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Protein

Putative inactive group IIC secretory phospholipase A2

Gene

PLA2G2C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Inactive phospholipase.Curated

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Calcium; via carbonyl oxygenBy similarity
Metal bindingi47 – 471Calcium; via carbonyl oxygenBy similarity
Metal bindingi49 – 491Calcium; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative inactive group IIC secretory phospholipase A2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase-like protein GIIC
Gene namesi
Name:PLA2G2C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9032. PLA2G2C.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2097.

Polymorphism and mutation databases

DMDMi300669681.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 149131Putative inactive group IIC secretory phospholipase A2PRO_0000319946Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 142By similarity
Disulfide bondi77 ↔ 107By similarity
Disulfide bondi95 ↔ 112By similarity
Disulfide bondi97 ↔ 105Sequence analysis

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ5R387.
TopDownProteomicsiQ5R387.

Expressioni

Gene expression databases

BgeeiQ5R387.
ExpressionAtlasiQ5R387. baseline and differential.

Interactioni

Chemistry

BindingDBiQ5R387.

Structurei

3D structure databases

ProteinModelPortaliQ5R387.
SMRiQ5R387. Positions 19-133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiQ5R387.
OMAiDTDRHSP.
OrthoDBiEOG7N63PF.
PhylomeDBiQ5R387.
TreeFamiTF319283.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5R387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVIAILTLL LFCSPTHSSF WQFQRRVKHI TGRSAFFSYY GYGCYCGLGD
60 70 80 90 100
KGIPVDDTDR HSPSSPSPYE KLKEFSCQPV LNSYQFHIVN GAVVCGCTLG
110 120 130 140
PGASCHCRLK ACECDKQSVH CFKESLPTYE KNFKQFSSQP RCGRHKPWC
Length:149
Mass (Da):16,844
Last modified:July 13, 2010 - v3
Checksum:iEB386EF6DF86AA8B
GO

Sequence cautioni

The sequence CAI20258.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391Q → R.
Corresponds to variant rs6426616 [ dbSNP | Ensembl ].
VAR_039057

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98257 Genomic DNA. Translation: CAI20258.1. Sequence problems.
PIRiA60718.
UniGeneiHs.512512.

Genome annotation databases

EnsembliENST00000429261; ENSP00000389335; ENSG00000187980.
UCSCiuc057cyp.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98257 Genomic DNA. Translation: CAI20258.1. Sequence problems.
PIRiA60718.
UniGeneiHs.512512.

3D structure databases

ProteinModelPortaliQ5R387.
SMRiQ5R387. Positions 19-133.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ5R387.
ChEMBLiCHEMBL2097.

Polymorphism and mutation databases

DMDMi300669681.

Proteomic databases

PRIDEiQ5R387.
TopDownProteomicsiQ5R387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000429261; ENSP00000389335; ENSG00000187980.
UCSCiuc057cyp.1. human.

Organism-specific databases

GeneCardsiPLA2G2C.
HGNCiHGNC:9032. PLA2G2C.
neXtProtiNX_Q5R387.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiQ5R387.
OMAiDTDRHSP.
OrthoDBiEOG7N63PF.
PhylomeDBiQ5R387.
TreeFamiTF319283.

Miscellaneous databases

NextBioi13622338.
PROiQ5R387.

Gene expression databases

BgeeiQ5R387.
ExpressionAtlasiQ5R387. baseline and differential.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Novel gene exon homologous to pancreatic phospholipase A2: sequence and chromosomal mapping of both human genes."
    Seilhamer J.J., Randall T.L., Johnson L.K., Heinzmann C., Klisak I., Sparkes R.S., Lusis A.J.
    J. Cell. Biochem. 39:327-337(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-60.

Entry informationi

Entry nameiPA2GC_HUMAN
AccessioniPrimary (citable) accession number: Q5R387
Secondary accession number(s): Q7M4M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 13, 2010
Last modified: May 11, 2016
This is version 93 of the entry and version 3 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

Caution

Ser-67 is present instead of the conserved His which is one of the active site residues. It is therefore expected that this protein lacks catalytic activity.Curated
The N-terminal region is predicted based on cross-species conservation and limited EST data. Exact gene structure in this region is unclear.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.