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Protein

Adenylate cyclase type 5

Gene

ADCY5

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:1618857, PubMed:8428899, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca2+ in response to increased blood glucose levels and contributes to the regulation of Ca2+-dependent insulin secretion (By similarity).By similarity7 Publications
Isoform 2: Lacks catalytic activity by itself, but can associate with isoform 1 to form active adenylyl cyclase.1 Publication

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.7 Publications

Cofactori

Mg2+3 Publications, Mn2+2 PublicationsNote: Binds 2 magnesium ions per subunit (PubMed:16766715, PubMed:19243146). Is also active with manganese (in vitro) (PubMed:11087399, PubMed:16766715).1 Publication3 Publications

Enzyme regulationi

Activated by forskolin (PubMed:1618857, PubMed:8428899). Activated by GNAS. Activity is further increased by interaction with the G-protein beta and gamma subunit complex formed by GNB1 and GNG2 (By similarity). Is not activated by calmodulin. Inhibited by adenosine and ATP analogs. Inhibited by calcium ions, already at micromolar concentrations (PubMed:1618857). Phosphorylation by RAF1 results in its activation (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi477 – 4771Magnesium 1; catalyticCombined sources1 Publication
Metal bindingi477 – 4771Magnesium 2; catalytic1 Publication
Metal bindingi478 – 4781Magnesium 2; via carbonyl oxygen; catalytic1 Publication
Metal bindingi521 – 5211Magnesium 1; catalyticCombined sources1 Publication
Metal bindingi521 – 5211Magnesium 2; catalytic1 Publication
Binding sitei565 – 5651ATP4 Publications
Binding sitei1127 – 11271ATPBy similarity
Binding sitei1248 – 12481ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi477 – 4826ATP4 Publications
Nucleotide bindingi519 – 5213ATP4 Publications
Nucleotide bindingi1201 – 12033ATPBy similarity
Nucleotide bindingi1208 – 12125ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 5 (EC:4.6.1.17 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 5
Adenylate cyclase type V
Adenylyl cyclase 5
Ca(2+)-inhibitable adenylyl cyclase
Gene namesi
Name:ADCY5
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

  • Cell membrane 2 Publications; Multi-pass membrane protein Curated
  • Cell projectioncilium By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 244244CytoplasmicSequence analysisAdd
BLAST
Transmembranei245 – 26521HelicalSequence analysisAdd
BLAST
Transmembranei271 – 29121HelicalSequence analysisAdd
BLAST
Transmembranei302 – 32221HelicalSequence analysisAdd
BLAST
Transmembranei328 – 34821HelicalSequence analysisAdd
BLAST
Transmembranei352 – 37221HelicalSequence analysisAdd
BLAST
Transmembranei377 – 39721HelicalSequence analysisAdd
BLAST
Topological domaini398 – 765368CytoplasmicSequence analysisCuratedAdd
BLAST
Transmembranei766 – 78621HelicalSequence analysisAdd
BLAST
Transmembranei792 – 81221HelicalSequence analysisAdd
BLAST
Transmembranei839 – 85921HelicalSequence analysisAdd
BLAST
Transmembranei908 – 92821HelicalSequence analysisAdd
BLAST
Transmembranei930 – 95021HelicalSequence analysisAdd
BLAST
Transmembranei988 – 100821HelicalSequence analysisAdd
BLAST
Topological domaini1009 – 1265257CytoplasmicSequence analysisCuratedAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi477 – 4771D → A or N: Almost abolishes enzyme activity. Abolishes enzyme activity; when associated with A-521 or N-521. 1 Publication
Mutagenesisi521 – 5211D → A or N: Almost abolishes enzyme activity. Abolishes enzyme activity; when associated with A-396 or N-396. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12651265Adenylate cyclase type 5PRO_0000195693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131PhosphoserineBy similarity
Modified residuei168 – 1681PhosphoserineBy similarity
Modified residuei669 – 6691PhosphoserineBy similarity
Glycosylationi873 – 8731N-linked (GlcNAc...)Sequence analysis
Glycosylationi890 – 8901N-linked (GlcNAc...)Sequence analysis
Glycosylationi976 – 9761N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP30803.

Expressioni

Tissue specificityi

Isoform 1 is detected in heart, and at lower levels in brain (PubMed:1618857). Isoform 2 is detected in heart (PubMed:8428899).2 Publications

Interactioni

Subunit structurei

Interacts with GNAS (PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Interacts with GNB1 and GNG2 (By similarity). Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (By similarity). Interacts with RAF1 (By similarity).By similarity6 Publications

Protein-protein interaction databases

DIPiDIP-179N.
IntActiP30803. 1 interaction.
STRINGi9615.ENSCAFP00000017783.

Structurei

Secondary structure

1
1265
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi464 – 47916Combined sources
Helixi481 – 4877Combined sources
Helixi490 – 51122Combined sources
Beta strandi514 – 5196Combined sources
Beta strandi522 – 5276Combined sources
Helixi536 – 55823Combined sources
Beta strandi563 – 57715Combined sources
Beta strandi579 – 5824Combined sources
Beta strandi586 – 5894Combined sources
Helixi590 – 60011Combined sources
Beta strandi603 – 6053Combined sources
Beta strandi606 – 6094Combined sources
Turni612 – 6198Combined sources
Beta strandi623 – 6253Combined sources
Helixi628 – 6303Combined sources
Helixi633 – 6375Combined sources
Beta strandi643 – 6453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZSX-ray2.30A442-656[»]
1CJKX-ray3.00A445-661[»]
1CJTX-ray2.80A445-661[»]
1CJUX-ray2.80A445-661[»]
1CJVX-ray3.00A445-661[»]
1CS4X-ray2.50A442-661[»]
1CULX-ray2.40A445-661[»]
1TL7X-ray2.80A445-661[»]
1U0HX-ray2.90A442-661[»]
2GVDX-ray2.90A444-661[»]
2GVZX-ray3.27A444-661[»]
3C14X-ray2.68A444-661[»]
3C15X-ray2.78A444-661[»]
3C16X-ray2.87A444-661[»]
3G82X-ray3.11A444-661[»]
3MAAX-ray3.00A444-661[»]
ProteinModelPortaliP30803.
SMRiP30803. Positions 457-646, 1066-1241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30803.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini472 – 599128Guanylate cyclase 1PROSITE-ProRule annotationAdd
BLAST
Domaini1075 – 1214140Guanylate cyclase 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain.5 Publications

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 2 guanylate cyclase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP30803.
KOiK08045.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P30803-1) [UniParc]FASTAAdd to basket

Also known as: V

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
MSGPRSASPP GCAATRGGPE HRAAWGEAEA RANGHPHAAG GATRGCSKKP
60 70 80 90 100
GGAVTPQLQQ QQQQQQHEQQ HEQQQHEQQQ HVQQQQRLAK RWRGDDDPPL
110 120 130 140 150
GGDDPLAGGF GFSFRSRSAW QERGGDDCGR GSRRRRRGAA GGGSSRAPPA
160 170 180 190 200
GGGGGPAAAG GAEVRPRSVE LGLDERRGRG RAEPEPEAEA GAPGGDRGAR
210 220 230 240 250
DGDGPAGPGA CCRALLQIFR SKKFPSDKLE RLYQRYFFRL NQSSLTMLMA
260 270 280 290 300
VLVLVCLVML AFHAARPPLR LPHLAVLAAA VGVILVMAVL CNRAAFHQDH
310 320 330 340 350
MGLACYALIA VVLAVQVVGL LLPQPRSASE GIWWTVFFIY TIYTLLPVRM
360 370 380 390 400
RAAVLSGVLL SALHLAIALR ANAQDRFLLK QLVSNVLIFS CTNIVGVCTH
410 420 430 440 450
YPAEVSQRQA FQETRECIQA RLHSQRENQQ QERLLLSVLP RHVAMEMKAD
460 470 480 490 500
INAKQEDMMF HKIYIQKHDN VSILFADIEG FTSLASQCTA QELVMTLNEL
510 520 530 540 550
FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC VEMGMDMIEA
560 570 580 590 600
ISLVREVTGV NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA
610 620 630 640 650
GGKAGRIHIT KATLSYLNGD YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ
660 670 680 690 700
KRKEEKAMIA KMNRQRTNSI GHNPPHWGAE RPFYNHLGGN QVSKEMKRMG
710 720 730 740 750
FEDPKDKNAQ ESANPEDEVD EFLGRAIDAR SIDRLRSEHV RKFLLTFREP
760 770 780 790 800
DLEKKYSKQV DDRFGAYVAC ASLVFLFICF VQITIVPHSV FMLSFYLTCF
810 820 830 840 850
LLLTLVVFVS VIYSCVKLFP GPLQSLSRKI VRSKTNSTLV GVFTITLVFL
860 870 880 890 900
SAFVNMFMCN SEDLLGCLAD EHNISTSRVN ACHVAASAAN LSLGDEQGFC
910 920 930 940 950
GTPWPSCNFP EYFTYSVLLS LLACSVFLQI SCIGKLVLML AIELIYVLVV
960 970 980 990 1000
EVPRVTLFDN ADLLVTANAI DFNNNNGTSQ CPEHATKVAL KVVTPIIISV
1010 1020 1030 1040 1050
FVLALYLHAQ QVESTARLDF LWKLQATEEK EEMEELQAYN RRLLHNILPK
1060 1070 1080 1090 1100
DVAAHFLARE RRNDELYYQS CECVAVMFAS IANFSEFYVE LEANNEGVEC
1110 1120 1130 1140 1150
LRVLNEIIAD FDEIISEDRF RQLEKIKTIG STYMAASGLN DSTYDKVGKT
1160 1170 1180 1190 1200
HIKALADFAM KLMDQMKYIN EHSFNNFQMK IGLNIGPVVA GVIGARKPQY
1210 1220 1230 1240 1250
DIWGNTVNVA SRMDSTGVPD RIQVTTDMYQ VLAANTYQLE CRGVVKVKGK
1260
GEMMTYFLNG GPPLS
Length:1,265
Mass (Da):140,319
Last modified:May 30, 2000 - v2
Checksum:i414322F64153DFB4
GO
Isoform 2 (identifier: P30803-2) [UniParc]FASTAAdd to basket

Also known as: V-alpha

The sequence of this isoform differs from the canonical sequence as follows:
     653-677: KEEKAMIAKMNRQRTNSIGHNPPHW → VRRGGGGPRPGGADSPGWWGASAGP
     678-1265: Missing.

Show »
Length:677
Mass (Da):73,690
Checksum:iAAB94BCFEBE08CC0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei653 – 67725KEEKA…NPPHW → VRRGGGGPRPGGADSPGWWG ASAGP in isoform 2. 1 PublicationVSP_000242Add
BLAST
Alternative sequencei678 – 1265588Missing in isoform 2. 1 PublicationVSP_000243Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88649 mRNA. Translation: AAC32726.1.
M97886 mRNA. Translation: AAA30827.1. Sequence problems.
PIRiA42904.
A45195.
RefSeqiNP_001161932.1. NM_001168460.1. [P30803-1]
UniGeneiCfa.1267.

Genome annotation databases

GeneIDi403859.
KEGGicfa:403859.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88649 mRNA. Translation: AAC32726.1.
M97886 mRNA. Translation: AAA30827.1. Sequence problems.
PIRiA42904.
A45195.
RefSeqiNP_001161932.1. NM_001168460.1. [P30803-1]
UniGeneiCfa.1267.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZSX-ray2.30A442-656[»]
1CJKX-ray3.00A445-661[»]
1CJTX-ray2.80A445-661[»]
1CJUX-ray2.80A445-661[»]
1CJVX-ray3.00A445-661[»]
1CS4X-ray2.50A442-661[»]
1CULX-ray2.40A445-661[»]
1TL7X-ray2.80A445-661[»]
1U0HX-ray2.90A442-661[»]
2GVDX-ray2.90A444-661[»]
2GVZX-ray3.27A444-661[»]
3C14X-ray2.68A444-661[»]
3C15X-ray2.78A444-661[»]
3C16X-ray2.87A444-661[»]
3G82X-ray3.11A444-661[»]
3MAAX-ray3.00A444-661[»]
ProteinModelPortaliP30803.
SMRiP30803. Positions 457-646, 1066-1241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-179N.
IntActiP30803. 1 interaction.
STRINGi9615.ENSCAFP00000017783.

Proteomic databases

PaxDbiP30803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403859.
KEGGicfa:403859.

Organism-specific databases

CTDi111.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP30803.
KOiK08045.

Miscellaneous databases

EvolutionaryTraceiP30803.
NextBioi20817352.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and characterization of a novel cardiac adenylylcyclase cDNA."
    Ishikawa Y., Katsushika S., Chen L., Halnon N.J., Kawabe J., Homcy C.J.
    J. Biol. Chem. 267:13553-13557(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Heart muscle.
  2. "In vivo generation of an adenylylcyclase isoform with a half-molecule motif."
    Katsushika S., Kawabe J., Homcy C.J., Ishikawa Y.
    J. Biol. Chem. 268:2273-2276(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ENZYME REGULATION, DOMAIN, TISSUE SPECIFICITY.
    Tissue: Heart muscle.
  3. Tomlinson J., Okumura S., Ishikawa Y.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
  4. "Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS."
    Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.
    Science 278:1907-1916(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 445-661 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS, INTERACTION WITH GNAS, DOMAIN.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 445-661 OF CHIMERA WITH ADCY5 IN COMPLEX WITH ATP ANALOGS; MAGNESIUM; MANGANESE AND GNAS, INTERACTION WITH GNAS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF ASP-477 AND ASP-521, DOMAIN.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 445-661 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; ATP ANALOG AND MAGNESIUM, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, INTERACTION WITH GNAS, DOMAIN.
  7. "Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate."
    Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.
    J. Biol. Chem. 280:7253-7261(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 445-661 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; MAGNESIUM AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GNAS, DOMAIN.
  8. "Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors."
    Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., Sprang S.R.
    Mol. Pharmacol. 70:878-886(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 444-661 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; MANGANESE AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, DOMAIN.
  9. "Structural basis for inhibition of mammalian adenylyl cyclase by calcium."
    Mou T.C., Masada N., Cooper D.M., Sprang S.R.
    Biochemistry 48:3387-3397(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 444-661 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; ATP AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, DOMAIN.

Entry informationi

Entry nameiADCY5_CANLF
AccessioniPrimary (citable) accession number: P30803
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 30, 2000
Last modified: May 11, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.