl-carrier-protein] S-malonyltransferase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8IVS2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8IVS2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     172-180: LYAVKIRAE → STVSPEEFL
     181-390: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 21

21

Mitochondrion Potential

Chain

22 – 390

369

Malonyl-CoA-acyl carrier protein transacylase, mitochondrial

PRO_0000000589

Sites

Active site

153

1

By similarity

Active site

270

1

By similarity

Natural variations

Alternative sequence

172 – 180

9

LYAVKIRAE → STVSPEEFL in isoform 2.

VSP_010517

Alternative sequence

181 – 390

210

Missing in isoform 2.

VSP_010518

Natural variant

303

1

A → G. Ref.3
Corresponds to variant rs13815 [ dbSNP | Ensembl ].

VAR_048183

Secondary structure

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390

Helix Strand Turn

Details...

Beta strand

63 – 67

5

Turn

75 – 83

9

Helix

87 – 98

12

Helix

102 – 108

7

Helix

111 – 115

5

Helix

117 – 138

22

Helix

140 – 144

5

Beta strand

146 – 151

6

Helix

155 – 162

8

Helix

168 – 187

20

Beta strand

191 – 197

7

Helix

204 – 217

14

Beta strand

225 – 232

8

Beta strand

235 – 241

7

Helix

242 – 250

9

Helix

252 – 255

4

Beta strand

259 – 262

4

Helix

272 – 274

3

Helix

275 – 286

12

Beta strand

294 – 298

5

Turn

300 – 302

3

Beta strand

303 – 305

3

Helix

309 – 311

3

Helix

312 – 319

8

Helix

326 – 333

8

Beta strand

344 – 352

9

Helix

353 – 361

9

Helix

363 – 366

4

Beta strand

369 – 372

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: 5CAF7AE9DFF36A21	FASTA	390	42,962
	10 20 30 40 50 60 MSVRVARVAW VRGLGASYRR GASSFPVPPP GAQGVAELLR DATGAEEEAP WAATERRMPG 70 80 90 100 110 120 QCSVLLFPGQ GSQVVGMGRG LLNYPRVREL YAAARRVLGY DLLELSLHGP QETLDRTVHC 130 140 150 160 170 180 QPAIFVASLA AVEKLHHLQP SVIENCVAAA GFSVGEFAAL VFAGAMEFAE GLYAVKIRAE 190 200 210 220 230 240 AMQEASEAVP SGMLSVLGQP QSKFNFACLE AREHCKSLGI ENPVCEVSNY LFPDCRVISG 250 260 270 280 290 300 HQEALRFLQK NSSKFHFRRT RMLPVSGAFH TRLMEPAVEP LTQALKAVDI KKPLVSVYSN 310 320 330 340 350 360 VHAHRYRHPG HIHKLLAQQL VSPVKWEQTM HAIYERKKGR GFPQTFEVGP GRQLGAILKS 370 380 390 CNMQAWKSYS AVDVLQTLEH VDLDPQEPPR
	Isoform 2 [UniParc]. Checksum: 8DA3FDA905D219C7	FASTA	180	19,176
	10 20 30 40 50 60 MSVRVARVAW VRGLGASYRR GASSFPVPPP GAQGVAELLR DATGAEEEAP WAATERRMPG 70 80 90 100 110 120 QCSVLLFPGQ GSQVVGMGRG LLNYPRVREL YAAARRVLGY DLLELSLHGP QETLDRTVHC 130 140 150 160 170 180 QPAIFVASLA AVEKLHHLQP SVIENCVAAA GFSVGEFAAL VFAGAMEFAE GSTVSPEEFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Reevaluating human gene annotation: a second-generation analysis of chromosome 22." Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I. Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[2]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT GLY-303. Tissue: Testis.
[4]	"Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein." Zhang L., Joshi A.K., Smith S. J. Biol. Chem. 278:40067-40074(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION.
[5]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL359401 mRNA. Translation: CAB94789.1.
AL359403 mRNA. Translation: CAB94790.1.
AL022237 Genomic DNA. Translation: CAA18261.1.
BC030985 mRNA. Translation: AAH30985.1.
BC042195 mRNA. Translation: AAH42195.2.

IPI

IPI00023359.
IPI00163960.

RefSeq

NP_055322.1. NM_014507.3.
NP_775738.3. NM_173467.4.

UniGene

Hs.349111.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C2N	X-ray	1.55	A/B	60-375	[»]

ProteinModelPortal

Q8IVS2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IVS2. 1 interaction.

STRING

9606.ENSP00000290429.

PTM databases

PhosphoSite

Q8IVS2.

Polymorphism databases

DMDM

48428076.

Proteomic databases

PaxDb

Q8IVS2.

PeptideAtlas

Q8IVS2.

PRIDE

Q8IVS2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290429; ENSP00000290429; ENSG00000100294.
ENST00000327555; ENSP00000331306; ENSG00000100294.

GeneID

27349.

KEGG

hsa:27349.

UCSC

uc003bdl.1. human.

Organism-specific databases

CTD

27349.

GeneCards

GC22M043528.

HGNC

HGNC:29622. MCAT.

HPA

HPA035471.

MIM

614479. gene.

neXtProt

NX_Q8IVS2.

PharmGKB

PA162395058.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0331.

HOGENOM

HOG000036504.

HOVERGEN

HBG051540.

InParanoid

Q8IVS2.

KO

K00645.

OMA

NEAYHNK.

Enzyme and pathway databases

UniPathway

UPA00094.

Gene expression databases

ArrayExpress

Q8IVS2.

Bgee

Q8IVS2.

CleanEx

HS_MCAT.

Genevestigator

Q8IVS2.

GermOnline

ENSG00000100294. Homo sapiens.

Family and domain databases

Gene3D

3.40.366.10. 2 hits.

InterPro

IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]

Pfam

PF00698. Acyl_transf_1. 1 hit.
[Graphical view]

SUPFAM

SSF52151. Acyl_Trfase/lysoPlipase. 1 hit.
SSF55048. Malonyl_transacylase_ACP-bd. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8IVS2.

GenomeRNAi

27349.

NextBio

50446.

SOURCE

Search...

Entry information

Entry name

FABD_HUMAN

Accession

Primary (citable) accession number: Q8IVS2
Secondary accession number(s): O95510, O95511

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.