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P07756 (CPSM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbamoyl-phosphate synthase [ammonia], mitochondrial

EC=6.3.4.16
Alternative name(s):
Carbamoyl-phosphate synthetase I
Short name=CPSase I
Gene names
Name:Cps1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. HAMAP-Rule MF_01209

Catalytic activity

2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate. Ref.3

Enzyme regulation

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator. N-acetyl-L-beta-phenylglutamate (Phe-NAG) can also activate CPSase I, but with an activation constant that is 2-fold higher than that for NAG. Ref.3

Subcellular location

Mitochondrion. Nucleusnucleolus By similarity HAMAP-Rule MF_01209.

Tissue specificity

Primarily in the liver and small intestine.

Domain

The type-1 glutamine amidotransferase domain is defective. HAMAP-Rule MF_01209

Post-translational modification

50% of the mature protein that was isolated had Leu-39 as its N-terminal residue and 50% had Ser-40 suggesting two adjacent processing sites. However, the possibility of proteolytic removal of Leu-39 during the isolation of the enzyme cannot be excluded. HAMAP-Rule MF_01209

Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation By similarity. HAMAP-Rule MF_01209

Sequence similarities

Contains 2 ATP-grasp domains.

Contains 1 glutamine amidotransferase type-1 domain.

Biophysicochemical properties

Kinetic parameters:

The activation constant Ka of N-acetyl-L-glutamate for the reaction is 0.11 mM.

KM=1.06 mM for ATP Ref.3

KM=6.43 mM for HCO3-

KM=1.07 mM for NH4+

Ontologies

Keywords
   Biological processUrea cycle
   Cellular componentMitochondrion
Nucleus
   DomainRepeat
Transit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanion homeostasis

Inferred from direct assay PubMed 4062872. Source: RGD

carbamoyl phosphate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

cellular response to cAMP

Inferred from expression pattern PubMed 17397987. Source: RGD

cellular response to fibroblast growth factor stimulus

Inferred from expression pattern PubMed 12832696. Source: RGD

cellular response to glucagon stimulus

Inferred from expression pattern PubMed 8460937. Source: RGD

cellular response to oleic acid

Inferred from expression pattern PubMed 8985169. Source: RGD

glutamine catabolic process

Inferred from electronic annotation. Source: InterPro

glycogen catabolic process

Inferred from electronic annotation. Source: Ensembl

hepatocyte differentiation

Inferred from expression pattern PubMed 12939595. Source: RGD

homocysteine metabolic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from expression pattern PubMed 8690412. Source: RGD

midgut development

Inferred from expression pattern PubMed 9544996. Source: RGD

nitric oxide metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

response to acid

Inferred from expression pattern PubMed 20452409. Source: RGD

response to amine

Inferred from expression pattern PubMed 2864015. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 11738098. Source: RGD

response to cAMP

Inferred from expression pattern PubMed 17397987PubMed 6092398. Source: RGD

response to dexamethasone

Inferred from expression pattern PubMed 19446026. Source: RGD

response to drug

Inferred from expression pattern PubMed 19135993. Source: RGD

response to food

Inferred from expression pattern PubMed 15481768. Source: RGD

response to glucagon

Inferred from expression pattern PubMed 3754512. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 17397987PubMed 8985169. Source: RGD

response to growth hormone

Inferred from expression pattern PubMed 9688877. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 17539997. Source: RGD

response to oleic acid

Inferred from expression pattern PubMed 8985169. Source: RGD

response to starvation

Inferred from expression pattern PubMed 1979948. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 9688877. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 14625847. Source: RGD

response to zinc ion

Inferred from expression pattern PubMed 12840196. Source: RGD

triglyceride catabolic process

Inferred from electronic annotation. Source: Ensembl

urea cycle

Inferred from direct assay PubMed 3680220PubMed 4062872. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 3527129. Source: RGD

mitochondrial inner membrane

Inferred from direct assay PubMed 3680220. Source: RGD

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 14561759. Source: HGNC

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 17669278. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 11577071. Source: RGD

calcium ion binding

Inferred from physical interaction PubMed 9506839. Source: RGD

carbamoyl-phosphate synthase (ammonia) activity

Inferred from direct assay PubMed 11577071PubMed 3680220PubMed 4062872. Source: RGD

endopeptidase activity

Inferred from mutant phenotype PubMed 15304357. Source: RGD

glutamate binding

Inferred from physical interaction PubMed 8663466. Source: RGD

modified amino acid binding

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Inferred from direct assay PubMed 3680220. Source: RGD

protein complex binding

Inferred from direct assay PubMed 17669278. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion HAMAP-Rule MF_01209
Chain39 – 15001462Carbamoyl-phosphate synthase [ammonia], mitochondrial HAMAP-Rule MF_01209
PRO_0000029899

Regions

Domain219 – 404186Glutamine amidotransferase type-1
Domain551 – 743193ATP-grasp 1
Domain1093 – 1284192ATP-grasp 2
Region39 – 218180Anthranilate phosphoribosyltransferase homolog HAMAP-Rule MF_01209

Sites

Binding site13911Allosteric activator
Binding site13941Allosteric activator
Binding site14101Allosteric activator
Binding site14371Allosteric activator
Binding site14401Allosteric activator
Binding site14491Allosteric activator

Amino acid modifications

Modified residue551N6-acetyllysine; alternate By similarity
Modified residue551N6-succinyllysine; alternate By similarity
Modified residue571N6-acetyllysine; alternate By similarity
Modified residue571N6-succinyllysine; alternate By similarity
Modified residue1191N6-acetyllysine; alternate By similarity
Modified residue1191N6-succinyllysine; alternate By similarity
Modified residue1571N6-acetyllysine; alternate By similarity
Modified residue1571N6-succinyllysine; alternate By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue1821N6-acetyllysine By similarity
Modified residue1971N6-acetyllysine By similarity
Modified residue2071N6-acetyllysine; alternate By similarity
Modified residue2071N6-succinyllysine; alternate By similarity
Modified residue2101N6-acetyllysine By similarity
Modified residue2141N6-acetyllysine; alternate By similarity
Modified residue2141N6-succinyllysine; alternate By similarity
Modified residue2191N6-acetyllysine By similarity
Modified residue2281N6-acetyllysine By similarity
Modified residue2791N6-acetyllysine By similarity
Modified residue2801N6-acetyllysine By similarity
Modified residue2871N6-acetyllysine; alternate By similarity
Modified residue2871N6-succinyllysine; alternate By similarity
Modified residue3071N6-acetyllysine; alternate By similarity
Modified residue3071N6-succinyllysine; alternate By similarity
Modified residue3101N6-acetyllysine By similarity
Modified residue4001N6-succinyllysine By similarity
Modified residue4021N6-succinyllysine By similarity
Modified residue4121N6-acetyllysine; alternate By similarity
Modified residue4121N6-succinyllysine; alternate By similarity
Modified residue4531N6-acetyllysine By similarity
Modified residue4581N6-acetyllysine; alternate By similarity
Modified residue4581N6-succinyllysine; alternate By similarity
Modified residue5221N6-acetyllysine; alternate By similarity
Modified residue5221N6-succinyllysine; alternate By similarity
Modified residue5271N6-acetyllysine; alternate By similarity
Modified residue5271N6-succinyllysine; alternate By similarity
Modified residue5321N6-acetyllysine By similarity
Modified residue5371Phosphoserine By similarity
Modified residue5531N6-acetyllysine; alternate By similarity
Modified residue5531N6-succinyllysine; alternate By similarity
Modified residue5601N6-acetyllysine; alternate By similarity
Modified residue5601N6-succinyllysine; alternate By similarity
Modified residue5751N6-acetyllysine; alternate By similarity
Modified residue5751N6-succinyllysine; alternate By similarity
Modified residue6031N6-acetyllysine; alternate By similarity
Modified residue6031N6-succinyllysine; alternate By similarity
Modified residue6121N6-acetyllysine; alternate By similarity
Modified residue6121N6-succinyllysine; alternate By similarity
Modified residue6301N6-acetyllysine By similarity
Modified residue7511N6-acetyllysine; alternate By similarity
Modified residue7511N6-succinyllysine; alternate By similarity
Modified residue7571N6-acetyllysine; alternate By similarity
Modified residue7571N6-succinyllysine; alternate By similarity
Modified residue7721N6-acetyllysine By similarity
Modified residue7931N6-acetyllysine; alternate By similarity
Modified residue7931N6-succinyllysine; alternate By similarity
Modified residue8111N6-acetyllysine By similarity
Modified residue8311N6-acetyllysine; alternate By similarity
Modified residue8311N6-succinyllysine; alternate By similarity
Modified residue8411N6-acetyllysine By similarity
Modified residue8561N6-acetyllysine By similarity
Modified residue8751N6-acetyllysine; alternate By similarity
Modified residue8751N6-succinyllysine; alternate By similarity
Modified residue8891N6-acetyllysine; alternate By similarity
Modified residue8891N6-succinyllysine; alternate By similarity
Modified residue8921N6-acetyllysine; alternate By similarity
Modified residue8921N6-succinyllysine; alternate By similarity
Modified residue9081N6-acetyllysine By similarity
Modified residue9151N6-acetyllysine; alternate By similarity
Modified residue9151N6-succinyllysine; alternate By similarity
Modified residue9191N6-acetyllysine; alternate By similarity
Modified residue9191N6-succinyllysine; alternate By similarity
Modified residue9351N6-acetyllysine By similarity
Modified residue10741N6-acetyllysine; alternate By similarity
Modified residue10741N6-succinyllysine; alternate By similarity
Modified residue10791Phosphoserine By similarity
Modified residue11001N6-acetyllysine; alternate By similarity
Modified residue11001N6-succinyllysine; alternate By similarity
Modified residue11491N6-succinyllysine By similarity
Modified residue11681N6-acetyllysine; alternate By similarity
Modified residue11681N6-succinyllysine; alternate By similarity
Modified residue11831N6-acetyllysine; alternate By similarity
Modified residue11831N6-succinyllysine; alternate By similarity
Modified residue12221N6-acetyllysine By similarity
Modified residue12321N6-acetyllysine; alternate By similarity
Modified residue12321N6-succinyllysine; alternate By similarity
Modified residue12691N6-acetyllysine; alternate By similarity
Modified residue12691N6-succinyllysine; alternate By similarity
Modified residue12911N6-acetyllysine; alternate By similarity
Modified residue12911N6-succinyllysine; alternate By similarity
Modified residue13561N6-acetyllysine; alternate By similarity
Modified residue13561N6-succinyllysine; alternate By similarity
Modified residue13601N6-succinyllysine By similarity
Modified residue14441N6-acetyllysine; alternate By similarity
Modified residue14441N6-succinyllysine; alternate By similarity
Modified residue14711N6-acetyllysine; alternate By similarity
Modified residue14711N6-succinyllysine; alternate By similarity
Modified residue14791N6-acetyllysine; alternate By similarity
Modified residue14791N6-succinyllysine; alternate By similarity
Modified residue14861N6-acetyllysine; alternate By similarity
Modified residue14861N6-succinyllysine; alternate By similarity

Experimental info

Mutagenesis13911T → V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. Ref.3
Mutagenesis13941T → A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. Ref.3
Mutagenesis14101W → K: 60-fold increase in the activation constant of NAG. Ref.3
Mutagenesis14371N → D: 70-fold increase in the activation constant of NAG. Ref.3
Mutagenesis14401N → D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P07756 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 038E8F893DE1C34D

FASTA1,500164,580
        10         20         30         40         50         60 
MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS 

        70         80         90        100        110        120 
FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI IGNGGAPDTT ARDELGLNKY 

       130        140        150        160        170        180 
MESDGIKVAG LLVLNYSHDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML 

       190        200        210        220        230        240 
GKIEFEGQSV DFVDPNKQNL IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA 

       250        260        270        280        290        300 
EVHLVPWNHD FTQMDYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT 

       310        320        330        340        350        360 
GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT 

       370        380        390        400        410        420 
NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK GKGTTITSVL PKPALVASRV 

       430        440        450        460        470        480 
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD 

       490        500        510        520        530        540 
AVYFLPITPQ FVTEVIKAER PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES 

       550        560        570        580        590        600 
IMATEDRQLF SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC 

       610        620        630        640        650        660 
PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT 

       670        680        690        700        710        720 
GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS 

       730        740        750        760        770        780 
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR 

       790        800        810        820        830        840 
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR 

       850        860        870        880        890        900 
KELSEPSSTR IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT 

       910        920        930        940        950        960 
EETLRQAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV 

       970        980        990       1000       1010       1020 
TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV 

      1030       1040       1050       1060       1070       1080 
STDFDECDKL YFEELSLERI LDIYHQEACN GCIISVGGQI PNNLAVPLYK NGVKIMGTSP 

      1090       1100       1110       1120       1130       1140 
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN 

      1150       1160       1170       1180       1190       1200 
VVFSEDEMKR FLEEATRVSQ EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG 

      1210       1220       1230       1240       1250       1260 
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA 

      1270       1280       1290       1300       1310       1320 
SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI IPSDYVAIKA PMFSWPRLRD 

      1330       1340       1350       1360       1370       1380 
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ 

      1390       1400       1410       1420       1430       1440 
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN 

      1450       1460       1470       1480       1490       1500 
NNTKFVHDNY VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA 

« Hide

References

[1]"Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat."
Nyunoya H., Broglie K.E., Widgren E.E., Lusty C.J.
J. Biol. Chem. 260:9346-9356(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Rat carbamyl-phosphate synthetase I gene. Promoter sequence and tissue-specific transcriptional regulation in vitro."
Lagace M., Howell B.W., Burak R., Lusty C.J., Shore G.C.
J. Biol. Chem. 262:10415-10418(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
[3]"Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase."
Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E., Yefimenko I., Rubio V., Cervera J.
Biochem. J. 424:211-220(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, ALLOSTERIC ACTIVATOR NAG BINDING SITE, KINETIC PARAMETERS, MUTAGENESIS OF THR-1391; THR-1394; TRP-1410; ASN-1437 AND ASN-1440.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12335 expand/collapse EMBL AC list , M11710, M12318, M12319, M12320, M12321, M12322, M12323, M12324, M12325, M12326, M12327, M12328 Genomic DNA. Translation: AAB59717.1.
J02805 Genomic DNA. Translation: AAA40959.1.
PIRSYRTCA. A28481.
RefSeqNP_058768.1. NM_017072.1.
UniGeneRn.53968.

3D structure databases

ProteinModelPortalP07756.
SMRP07756. Positions 1343-1478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000019021.

Protein family/group databases

MEROPSC26.951.

PTM databases

PhosphoSiteP07756.

Proteomic databases

PaxDbP07756.
PRIDEP07756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704.
GeneID497840.
KEGGrno:497840.
UCSCRGD:2395. rat.

Organism-specific databases

CTD1373.
RGD2395. Cps1.

Phylogenomic databases

eggNOGCOG0458.
GeneTreeENSGT00390000015604.
HOGENOMHOG000234583.
HOVERGENHBG000279.
InParanoidP07756.
KOK01948.
OMAFDKFQGA.
OrthoDBEOG7M6D6F.
PhylomeDBP07756.

Enzyme and pathway databases

SABIO-RKP07756.

Gene expression databases

GenevestigatorP07756.

Family and domain databases

Gene3D1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.50.30.20. 1 hit.
HAMAPMF_01209. CPSase_S_chain.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR017926. GATASE.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSPR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF48108. SSF48108. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsTIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio697797.
PROP07756.

Entry information

Entry nameCPSM_RAT
AccessionPrimary (citable) accession number: P07756
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families