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Q8IVS2

- FABD_HUMAN

UniProt

Q8IVS2 - FABD_HUMAN

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Protein
Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
Gene
MCAT, MT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531 By similarity
Active sitei270 – 2701 By similarity

GO - Molecular functioni

  1. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. transferase activity Source: UniProtKB

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB
  2. metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS02028-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl-CoA-acyl carrier protein transacylase, mitochondrial (EC:2.3.1.39)
Short name:
MCT
Alternative name(s):
Mitochondrial malonyl CoA:ACP acyltransferase
Mitochondrial malonyltransferase
[Acyl-carrier-protein] malonyltransferase
Gene namesi
Name:MCAT
Synonyms:MT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:29622. MCAT.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162395058.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121Mitochondrion Reviewed prediction
Add
BLAST
Chaini22 – 390369Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
PRO_0000000589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei314 – 3141N6-succinyllysine By similarity

Proteomic databases

MaxQBiQ8IVS2.
PaxDbiQ8IVS2.
PeptideAtlasiQ8IVS2.
PRIDEiQ8IVS2.

PTM databases

PhosphoSiteiQ8IVS2.

Expressioni

Gene expression databases

ArrayExpressiQ8IVS2.
BgeeiQ8IVS2.
CleanExiHS_MCAT.
GenevestigatoriQ8IVS2.

Organism-specific databases

HPAiHPA035471.

Interactioni

Protein-protein interaction databases

BioGridi118161. 15 interactions.
IntActiQ8IVS2. 2 interactions.
MINTiMINT-4828919.
STRINGi9606.ENSP00000290429.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 675
Turni75 – 839
Helixi87 – 9812
Helixi102 – 1087
Helixi111 – 1155
Helixi117 – 13822
Helixi140 – 1445
Beta strandi146 – 1516
Helixi155 – 1628
Helixi168 – 18720
Beta strandi191 – 1977
Helixi204 – 21714
Beta strandi225 – 2328
Beta strandi235 – 2417
Helixi242 – 2509
Helixi252 – 2554
Beta strandi259 – 2624
Helixi272 – 2743
Helixi275 – 28612
Beta strandi294 – 2985
Turni300 – 3023
Beta strandi303 – 3053
Helixi309 – 3113
Helixi312 – 3198
Helixi326 – 3338
Beta strandi344 – 3529
Helixi353 – 3619
Helixi363 – 3664
Beta strandi369 – 3724

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C2NX-ray1.55A/B60-375[»]
ProteinModelPortaliQ8IVS2.
SMRiQ8IVS2. Positions 3-375.

Miscellaneous databases

EvolutionaryTraceiQ8IVS2.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036504.
HOVERGENiHBG051540.
InParanoidiQ8IVS2.
KOiK00645.
OMAiMVFEEVD.
OrthoDBiEOG7D85X6.
PhylomeDBiQ8IVS2.
TreeFamiTF313401.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IVS2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSVRVARVAW VRGLGASYRR GASSFPVPPP GAQGVAELLR DATGAEEEAP    50
WAATERRMPG QCSVLLFPGQ GSQVVGMGRG LLNYPRVREL YAAARRVLGY 100
DLLELSLHGP QETLDRTVHC QPAIFVASLA AVEKLHHLQP SVIENCVAAA 150
GFSVGEFAAL VFAGAMEFAE GLYAVKIRAE AMQEASEAVP SGMLSVLGQP 200
QSKFNFACLE AREHCKSLGI ENPVCEVSNY LFPDCRVISG HQEALRFLQK 250
NSSKFHFRRT RMLPVSGAFH TRLMEPAVEP LTQALKAVDI KKPLVSVYSN 300
VHAHRYRHPG HIHKLLAQQL VSPVKWEQTM HAIYERKKGR GFPQTFEVGP 350
GRQLGAILKS CNMQAWKSYS AVDVLQTLEH VDLDPQEPPR 390
Length:390
Mass (Da):42,962
Last modified:June 7, 2004 - v2
Checksum:i5CAF7AE9DFF36A21
GO
Isoform 2 (identifier: Q8IVS2-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:180
Mass (Da):19,176
Checksum:i8DA3FDA905D219C7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031A → G.1 Publication
Corresponds to variant rs13815 [ dbSNP | Ensembl ].
VAR_048183

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei172 – 1809LYAVKIRAE → STVSPEEFL in isoform 2.
VSP_010517
Alternative sequencei181 – 390210Missing in isoform 2.
VSP_010518Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL359401 mRNA. Translation: CAB94789.1.
AL359403 mRNA. Translation: CAB94790.1.
AK314059 mRNA. Translation: BAG36765.1.
AL022237 Genomic DNA. Translation: CAQ07851.1.
AL022237 Genomic DNA. Translation: CAA18261.1.
CH471138 Genomic DNA. Translation: EAW73286.1.
BC030985 mRNA. Translation: AAH30985.1.
BC042195 mRNA. Translation: AAH42195.2.
CCDSiCCDS14045.1. [Q8IVS2-2]
CCDS33660.1. [Q8IVS2-1]
RefSeqiNP_055322.1. NM_014507.3. [Q8IVS2-2]
NP_775738.3. NM_173467.4. [Q8IVS2-1]
UniGeneiHs.349111.

Genome annotation databases

EnsembliENST00000290429; ENSP00000290429; ENSG00000100294. [Q8IVS2-1]
ENST00000327555; ENSP00000331306; ENSG00000100294. [Q8IVS2-2]
GeneIDi27349.
KEGGihsa:27349.
UCSCiuc003bdl.1. human. [Q8IVS2-1]
uc003bdm.1. human.

Polymorphism databases

DMDMi48428076.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL359401 mRNA. Translation: CAB94789.1 .
AL359403 mRNA. Translation: CAB94790.1 .
AK314059 mRNA. Translation: BAG36765.1 .
AL022237 Genomic DNA. Translation: CAQ07851.1 .
AL022237 Genomic DNA. Translation: CAA18261.1 .
CH471138 Genomic DNA. Translation: EAW73286.1 .
BC030985 mRNA. Translation: AAH30985.1 .
BC042195 mRNA. Translation: AAH42195.2 .
CCDSi CCDS14045.1. [Q8IVS2-2 ]
CCDS33660.1. [Q8IVS2-1 ]
RefSeqi NP_055322.1. NM_014507.3. [Q8IVS2-2 ]
NP_775738.3. NM_173467.4. [Q8IVS2-1 ]
UniGenei Hs.349111.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C2N X-ray 1.55 A/B 60-375 [» ]
ProteinModelPortali Q8IVS2.
SMRi Q8IVS2. Positions 3-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118161. 15 interactions.
IntActi Q8IVS2. 2 interactions.
MINTi MINT-4828919.
STRINGi 9606.ENSP00000290429.

PTM databases

PhosphoSitei Q8IVS2.

Polymorphism databases

DMDMi 48428076.

Proteomic databases

MaxQBi Q8IVS2.
PaxDbi Q8IVS2.
PeptideAtlasi Q8IVS2.
PRIDEi Q8IVS2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290429 ; ENSP00000290429 ; ENSG00000100294 . [Q8IVS2-1 ]
ENST00000327555 ; ENSP00000331306 ; ENSG00000100294 . [Q8IVS2-2 ]
GeneIDi 27349.
KEGGi hsa:27349.
UCSCi uc003bdl.1. human. [Q8IVS2-1 ]
uc003bdm.1. human.

Organism-specific databases

CTDi 27349.
GeneCardsi GC22M043528.
HGNCi HGNC:29622. MCAT.
HPAi HPA035471.
MIMi 614479. gene.
neXtProti NX_Q8IVS2.
PharmGKBi PA162395058.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0331.
HOGENOMi HOG000036504.
HOVERGENi HBG051540.
InParanoidi Q8IVS2.
KOi K00645.
OMAi MVFEEVD.
OrthoDBi EOG7D85X6.
PhylomeDBi Q8IVS2.
TreeFami TF313401.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci MetaCyc:HS02028-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q8IVS2.
GeneWikii MCAT_(gene).
GenomeRNAii 27349.
NextBioi 50446.
PROi Q8IVS2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IVS2.
Bgeei Q8IVS2.
CleanExi HS_MCAT.
Genevestigatori Q8IVS2.

Family and domain databases

Gene3Di 3.40.366.10. 2 hits.
InterProi IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
[Graphical view ]
SUPFAMi SSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Caudate nucleus.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "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.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Structure of human mitochondrial malonyltransferase."
    Structural genomics consortium (SGC)
    Submitted (SEP-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 60-375.

Entry informationi

Entry nameiFABD_HUMAN
AccessioniPrimary (citable) accession number: Q8IVS2
Secondary accession number(s): B0QY72, O95510, O95511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: September 3, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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