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Q8CG14

- CS1A_MOUSE

UniProt

Q8CG14 - CS1A_MOUSE

Protein

Complement C1s-A subcomponent

Gene

C1sa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (27 Sep 2005)
      Previous versions | rss
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    Functioni

    C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4 By similarity.By similarity

    Catalytic activityi

    Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase.

    Enzyme regulationi

    Inhibited by SERPING1.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi60 – 601CalciumBy similarity
    Metal bindingi68 – 681CalciumBy similarity
    Metal bindingi113 – 1131CalciumBy similarity
    Metal bindingi131 – 1311CalciumBy similarity
    Metal bindingi132 – 1321Calcium; via carbonyl oxygenBy similarity
    Metal bindingi134 – 1341CalciumBy similarity
    Metal bindingi149 – 1491CalciumBy similarity
    Metal bindingi150 – 1501Calcium; via carbonyl oxygenBy similarity
    Metal bindingi153 – 1531Calcium; via carbonyl oxygenBy similarity
    Active sitei475 – 4751Charge relay systemBy similarity
    Active sitei529 – 5291Charge relay systemBy similarity
    Active sitei631 – 6311Charge relay systemBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. complement activation, classical pathway Source: UniProtKB-KW
    2. innate immune response Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    MEROPSiS01.360.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement C1s-A subcomponent (EC:3.4.21.42)
    Alternative name(s):
    C1 esterase
    Complement component 1 subcomponent s-A
    Cleaved into the following 2 chains:
    Gene namesi
    Name:C1sa
    Synonyms:C1s
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1355312. C1s.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515By similarityAdd
    BLAST
    Chaini16 – 688673Complement C1s-A subcomponentPRO_0000042193Add
    BLAST
    Chaini16 – 437422Complement C1s-A subcomponent heavy chainBy similarityPRO_0000042194Add
    BLAST
    Chaini438 – 688251Complement C1s-A subcomponent light chainBy similarityPRO_0000042195Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi65 ↔ 83By similarity
    Disulfide bondi135 ↔ 147By similarity
    Disulfide bondi143 ↔ 156By similarity
    Modified residuei149 – 1491(3R)-3-hydroxyasparagineBy similarity
    Disulfide bondi158 ↔ 171By similarity
    Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi175 ↔ 202By similarity
    Disulfide bondi234 ↔ 251By similarity
    Disulfide bondi294 ↔ 341By similarity
    Disulfide bondi321 ↔ 354By similarity
    Disulfide bondi359 ↔ 403By similarity
    Disulfide bondi386 ↔ 421By similarity
    Disulfide bondi425 ↔ 549Interchain (between heavy and light chains)PROSITE-ProRule annotation
    Disulfide bondi595 ↔ 618By similarity
    Disulfide bondi627 ↔ 659By similarity
    Glycosylationi641 – 6411N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiQ8CG14.
    PRIDEiQ8CG14.

    PTM databases

    PhosphoSiteiQ8CG14.

    Expressioni

    Tissue specificityi

    Predominantly expressed in liver.1 Publication

    Gene expression databases

    CleanExiMM_C1S.
    GenevestigatoriQ8CG14.

    Interactioni

    Subunit structurei

    C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. Activated C1s is an disulfide-linked heterodimer of a heavy chain and a light chain By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CG14.
    SMRiQ8CG14. Positions 17-683.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 130115CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini131 – 17242EGF-like; calcium-bindingSequence AnalysisAdd
    BLAST
    Domaini175 – 290116CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini292 – 35665Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini357 – 42367Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 680243Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 2 CUB domains.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.Curated
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiCOG5640.
    HOVERGENiHBG000559.
    InParanoidiQ8CG14.
    KOiK01331.
    PhylomeDBiQ8CG14.

    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.
    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.

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

    Q8CG14-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWCLVLFSLL ASFSAEPTMH GEILSPNYPQ AYPNDVVKSW DIEVPEGFGI    50
    HLYFTHVDIE PSESCAYDSV QIISGGIEEG RLCGQKTSKS PNSPIIEEFQ 100
    FPYNKLQVVF TSDFSNEERF TGFAAYYTAI DINECTDFTD VPCSHFCNNF 150
    IGGYFCSCPP EYFLHDDMRN CGVNCSGDVF TALIGEISSP NYPNPYPENS 200
    RCEYQIQLQE GFQVVVTMQR EDFDVEPADS EGNCPDSLTF ASKNQQFGPY 250
    CGNGFPGPLT IRTQSNTLGI VFQTDLMGQK KGWKLRYHGD PISCAKKITA 300
    NSTWEPDKAK YVFKDVVKIT CVDGFEVVEG HVSSTSYYST CQSDGQWSNS 350
    GLKCQPVYCG IPDPIANGKV EEPENSVFGT VVHYTCEEPY YYMEHEEGGE 400
    YRCAANGRWV NDQLGIELPR CIPACGVPTE PFQVHQRIFG GQPAKIENFP 450
    WQVFFNHPRA SGALINEYWV LTAAHVLEKI SDPLMYVGTM SVRTTLLENA 500
    QRLYSKRVFI HPSWKKEDDP NTRTNFDNDI ALVQLKDPVK MGPKVSPICL 550
    PGTSSEYNVS PGDMGLISGW GSTEKKVFVI NLRGAKVPVT SLETCKQVKE 600
    ENPTVRPEDY VFTDNMICAG EKGVDSCHGD SGGAFAFQVP NVTVPKFYVA 650
    GLVSWGKRCG TYGVYTKVKN YVDWILKTMQ ENSGPRKD 688
    Length:688
    Mass (Da):76,858
    Last modified:September 27, 2005 - v2
    Checksum:iBAC166C861CB8A25
    GO

    Sequence cautioni

    The sequence BAC39910.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761G → D in AAO15556. (PubMed:12513694)Curated
    Sequence conflicti76 – 761G → D in BAC39910. (PubMed:16141072)Curated
    Sequence conflicti86 – 861K → R in AAO15556. (PubMed:12513694)Curated
    Sequence conflicti86 – 861K → R in BAC39910. (PubMed:16141072)Curated
    Sequence conflicti305 – 3051E → Q in AAO15556. (PubMed:12513694)Curated
    Sequence conflicti305 – 3051E → Q in BAC39910. (PubMed:16141072)Curated
    Sequence conflicti378 – 3781F → L in BAC39910. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF459019 mRNA. Translation: AAO15558.1.
    AF459017, AF459015, AF459016 Genomic DNA. Translation: AAO15556.1.
    AK087522 mRNA. Translation: BAC39910.1. Different initiation.
    BC022123 mRNA. Translation: AAH22123.1.
    BC018319 mRNA. Translation: AAH18319.1.
    RefSeqiNP_001091086.1. NM_001097617.1.
    NP_659187.2. NM_144938.2.
    UniGeneiMm.219527.

    Genome annotation databases

    GeneIDi50908.
    KEGGimmu:50908.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF459019 mRNA. Translation: AAO15558.1 .
    AF459017 , AF459015 , AF459016 Genomic DNA. Translation: AAO15556.1 .
    AK087522 mRNA. Translation: BAC39910.1 . Different initiation.
    BC022123 mRNA. Translation: AAH22123.1 .
    BC018319 mRNA. Translation: AAH18319.1 .
    RefSeqi NP_001091086.1. NM_001097617.1.
    NP_659187.2. NM_144938.2.
    UniGenei Mm.219527.

    3D structure databases

    ProteinModelPortali Q8CG14.
    SMRi Q8CG14. Positions 17-683.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.360.

    PTM databases

    PhosphoSitei Q8CG14.

    Proteomic databases

    PaxDbi Q8CG14.
    PRIDEi Q8CG14.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 50908.
    KEGGi mmu:50908.

    Organism-specific databases

    CTDi 50908.
    MGIi MGI:1355312. C1s.

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG000559.
    InParanoidi Q8CG14.
    KOi K01331.
    PhylomeDBi Q8CG14.

    Miscellaneous databases

    NextBioi 307885.
    PROi Q8CG14.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_C1S.
    Genevestigatori Q8CG14.

    Family and domain databases

    Gene3Di 2.60.120.290. 2 hits.
    InterProi IPR000859. 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.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00431. CUB. 2 hits.
    PF00084. Sushi. 2 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001155. C1r_C1s_MASP. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00032. CCP. 2 hits.
    SM00042. CUB. 2 hits.
    SM00179. EGF_CA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 2 hits.
    SSF50494. SSF50494. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEi PS00010. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Complement C1r and C1s genes are duplicated in the mouse: differential expression generates alternative isomorphs in the liver and in the male reproductive system."
      Garnier G., Circolo A., Xu Y., Volanakis J.E.
      Biochem. J. 371:631-640(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
      Strain: 129/SvJ and BALB/c.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Eye.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Liver.

    Entry informationi

    Entry nameiCS1A_MOUSE
    AccessioniPrimary (citable) accession number: Q8CG14
    Secondary accession number(s): Q8BJC4, Q8CH28, Q8VBY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 98 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3