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Protein
Submitted name:

Complement C1s subcomponent

Gene

C1s

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei481 – 4811Charge relay systemUniRule annotation
Active sitei535 – 5351Charge relay systemUniRule annotation
Active sitei637 – 6371Charge relay systemUniRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. complement activation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, ProteaseSAAS annotation

Enzyme and pathway databases

ReactomeiREACT_298926. Classical antibody-mediated complement activation.
REACT_351741. Initial triggering of complement.

Protein family/group databases

MEROPSiS01.193.

Names & Taxonomyi

Protein namesi
Submitted name:
Complement C1s subcomponentImported
Submitted name:
RCG29725, isoform CRA_bImported
Gene namesi
Name:C1sImported
ORF Names:rCG_29725Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi619983. C1s.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 89UniRule annotation
Disulfide bondi141 ↔ 153UniRule annotation
Disulfide bondi149 ↔ 162UniRule annotation
Disulfide bondi164 ↔ 177UniRule annotation
Disulfide bondi181 ↔ 208UniRule annotation
Disulfide bondi300 ↔ 347UniRule annotation
Disulfide bondi327 ↔ 360UniRule annotation
Disulfide bondi365 ↔ 409UniRule annotation
Disulfide bondi392 ↔ 427UniRule annotation
Disulfide bondi431 ↔ 555Interchain (between heavy and light chains)UniRule annotation
Disulfide bondi601 ↔ 624UniRule annotation
Disulfide bondi633 ↔ 665UniRule annotation

Keywords - PTMi

Disulfide bondUniRule annotationSAAS annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S1 family.UniRule annotation
Contains peptidase S1 domain.SAAS annotation

Keywords - Domaini

EGF-like domainUniRule annotationSAAS annotation, RepeatSAAS annotation

Phylogenomic databases

GeneTreeiENSGT00760000118890.
OMAiPTMYGEI.
OrthoDBiEOG7W6WK4.
TreeFamiTF330373.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

G3V7L3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKSPEMWCF VFFSLLASFS AEPTMYGEIL SPNYPQAYPN EVVKTWDIEV
60 70 80 90 100
PEGFGIHLYF THLDMELSEN CAYDSVQIIS GGIEEERLCG QRTSKSPNSP
110 120 130 140 150
IVEEFQFPYN RLQVVFTSDF SNEERFTGFA AYYSAVDVNE CTDFTDVPCS
160 170 180 190 200
HFCNNFIGGY FCSCPPEYFL HDDMRTCGVN CSGDVFTALI GEIASPNYPN
210 220 230 240 250
PYPENSRCEY QIRLQEGFRL VLTIRREDFD VEPADSEGNC HDSLTFAAKN
260 270 280 290 300
QQFGPYCGNG FPGPLTIKTQ SNTLDIVFQT DLTGQNKGWK LRYHGDPIPC
310 320 330 340 350
PKEISANSIW EPEKAKYVFK DVVKITCVDG FEVVEGNVGS TSFYSTCQSN
360 370 380 390 400
GQWSNSRLEC QPVDCGVPEP IENGKVEDPE DTVFGSVIHY TCEEPYYYME
410 420 430 440 450
QEEGGEYHCA ANGSWVNDQL GVELPKCIPV CGVPTEPFKV QQRIFGGYST
460 470 480 490 500
KIQSFPWQVY FESPRGGGAL IDEYWVLTAA HVVEGNSDPV MYVGSTLLKI
510 520 530 540 550
ERLRNAQRLI TERVIIHPSW KQEDDLNTRT NFDNDIALVQ LKDPVKMGPT
560 570 580 590 600
VAPICLPETS SDYNPSEGDL GLISGWGRTE NRTNVIQLRG AKLPITSLEK
610 620 630 640 650
CQQVKVENPK ARSNDYVFTD NMICAGEKGV DSCEGDSGGA FALPVPNVKD
660 670 680 690
PKFYVAGLVS WGKKCGTYGI YTKVKNYVDW ILKTMQENSG PKKD
Length:694
Mass (Da):77,713
Last modified:November 16, 2011 - v1
Checksum:i455A9EE10C8CC12F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06033512 Genomic DNA. No translation available.
CH473964 Genomic DNA. Translation: EDM01952.1.

Genome annotation databases

EnsembliENSRNOT00000016330; ENSRNOP00000016330; ENSRNOG00000011971.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06033512 Genomic DNA. No translation available.
CH473964 Genomic DNA. Translation: EDM01952.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016330; ENSRNOP00000016330; ENSRNOG00000011971.

Organism-specific databases

RGDi619983. C1s.

Phylogenomic databases

GeneTreeiENSGT00760000118890.
OMAiPTMYGEI.
OrthoDBiEOG7W6WK4.
TreeFamiTF330373.

Enzyme and pathway databases

ReactomeiREACT_298926. Classical antibody-mediated complement activation.
REACT_351741. Initial triggering of complement.

Miscellaneous databases

NextBioi35583970.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (SEP-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiG3V7L3_RAT
AccessioniPrimary (citable) accession number: G3V7L3
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: April 29, 2015
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.