UniProtKB - P97570 (PLPL9_RAT)
85/88 kDa calcium-independent phospholipase A2
Pla2g6
Functioni
Catalytic activityi
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+2 PublicationsEC:3.1.1.42 PublicationsThis reaction proceeds in the forward2 Publications direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+2 PublicationsThis reaction proceeds in the forward2 Publications direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-sn-glycero-3-phosphate + H+ + hexadecanoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H+ + sn-glycerol 3-phosphocholineBy similarityEC:3.1.1.5By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H+ + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H+ + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:3.1.2.21 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1ʼ,3ʼ-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-octadecenoate + 1ʼ-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3ʼ-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1ʼ-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3ʼ-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-octadecenoate + 1ʼ,3ʼ-bis-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1ʼ,3ʼ-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1ʼ-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3ʼ-[1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H+1 PublicationThis reaction proceeds in the backward1 Publication direction.
- 1-octadecanoyl-2-(15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoethanolamine + 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
Activity regulationi
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 520 | NucleophilePROSITE-ProRule annotation | 1 | |
Active sitei | 653 | Proton acceptorPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB
- ATP-dependent protein binding Source: RGD
- calcium-independent phospholipase A2 activity Source: UniProtKB
- calmodulin binding Source: UniProtKB-KW
- identical protein binding Source: RGD
- lysophospholipase activity Source: UniProtKB
- myristoyl-CoA hydrolase activity Source: UniProtKB-EC
- palmitoyl-CoA hydrolase activity Source: UniProtKB
- phosphatidyl phospholipase B activity Source: UniProtKB-EC
- phospholipase A2 activity Source: Reactome
- phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) Source: UniProtKB-EC
- phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) Source: UniProtKB-EC
- protein kinase binding Source: RGD
- serine hydrolase activity Source: RGD
GO - Biological processi
- antibacterial humoral response Source: RGD
- cardiolipin acyl-chain remodeling Source: UniProtKB
- cardiolipin biosynthetic process Source: RGD
- chemotaxis Source: UniProtKB-KW
- maternal process involved in female pregnancy Source: RGD
- memory Source: RGD
- negative regulation of synaptic transmission, glutamatergic Source: RGD
- phosphatidic acid metabolic process Source: UniProtKB
- phosphatidylcholine catabolic process Source: UniProtKB
- phosphatidylethanolamine catabolic process Source: UniProtKB
- platelet activating factor metabolic process Source: UniProtKB
- positive regulation of arachidonic acid secretion Source: RGD
- positive regulation of blood vessel diameter Source: RGD
- positive regulation of ceramide biosynthetic process Source: RGD
- positive regulation of cytosolic calcium ion concentration Source: RGD
- positive regulation of exocytosis Source: RGD
- positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: RGD
- positive regulation of protein kinase C signaling Source: RGD
- positive regulation of protein phosphorylation Source: RGD
- positive regulation of release of cytochrome c from mitochondria Source: RGD
- regulation of store-operated calcium channel activity Source: RGD
- response to endoplasmic reticulum stress Source: RGD
- urinary bladder smooth muscle contraction Source: RGD
Keywordsi
Molecular function | Calmodulin-binding, Hydrolase |
Biological process | Chemotaxis, Lipid metabolism, Phospholipid metabolism |
Enzyme and pathway databases
Reactomei | R-RNO-1482788, Acyl chain remodelling of PC R-RNO-1482839, Acyl chain remodelling of PE R-RNO-2029485, Role of phospholipids in phagocytosis R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic |
Names & Taxonomyi
Protein namesi | Recommended name: 85/88 kDa calcium-independent phospholipase A2 (EC:3.1.1.42 Publications)Short name: CaI-PLA2 Alternative name(s): 2-lysophosphatidylcholine acylhydrolase (EC:3.1.1.5By similarity) Group VI phospholipase A2 Short name: GVI PLA2 Intracellular membrane-associated calcium-independent phospholipase A2 beta Short name: iPLA2-beta Palmitoyl-CoA hydrolase (EC:3.1.2.21 Publication) Patatin-like phospholipase domain-containing protein 9 Short name: PNPLA9 |
Gene namesi | Name:Pla2g6 Synonyms:Pnpla9 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 628867, Pla2g6 |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity
Mitochondrion
- Mitochondrion By similarity
Other locations
- Cytoplasm By similarity
- pseudopodium By similarity
Note: Recruited to the membrane-enriched pseudopods upon MCP1/CCL2 stimulation in monocytes.By similarity
Cytoskeleton
- centriolar satellite Source: Ensembl
Cytosol
- cytosol Source: RGD
Extracellular region or secreted
- extracellular space Source: RGD
Mitochondrion
- mitochondrial inner membrane Source: Reactome
- mitochondrion Source: RGD
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB-KW
- pseudopodium Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 481 – 501 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 512 – 532 | HelicalSequence analysisAdd BLAST | 21 |
Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Membrane, MitochondrionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000067039 | 1 – 807 | 85/88 kDa calcium-independent phospholipase A2Add BLAST | 807 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 13 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | P97570 |
PRIDEi | P97570 |
PTM databases
iPTMneti | P97570 |
PhosphoSitePlusi | P97570 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSRNOG00000012295, Expressed in testis and 22 other tissues |
Genevisiblei | P97570, RN |
Interactioni
Subunit structurei
Homodimer formed by catalytic domains tightly interacting through a large hydrophobic interface. The contact area involves 3 alpha helices, several loops and a part of the beta sheet from each monomer. Both active sites of the dimer are in close proximity adopting an open conformation that provide sufficient space for phospholipid access and favoring cooperativity in deacylation-reacylation reactions. Each monomer has 9 ankyrin repeats stacked side-by-side in an elongated structure oriented outwards from the catalytic core.
By similarityGO - Molecular functioni
- ATP-dependent protein binding Source: RGD
- calmodulin binding Source: UniProtKB-KW
- identical protein binding Source: RGD
- protein kinase binding Source: RGD
Protein-protein interaction databases
IntActi | P97570, 1 interactor |
STRINGi | 10116.ENSRNOP00000017104 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 120 – 147 | ANK 1By similarityAdd BLAST | 28 | |
Repeati | 151 – 181 | ANK 1Sequence analysisAdd BLAST | 31 | |
Repeati | 185 – 215 | ANK 2Sequence analysisAdd BLAST | 31 | |
Repeati | 219 – 248 | ANK 3Sequence analysisAdd BLAST | 30 | |
Repeati | 251 – 281 | ANK 4Sequence analysisAdd BLAST | 31 | |
Repeati | 286 – 312 | ANK 5Sequence analysisAdd BLAST | 27 | |
Repeati | 316 – 345 | ANK 6Sequence analysisAdd BLAST | 30 | |
Repeati | 349 – 378 | ANK 7Sequence analysisAdd BLAST | 30 | |
Repeati | 382 – 403 | ANK 9By similarityAdd BLAST | 22 | |
Domaini | 482 – 666 | PNPLAPROSITE-ProRule annotationAdd BLAST | 185 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 678 – 687 | Calmodulin-binding (1-9-14 motif)1 Publication | 10 | |
Regioni | 749 – 760 | Calmodulin-binding (IQ motif)1 PublicationAdd BLAST | 12 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 486 – 491 | GXGXXGPROSITE-ProRule annotation | 6 | |
Motifi | 518 – 522 | GXSXGPROSITE-ProRule annotation | 5 | |
Motifi | 653 – 655 | DGA/GPROSITE-ProRule annotation | 3 |
Domaini
Keywords - Domaini
ANK repeat, Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0513, Eukaryota |
GeneTreei | ENSGT00940000158756 |
HOGENOMi | CLU_010817_0_0_1 |
InParanoidi | P97570 |
OMAi | DSWTRPY |
OrthoDBi | 841851at2759 |
PhylomeDBi | P97570 |
TreeFami | TF319230 |
Family and domain databases
Gene3Di | 1.25.40.20, 2 hits |
InterProi | View protein in InterPro IPR016035, Acyl_Trfase/lysoPLipase IPR002110, Ankyrin_rpt IPR020683, Ankyrin_rpt-contain_dom IPR036770, Ankyrin_rpt-contain_sf IPR002641, PNPLA_dom |
Pfami | View protein in Pfam PF12796, Ank_2, 1 hit PF01734, Patatin, 1 hit |
PRINTSi | PR01415, ANKYRIN |
SMARTi | View protein in SMART SM00248, ANK, 6 hits |
SUPFAMi | SSF48403, SSF48403, 1 hit SSF52151, SSF52151, 1 hit |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 4 hits PS51635, PNPLA, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MQFFGRLVNT LSSVTNLFSN PFRVKEVSLA DYASSERVRE EGQLILLQNA
60 70 80 90 100
SNRTWDCVLV SPRNPQSGFR LFQLESEADA LVNFQQYSSQ LPPFYESSVQ
110 120 130 140 150
VLHVEVLQHL TDLIRNHPSW TVTHLAVELG IRECFHHSRI ISCANSTENE
160 170 180 190 200
EGCTPLHLAC RKGDSEILVE LVQYCHAQMD VTDNKGETAF HYAVQGDNPQ
210 220 230 240 250
VLQLLGKNAS AGLNQVNNQG LTPLHLACQM GKQEMVRVLL LCNARCNIMG
260 270 280 290 300
PGGFPIHTAM KFSQKGCAEM IISMDSNQIH SKDPRYGASP LHWAKNAEMA
310 320 330 340 350
RMLLKRGCDV DSTSASGNTA LHVAVTRNRF DCVMVLLTYG ANAGARGEHG
360 370 380 390 400
NTPLHLAMSK DNMEMVKALI VFGAEVDTPN DFGETPAFIA SKISKLITRK
410 420 430 440 450
ALLTLLKTVG ADYHFPFIQG VSTEQSSAAG PHPFFSLDRT QPPTISLNNL
460 470 480 490 500
ELQDLMPVSR ARKPAFILSS MRDEKRSHDH LLCLDGGGVK GLVIIQLLIA
510 520 530 540 550
IEKASGVATK DLFDWVAGTS TGGILALAIL HSKSMAYMRG VYFRMKDEVF
560 570 580 590 600
RGSRPYESGP LEEFLKREFG EHTKMTDVKK PKVMLTGTLS DRQPAELHLF
610 620 630 640 650
RNYDAPEAVR EPRCTPNINL KPPTQPADQL VWRAARSSGA APTYFRPNGR
660 670 680 690 700
FLDGGLLANN PTLDAMTEIH EYNQDMIRKG QGNKVKKLSI VVSLGTGKSP
710 720 730 740 750
QVPVTCVDVF RPSNPWELAK TVFGAKELGK MVVDCCTDPD GRAVDRARAW
760 770 780 790 800
CEMVGIQYFR LNPQLGSDIM LDEVSDAVLV NALWETEVYI YEHREEFQKL
VQLLLSP
The sequence of this isoform differs from the canonical sequence as follows:
396-451: LITRKALLTLLKTVGADYHFPFIQGVSTEQSSAAGPHPFFSLDRTQPPTISLNNLE → Q
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 24 | V → A in AAC53136 (PubMed:9111008).Curated | 1 | |
Sequence conflicti | 58 | V → D in AAC53136 (PubMed:9111008).Curated | 1 | |
Sequence conflicti | 68 | G → D in AAC53136 (PubMed:9111008).Curated | 1 | |
Sequence conflicti | 80 | A → V in AAC53136 (PubMed:9111008).Curated | 1 | |
Sequence conflicti | 99 | V → E in AAC53136 (PubMed:9111008).Curated | 1 | |
Sequence conflicti | 109 | Missing in AAC53136 (PubMed:9111008).Curated | 1 | |
Sequence conflicti | 142 | S → T in AAC53136 (PubMed:9111008).Curated | 1 | |
Sequence conflicti | 477 | S → T in AAC53136 (PubMed:9111008).Curated | 1 | |
Sequence conflicti | 793 | H → Y in AAC53136 (PubMed:9111008).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_044365 | 396 – 451 | LITRK…LNNLE → Q in isoform Short. 1 PublicationAdd BLAST | 56 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U51898 mRNA Translation: AAC53136.1 AABR06052011 Genomic DNA No translation available. CH473950 Genomic DNA Translation: EDM15808.1 CH473950 Genomic DNA Translation: EDM15809.1 BC081916 mRNA Translation: AAH81916.1 |
RefSeqi | NP_001005560.1, NM_001005560.1 [P97570-1] NP_001257725.1, NM_001270796.1 [P97570-2] |
Genome annotation databases
Ensembli | ENSRNOT00000016827; ENSRNOP00000016827; ENSRNOG00000012295 [P97570-2] ENSRNOT00000017108; ENSRNOP00000017104; ENSRNOG00000012295 [P97570-1] ENSRNOT00000087344; ENSRNOP00000072104; ENSRNOG00000012295 [P97570-1] ENSRNOT00000090565; ENSRNOP00000075311; ENSRNOG00000012295 [P97570-2] |
GeneIDi | 360426 |
KEGGi | rno:360426 |
UCSCi | RGD:628867, rat [P97570-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U51898 mRNA Translation: AAC53136.1 AABR06052011 Genomic DNA No translation available. CH473950 Genomic DNA Translation: EDM15808.1 CH473950 Genomic DNA Translation: EDM15809.1 BC081916 mRNA Translation: AAH81916.1 |
RefSeqi | NP_001005560.1, NM_001005560.1 [P97570-1] NP_001257725.1, NM_001270796.1 [P97570-2] |
3D structure databases
SMRi | P97570 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | P97570, 1 interactor |
STRINGi | 10116.ENSRNOP00000017104 |
Chemistry databases
ChEMBLi | CHEMBL1075318 |
PTM databases
iPTMneti | P97570 |
PhosphoSitePlusi | P97570 |
Proteomic databases
PaxDbi | P97570 |
PRIDEi | P97570 |
Genome annotation databases
Organism-specific databases
CTDi | 8398 |
RGDi | 628867, Pla2g6 |
Phylogenomic databases
eggNOGi | KOG0513, Eukaryota |
GeneTreei | ENSGT00940000158756 |
HOGENOMi | CLU_010817_0_0_1 |
InParanoidi | P97570 |
OMAi | DSWTRPY |
OrthoDBi | 841851at2759 |
PhylomeDBi | P97570 |
TreeFami | TF319230 |
Enzyme and pathway databases
Reactomei | R-RNO-1482788, Acyl chain remodelling of PC R-RNO-1482839, Acyl chain remodelling of PE R-RNO-2029485, Role of phospholipids in phagocytosis R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic |
Miscellaneous databases
PROi | PR:P97570 |
Gene expression databases
Bgeei | ENSRNOG00000012295, Expressed in testis and 22 other tissues |
Genevisiblei | P97570, RN |
Family and domain databases
Gene3Di | 1.25.40.20, 2 hits |
InterProi | View protein in InterPro IPR016035, Acyl_Trfase/lysoPLipase IPR002110, Ankyrin_rpt IPR020683, Ankyrin_rpt-contain_dom IPR036770, Ankyrin_rpt-contain_sf IPR002641, PNPLA_dom |
Pfami | View protein in Pfam PF12796, Ank_2, 1 hit PF01734, Patatin, 1 hit |
PRINTSi | PR01415, ANKYRIN |
SMARTi | View protein in SMART SM00248, ANK, 6 hits |
SUPFAMi | SSF48403, SSF48403, 1 hit SSF52151, SSF52151, 1 hit |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 4 hits PS51635, PNPLA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PLPL9_RAT | |
Accessioni | P97570Primary (citable) accession number: P97570 Secondary accession number(s): G3V7M8, Q66HD1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | October 31, 2012 | |
Last modified: | December 2, 2020 | |
This is version 156 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |