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P01026

- CO3_RAT

UniProt

P01026 - CO3_RAT

Protein

Complement C3

Gene

C3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.1 Publication
    Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. In chronic inflammation, acts as a chemoattractant for neutrophils (PubMed:8352775).1 Publication
    C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation.1 Publication
    Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei747 – 7482Cleavage; by carboxypeptidasesBy similarity
    Sitei748 – 7492Cleavage; by C3 convertase
    Sitei959 – 9602Cleavage; by factor ISequence Analysis
    Sitei1303 – 13042Cleavage; by factor IBy similarity
    Sitei1320 – 13212Cleavage; by factor IBy similarity

    GO - Molecular functioni

    1. C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
    2. cofactor binding Source: RGD
    3. endopeptidase inhibitor activity Source: InterPro
    4. lipid binding Source: RGD
    5. protein binding Source: RGD

    GO - Biological processi

    1. blood coagulation Source: RGD
    2. chemotaxis Source: UniProtKB-KW
    3. complement activation Source: RGD
    4. complement activation, alternative pathway Source: UniProtKB-KW
    5. complement activation, classical pathway Source: RGD
    6. fatty acid metabolic process Source: UniProtKB-KW
    7. inflammatory response Source: UniProtKB-KW
    8. positive regulation of developmental growth Source: RGD
    9. positive regulation of ERK1 and ERK2 cascade Source: RGD
    10. positive regulation of glucose transport Source: UniProtKB
    11. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    12. positive regulation of lipid storage Source: UniProtKB
    13. positive regulation of protein phosphorylation Source: UniProtKB
    14. regulation of triglyceride biosynthetic process Source: UniProtKB
    15. response to estradiol Source: RGD
    16. response to estrogen Source: RGD
    17. response to glucocorticoid Source: RGD
    18. response to magnesium ion Source: RGD
    19. response to progesterone Source: RGD
    20. tolerance induction Source: RGD

    Keywords - Biological processi

    Chemotaxis, Complement alternate pathway, Complement pathway, Fatty acid metabolism, Immunity, Inflammatory response, Innate immunity, Lipid metabolism

    Protein family/group databases

    MEROPSiI39.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement C3
    Cleaved into the following 12 chains:
    Gene namesi
    Name:C3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2232. C3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: RGD

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 16631639Complement C3PRO_0000005937Add
    BLAST
    Chaini25 – 666642Complement C3 beta chainPRO_0000005938Add
    BLAST
    Chaini568 – 66699C3-beta-cPRO_0000395292Add
    BLAST
    Chaini671 – 1663993Complement C3 alpha chainPRO_0000005939Add
    BLAST
    Chaini671 – 74878C3a anaphylatoxinPRO_0000005940Add
    BLAST
    Chaini671 – 74777Acylation stimulating proteinBy similarityPRO_0000419937Add
    BLAST
    Chaini749 – 1663915Complement C3b alpha' chainPRO_0000005941Add
    BLAST
    Chaini749 – 959211Complement C3c alpha' chain fragment 1PRO_0000273950Add
    BLAST
    Chaini960 – 1303344Complement C3dg fragmentBy similarityPRO_0000273951Add
    BLAST
    Chaini960 – 100142Complement C3g fragmentBy similarityPRO_0000273952Add
    BLAST
    Chaini1002 – 1303302Complement C3d fragmentBy similarityPRO_0000273953Add
    BLAST
    Peptidei1304 – 132017Complement C3f fragmentBy similarityPRO_0000273954Add
    BLAST
    Chaini1321 – 1663343Complement C3c alpha' chain fragment 2By similarityPRO_0000273955Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi558 ↔ 816Interchain (between beta and alpha chains)PROSITE-ProRule annotation
    Disulfide bondi626 ↔ 661By similarity
    Disulfide bondi693 ↔ 720By similarity
    Disulfide bondi694 ↔ 727By similarity
    Disulfide bondi707 ↔ 728By similarity
    Disulfide bondi873 ↔ 1513By similarity
    Glycosylationi939 – 9391N-linked (GlcNAc...)Curated
    Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)By similarity
    Disulfide bondi1101 ↔ 1158By similarity
    Disulfide bondi1358 ↔ 1489By similarity
    Disulfide bondi1389 ↔ 1458By similarity
    Disulfide bondi1506 ↔ 1511By similarity
    Disulfide bondi1518 ↔ 1590By similarity
    Disulfide bondi1537 ↔ 1661By similarity
    Glycosylationi1617 – 16171N-linked (GlcNAc...)Curated

    Post-translational modificationi

    C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by dietary chylomicrons By similarity.By similarity
    Phosphorylation sites are present in the extracellular medium.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Thioester bond

    Proteomic databases

    PRIDEiP01026.

    PTM databases

    PhosphoSiteiP01026.

    Expressioni

    Gene expression databases

    GenevestigatoriP01026.

    Interactioni

    Subunit structurei

    C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). Interacts with VSIG4. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi246419. 1 interaction.

    Structurei

    Secondary structure

    1
    1663
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1013 – 103119
    Helixi1034 – 10374
    Helixi1039 – 10413
    Helixi1042 – 105716
    Helixi1076 – 108914
    Turni1090 – 10923
    Helixi1097 – 111115
    Helixi1127 – 11348
    Helixi1139 – 115820
    Turni1159 – 11613
    Helixi1165 – 118016
    Helixi1186 – 119813
    Helixi1206 – 12138
    Turni1216 – 12183
    Helixi1226 – 124217
    Turni1246 – 12483
    Helixi1249 – 125810
    Helixi1269 – 128517

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QQFX-ray1.45A1010-1286[»]
    1QSJX-ray1.90A/B/C/D1010-1286[»]
    ProteinModelPortaliP01026.
    SMRiP01026. Positions 25-663, 672-1663.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01026.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini693 – 72836Anaphylatoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini1518 – 1661144NTRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1424 – 145633Properdin-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
    Contains 1 NTR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005110.
    KOiK03990.
    PhylomeDBiP01026.

    Family and domain databases

    Gene3Di1.20.91.20. 1 hit.
    1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProiIPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR000020. Anaphylatoxin/fibulin.
    IPR018081. Anaphylatoxin_comp_syst.
    IPR001840. Anaphylatoxn_comp_syst_dom.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR001134. Netrin_domain.
    IPR018933. Netrin_module_non-TIMP.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR008993. TIMP-like_OB-fold.
    [Graphical view]
    PfamiPF00207. A2M. 1 hit.
    PF07678. A2M_comp. 1 hit.
    PF01835. A2M_N. 1 hit.
    PF07703. A2M_N_2. 1 hit.
    PF07677. A2M_recep. 1 hit.
    PF01821. ANATO. 1 hit.
    PF01759. NTR. 1 hit.
    PF10569. Thiol-ester_cl. 1 hit.
    [Graphical view]
    PRINTSiPR00004. ANAPHYLATOXN.
    SMARTiSM00104. ANATO. 1 hit.
    SM00643. C345C. 1 hit.
    [Graphical view]
    SUPFAMiSSF47686. SSF47686. 1 hit.
    SSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF50242. SSF50242. 1 hit.
    PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    PS01177. ANAPHYLATOXIN_1. 1 hit.
    PS01178. ANAPHYLATOXIN_2. 1 hit.
    PS50189. NTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01026-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPTSGSQLL VLLLLLASSL LALGSPMYSI ITPNVLRLES EETFILEAHD     50
    AQGDVPVTVT VQDFLKKQVL TSEKTVLTGA TGHLNRVFIK IPASKEFNAD 100
    KGHKYVTVVA NFGATVVEKA VLVSFQSGYL FIQTDKTIYT PGSTVFYRIF 150
    TVDNNLLPVG KTVVIVIETP DGVPIKRDIL SSHNQYGILP LSWNIPELVN 200
    MGQWKIRAFY EHAPKQTFSA EFEVKEYVLP SFEVLVEPTE KFYYIHGPKG 250
    LEVSITARFL YGKNVDGTAF VIFGVQDEDK KISLALSLTR VLIEDGSGEA 300
    VLSRKVLMDG VRPSSPEALV GKSLYVSVTV ILHSGSDMVE AERSGIPIVT 350
    SPYQIHFTKT PKFFKPAMPF DLMVFVTNPD GSPARRVPVV TQGSDAQALT 400
    QDDGVAKLSV NTPNNRQPLT ITVSTKKEGI PDARQATRTM QAQPYSTMHN 450
    SNNYLHLSVS RVELKPGDNL NVNFHLRTDA GQEAKIRYYT YLVMNKGKLL 500
    KAGRQVREPG QDLVVLSLPI TPEFIPSFRL VAYYTLIGAN GQREVVADSV 550
    WVDVKDSCVG TLVVKGDPRD NRQPAPGHQT TLRIEGNQGA RVGLVAVDKG 600
    VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLTFKTNQG 650
    LQTDQREDPE CAKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD 700
    IPMPYSCQRR ARLITQGESC LKAFMDCCNY ITKLREQHRR DHVLGLARSD 750
    VDEDIIPEED IISRSHFPES WLWTIEELKE PEKNGISTKV MNIFLKDSIT 800
    TWEILAVSLS DKKGICVADP YEITVMQDFF IDLRLPYSVV RNEQVEIRAV 850
    LFNYREQEKL KVRVELLHNP AFCSMATAKK RYYQTIEIPP KSSVAVPYVI 900
    VPLKIGLQEV EVKAAVFNHF ISDGVKKILK VVPEGMRVNK TVAVRTLDPE 950
    HLNQGGVQRE DVNAADLSDQ VPDTDSETRI LLQGTPVAQM AEDAVDGERL 1000
    KHLIVTPSGC GEQNMIGMTP TVIAVHYLDQ TEQWEKFGLE KRQEALELIK 1050
    KGYTQQLAFK QPISAYAAFN NRPPSTWLTA MWSRSFSLAA NLIAIDSQVL 1100
    CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNTKEAD VSLTAFVLIA 1150
    LQEARDICEG QVNSLPGSIN KAGEYLEASY LNLQRPYTVA IAGYALALMN 1200
    KLEEPYLTKF LNTAKDRNRW EEPGQQLYNV EATSYALLAL LLLKDFDSVP 1250
    PVVRWLNDER YYGGGYGSTQ ATFMVFQALA QYRADVPDHK DLNMDVSLHL 1300
    PSRSSPTVFR LLWESGSLLR SEETKQNEGF SLTAKGKGQG TLSVVTVYHA 1350
    KVKGKTTCKK FDLRVTIKPA PETAKKPQDA KSSMILDICT RYLGDVDATM 1400
    SILDISMMTG FIPDTNDLEL LSSGVDRYIS KYEMDKAFSN KNTLIIYLEK 1450
    ISHSEEDCLS FKVHQFFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG 1500
    MLSKLCHNEM CRCAEENCFM HQSQDQVSLN ERLDKACEPG VDYVYKTKLT 1550
    TIELSDDFDE YIMTIEQVIK SGSDEVQAGQ ERRFISHVKC RNALKLQKGK 1600
    QYLMWGLSSD LWGEKPNTSY IIGKDTWVEH WPEAEERQDQ KNQKQCEDLG 1650
    AFTETMVVFG CPN 1663
    Length:1,663
    Mass (Da):186,460
    Last modified:August 1, 1990 - v3
    Checksum:i2F87CCB143CDD4BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti704 – 7041P → K in AAG00532. 1 PublicationCurated
    Sequence conflicti721 – 7222LK → KL AA sequence (PubMed:309768)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52477 mRNA. Translation: CAA36716.1.
    AF286158 mRNA. Translation: AAG00532.1.
    M29866 mRNA. Translation: AAA40837.1.
    PIRiS15764. C3RT.
    RefSeqiNP_058690.2. NM_016994.2.
    UniGeneiRn.11378.

    Genome annotation databases

    GeneIDi24232.
    KEGGirno:24232.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52477 mRNA. Translation: CAA36716.1 .
    AF286158 mRNA. Translation: AAG00532.1 .
    M29866 mRNA. Translation: AAA40837.1 .
    PIRi S15764. C3RT.
    RefSeqi NP_058690.2. NM_016994.2.
    UniGenei Rn.11378.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QQF X-ray 1.45 A 1010-1286 [» ]
    1QSJ X-ray 1.90 A/B/C/D 1010-1286 [» ]
    ProteinModelPortali P01026.
    SMRi P01026. Positions 25-663, 672-1663.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246419. 1 interaction.

    Protein family/group databases

    MEROPSi I39.950.

    PTM databases

    PhosphoSitei P01026.

    Proteomic databases

    PRIDEi P01026.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24232.
    KEGGi rno:24232.

    Organism-specific databases

    CTDi 718.
    RGDi 2232. C3.

    Phylogenomic databases

    HOVERGENi HBG005110.
    KOi K03990.
    PhylomeDBi P01026.

    Miscellaneous databases

    EvolutionaryTracei P01026.
    NextBioi 602683.

    Gene expression databases

    Genevestigatori P01026.

    Family and domain databases

    Gene3Di 1.20.91.20. 1 hit.
    1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProi IPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR000020. Anaphylatoxin/fibulin.
    IPR018081. Anaphylatoxin_comp_syst.
    IPR001840. Anaphylatoxn_comp_syst_dom.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR001134. Netrin_domain.
    IPR018933. Netrin_module_non-TIMP.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR008993. TIMP-like_OB-fold.
    [Graphical view ]
    Pfami PF00207. A2M. 1 hit.
    PF07678. A2M_comp. 1 hit.
    PF01835. A2M_N. 1 hit.
    PF07703. A2M_N_2. 1 hit.
    PF07677. A2M_recep. 1 hit.
    PF01821. ANATO. 1 hit.
    PF01759. NTR. 1 hit.
    PF10569. Thiol-ester_cl. 1 hit.
    [Graphical view ]
    PRINTSi PR00004. ANAPHYLATOXN.
    SMARTi SM00104. ANATO. 1 hit.
    SM00643. C345C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47686. SSF47686. 1 hit.
    SSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF50242. SSF50242. 1 hit.
    PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    PS01177. ANAPHYLATOXIN_1. 1 hit.
    PS01178. ANAPHYLATOXIN_2. 1 hit.
    PS50189. NTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide and deduced amino acid sequence of rat complement C3."
      Misumi Y., Sohda M., Ikehara Y.
      Nucleic Acids Res. 18:2178-2178(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Liver.
    2. "Complement component C3-derived neutrophil chemotactic factors purified from exudate of rat carrageenin-induced inflammation."
      Nakagawa H., Komorita N.
      Biochem. Biophys. Res. Commun. 194:1181-1187(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 568-592 AND 671-687, IDENTIFICATION OF C3A ANAPHYLATOXIN AND C3-BETA-C, FUNCTION.
      Tissue: Neutrophil.
    3. "Purification, characterization, and amino acid sequence of rat anaphylatoxin (C3a)."
      Jacobs J.W., Rubin J.S., Hugli T.E., Bogardt R.A. Jr., Mariz I.K., Daniels J.S., Daughaday W.H., Bradshaw R.A.
      Biochemistry 17:5031-5038(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 671-748.
    4. "Nucleotide and deduced amino acid sequence of rat complement component C3a derived from Sprague-Dawley strain."
      Wahrmann M., Krieger S., Liewehr A.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 671-748.
      Strain: Sprague-Dawley.
      Tissue: Liver.
    5. "Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment."
      Zanotti G., Bassetto A., Battistutta R., Folli C., Arcidiaco P., Stoppini M., Berni R.
      Biochim. Biophys. Acta 1478:232-238(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 960-969, X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 1010-1286.
    6. "Estrogen regulation of tissue-specific expression of complement C3."
      Sundstrom S.A., Komm B.S., Ponce-De-Leon H., Yi Z., Teuscher C., Lyttle C.R.
      J. Biol. Chem. 264:16941-16947(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1316-1595.

    Entry informationi

    Entry nameiCO3_RAT
    AccessioniPrimary (citable) accession number: P01026
    Secondary accession number(s): Q9ET19, Q9QV57, Q9QV58
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3