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Protein

1-acyl-sn-glycerol-3-phosphate acyltransferase gamma

Gene

AGPAT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (PubMed:21173190). Has a preference for arachidonoyl-CoA as a donor. Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity).By similarity1 Publication

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Kineticsi

  1. KM=4.78 µM for LPA sn-1 C18:11 Publication
  2. KM=21.53 µM for C18:1-CoA1 Publication
  1. Vmax=6.35 nmol/min/mg enzyme toward LPA sn-1 C18:11 Publication
  2. Vmax=0.74 nmol/min/mg enzyme toward C18:1-CoA1 Publication

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 2, mitochondrial (GPAT2), Glycerol-3-phosphate acyltransferase 4 (GPAT4), Glycerol-3-phosphate acyltransferase 3 (GPAT3), Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (AGPAT2), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (AGPAT4), 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (AGPAT3), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (AGPAT5), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (AGPAT1), Lysocardiolipin acyltransferase 1 (LCLAT1)
  3. Phosphatidate cytidylyltransferase 1 (CDS1), Phosphatidate cytidylyltransferase 2 (CDS2), Phosphatidate cytidylyltransferase, mitochondrial (TAMM41), Phosphatidate cytidylyltransferase (CDS1), Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS08470-MONOMER.
BRENDAi2.3.1.51. 2681.
ReactomeiR-HSA-1483166. Synthesis of PA.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00557; UER00613.

Chemistry

SwissLipidsiSLP:000000823.

Names & Taxonomyi

Protein namesi
Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 3
Short name:
1-AGP acyltransferase 3
Short name:
1-AGPAT 3
Lysophosphatidic acid acyltransferase gamma
Short name:
LPAAT-gamma
Gene namesi
Name:AGPAT3
Synonyms:LPAAT3
ORF Names:UNQ759/PRO1490
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:326. AGPAT3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 124124CytoplasmicSequence analysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Topological domaini146 – 316171LumenalSequence analysisAdd
BLAST
Transmembranei317 – 33923HelicalSequence analysisAdd
BLAST
Topological domaini340 – 37637CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • Golgi membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • nuclear envelope Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24623.

Polymorphism and mutation databases

BioMutaiAGPAT3.
DMDMi12643817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3763761-acyl-sn-glycerol-3-phosphate acyltransferase gammaPRO_0000208194Add
BLAST

Proteomic databases

EPDiQ9NRZ7.
MaxQBiQ9NRZ7.
PaxDbiQ9NRZ7.
PRIDEiQ9NRZ7.

PTM databases

iPTMnetiQ9NRZ7.
PhosphoSiteiQ9NRZ7.
SwissPalmiQ9NRZ7.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis, pancreas and kidney, followed by spleen, lung, adipose tissue and liver.1 Publication

Gene expression databases

BgeeiQ9NRZ7.
CleanExiHS_AGPAT3.
ExpressionAtlasiQ9NRZ7. baseline and differential.
GenevisibleiQ9NRZ7. HS.

Interactioni

Protein-protein interaction databases

BioGridi121224. 18 interactions.
IntActiQ9NRZ7. 2 interactions.
STRINGi9606.ENSP00000291572.

Structurei

3D structure databases

ProteinModelPortaliQ9NRZ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 1016HXXXXD motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1505. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00530000062943.
HOVERGENiHBG008205.
InParanoidiQ9NRZ7.
KOiK13523.
OMAiMEVAESK.
OrthoDBiEOG7H7928.
PhylomeDBiQ9NRZ7.
TreeFamiTF314065.

Family and domain databases

InterProiIPR032098. Acyltransf_C.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF16076. Acyltransf_C. 1 hit.
PF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NRZ7-1) [UniParc]FASTAAdd to basket

Also known as: Gamma-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.

« Hide

        10         20         30         40         50
MGLLAFLKTQ FVLHLLVGFV FVVSGLVINF VQLCTLALWP VSKQLYRRLN
60 70 80 90 100
CRLAYSLWSQ LVMLLEWWSC TECTLFTDQA TVERFGKEHA VIILNHNFEI
110 120 130 140 150
DFLCGWTMCE RFGVLGSSKV LAKKELLYVP LIGWTWYFLE IVFCKRKWEE
160 170 180 190 200
DRDTVVEGLR RLSDYPEYMW FLLYCEGTRF TETKHRVSME VAAAKGLPVL
210 220 230 240 250
KYHLLPRTKG FTTAVKCLRG TVAAVYDVTL NFRGNKNPSL LGILYGKKYE
260 270 280 290 300
ADMCVRRFPL EDIPLDEKEA AQWLHKLYQE KDALQEIYNQ KGMFPGEQFK
310 320 330 340 350
PARRPWTLLN FLSWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF
360 370
GVRRLIGVTE IEKGSSYGNQ EFKKKE
Length:376
Mass (Da):43,381
Last modified:October 1, 2000 - v1
Checksum:iC12CDBB7CC363852
GO
Isoform 2 (identifier: Q9NRZ7-2) [UniParc]FASTAAdd to basket

Also known as: Gamma-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.

Show »
Length:314
Mass (Da):36,271
Checksum:iFFB9EA98F4F5C204
GO
Isoform 3 (identifier: Q9NRZ7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MGLLAFLKTQ...CRLAYSLWSQ → MQSGGSLPFC...SANALPLSAE

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):45,514
Checksum:i9729B3AE9FB5E518
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741T → P in CAD38635 (PubMed:14702039).Curated
Sequence conflicti358 – 37619VTEIE…FKKKE → ESLEPGRWRLQ in AAQ89067 (PubMed:12975309).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6262Missing in isoform 2. 1 PublicationVSP_005072Add
BLAST
Alternative sequencei1 – 6060MGLLA…SLWSQ → MQSGGSLPFCCYLPSVSSQL LLRESYCNFIKRTQCKSSKL MFSRDFLSGQKYCRCLLWAL PDHPRRRGPTSANALPLSAE in isoform 3. 1 PublicationVSP_013144Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156774 mRNA. Translation: AAF80336.1.
AF156775 mRNA. Translation: AAF80337.1.
AB040138 mRNA. Translation: BAB18943.1.
AY358704 mRNA. Translation: AAQ89067.1.
AP001054 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09461.1.
CH471079 Genomic DNA. Translation: EAX09463.1.
CH471079 Genomic DNA. Translation: EAX09464.1.
CH471079 Genomic DNA. Translation: EAX09465.1.
BC011971 mRNA. Translation: AAH11971.1.
BC040603 mRNA. Translation: AAH40603.1.
BC063552 mRNA. Translation: AAH63552.1.
AK125804 mRNA. Translation: BAC86299.1.
AL832919 mRNA. Translation: CAD38635.2.
CCDSiCCDS13703.1. [Q9NRZ7-1]
RefSeqiNP_001032642.1. NM_001037553.1. [Q9NRZ7-1]
NP_064517.1. NM_020132.4. [Q9NRZ7-1]
XP_005261217.1. XM_005261160.3. [Q9NRZ7-1]
XP_006724092.1. XM_006724029.2. [Q9NRZ7-1]
XP_006724093.1. XM_006724030.2. [Q9NRZ7-1]
XP_006724094.1. XM_006724031.2. [Q9NRZ7-2]
XP_011527967.1. XM_011529665.1. [Q9NRZ7-1]
XP_011527968.1. XM_011529666.1. [Q9NRZ7-2]
UniGeneiHs.248785.

Genome annotation databases

EnsembliENST00000291572; ENSP00000291572; ENSG00000160216. [Q9NRZ7-1]
ENST00000327505; ENSP00000332989; ENSG00000160216. [Q9NRZ7-1]
ENST00000398058; ENSP00000381135; ENSG00000160216. [Q9NRZ7-1]
ENST00000398061; ENSP00000381138; ENSG00000160216. [Q9NRZ7-1]
ENST00000398063; ENSP00000381140; ENSG00000160216. [Q9NRZ7-1]
ENST00000546158; ENSP00000443510; ENSG00000160216. [Q9NRZ7-1]
GeneIDi56894.
KEGGihsa:56894.
UCSCiuc002zdv.4. human. [Q9NRZ7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156774 mRNA. Translation: AAF80336.1.
AF156775 mRNA. Translation: AAF80337.1.
AB040138 mRNA. Translation: BAB18943.1.
AY358704 mRNA. Translation: AAQ89067.1.
AP001054 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09461.1.
CH471079 Genomic DNA. Translation: EAX09463.1.
CH471079 Genomic DNA. Translation: EAX09464.1.
CH471079 Genomic DNA. Translation: EAX09465.1.
BC011971 mRNA. Translation: AAH11971.1.
BC040603 mRNA. Translation: AAH40603.1.
BC063552 mRNA. Translation: AAH63552.1.
AK125804 mRNA. Translation: BAC86299.1.
AL832919 mRNA. Translation: CAD38635.2.
CCDSiCCDS13703.1. [Q9NRZ7-1]
RefSeqiNP_001032642.1. NM_001037553.1. [Q9NRZ7-1]
NP_064517.1. NM_020132.4. [Q9NRZ7-1]
XP_005261217.1. XM_005261160.3. [Q9NRZ7-1]
XP_006724092.1. XM_006724029.2. [Q9NRZ7-1]
XP_006724093.1. XM_006724030.2. [Q9NRZ7-1]
XP_006724094.1. XM_006724031.2. [Q9NRZ7-2]
XP_011527967.1. XM_011529665.1. [Q9NRZ7-1]
XP_011527968.1. XM_011529666.1. [Q9NRZ7-2]
UniGeneiHs.248785.

3D structure databases

ProteinModelPortaliQ9NRZ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121224. 18 interactions.
IntActiQ9NRZ7. 2 interactions.
STRINGi9606.ENSP00000291572.

Chemistry

SwissLipidsiSLP:000000823.

PTM databases

iPTMnetiQ9NRZ7.
PhosphoSiteiQ9NRZ7.
SwissPalmiQ9NRZ7.

Polymorphism and mutation databases

BioMutaiAGPAT3.
DMDMi12643817.

Proteomic databases

EPDiQ9NRZ7.
MaxQBiQ9NRZ7.
PaxDbiQ9NRZ7.
PRIDEiQ9NRZ7.

Protocols and materials databases

DNASUi56894.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291572; ENSP00000291572; ENSG00000160216. [Q9NRZ7-1]
ENST00000327505; ENSP00000332989; ENSG00000160216. [Q9NRZ7-1]
ENST00000398058; ENSP00000381135; ENSG00000160216. [Q9NRZ7-1]
ENST00000398061; ENSP00000381138; ENSG00000160216. [Q9NRZ7-1]
ENST00000398063; ENSP00000381140; ENSG00000160216. [Q9NRZ7-1]
ENST00000546158; ENSP00000443510; ENSG00000160216. [Q9NRZ7-1]
GeneIDi56894.
KEGGihsa:56894.
UCSCiuc002zdv.4. human. [Q9NRZ7-1]

Organism-specific databases

CTDi56894.
GeneCardsiAGPAT3.
HGNCiHGNC:326. AGPAT3.
MIMi614794. gene.
neXtProtiNX_Q9NRZ7.
PharmGKBiPA24623.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1505. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00530000062943.
HOVERGENiHBG008205.
InParanoidiQ9NRZ7.
KOiK13523.
OMAiMEVAESK.
OrthoDBiEOG7H7928.
PhylomeDBiQ9NRZ7.
TreeFamiTF314065.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.
BioCyciMetaCyc:HS08470-MONOMER.
BRENDAi2.3.1.51. 2681.
ReactomeiR-HSA-1483166. Synthesis of PA.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-75109. Triglyceride Biosynthesis.

Miscellaneous databases

ChiTaRSiAGPAT3. human.
GeneWikiiAGPAT3.
GenomeRNAii56894.
PROiQ9NRZ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRZ7.
CleanExiHS_AGPAT3.
ExpressionAtlasiQ9NRZ7. baseline and differential.
GenevisibleiQ9NRZ7. HS.

Family and domain databases

InterProiIPR032098. Acyltransf_C.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF16076. Acyltransf_C. 1 hit.
PF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The structure and functions of human lysophosphatidic acid acyltransferases."
    Leung D.W.
    Front. Biosci. 6:D944-D953(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "Isolation of a novel gene encoding 1-acylglycerol-3-phosphate O-acyltransferase 3 (AGPAT3) from the human chromosome 21q22.3."
    Nagamine K., Kudoh J., Minoshima S., Kawasaki K., Hase T., Shimizu N.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain, Skin and Testis.
  7. "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] OF 1-372 (ISOFORM 3).
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-376.
    Tissue: Melanoma.
  9. Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
  10. "Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria."
    Prasad S.S., Garg A., Agarwal A.K.
    J. Lipid Res. 52:451-462(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPLCC_HUMAN
AccessioniPrimary (citable) accession number: Q9NRZ7
Secondary accession number(s): D3DSL2
, Q3ZCU2, Q6UWP6, Q6ZUC6, Q8N3Q7, Q9NRZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 133 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.