CS1A_MOUSE
ID CS1A_MOUSE Reviewed; 688 AA.
AC Q8CG14; Q8BJC4; Q8CH28; Q8VBY4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Complement C1s-1 subcomponent {ECO:0000305};
DE EC=3.4.21.42 {ECO:0000250|UniProtKB:P09871};
DE AltName: Full=C1 esterase;
DE AltName: Full=Complement C1s-A subcomponent;
DE AltName: Full=Complement component 1 subcomponent s-A;
DE AltName: Full=Complement component 1, S subcomponent 1 {ECO:0000312|MGI:MGI:1355312};
DE Contains:
DE RecName: Full=Complement C1s-A subcomponent heavy chain;
DE Contains:
DE RecName: Full=Complement C1s-A subcomponent light chain;
DE Flags: Precursor;
GN Name=C1s1 {ECO:0000312|MGI:MGI:1355312};
GN Synonyms=C1s {ECO:0000303|PubMed:12513694},
GN C1sa {ECO:0000312|MGI:MGI:1355312};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ, and BALB/cJ;
RX PubMed=12513694; DOI=10.1042/bj20021555;
RA Garnier G., Circolo A., Xu Y., Volanakis J.E.;
RT "Complement C1r and C1s genes are duplicated in the mouse: differential
RT expression generates alternative isomorphs in the liver and in the male
RT reproductive system.";
RL Biochem. J. 371:631-640(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: C1s B chain is a serine protease that combines with C1q and
CC C1r to form C1, the first component of the classical pathway of the
CC complement system. C1r activates C1s so that it can, in turn, activate
CC C2 and C4 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Arg-|-Ala bond in complement component C4 to form
CC C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to
CC form C2a and C2b: the 'classical' pathway C3 convertase.;
CC EC=3.4.21.42; Evidence={ECO:0000250|UniProtKB:P09871};
CC -!- ACTIVITY REGULATION: Inhibited by SERPING1.
CC {ECO:0000250|UniProtKB:P09871}.
CC -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, C1r and
CC C1s in the molar ration of 1:2:2. Activated C1s is an disulfide-linked
CC heterodimer of a heavy chain and a light chain.
CC {ECO:0000250|UniProtKB:P09871}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver.
CC {ECO:0000269|PubMed:12513694}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000250|UniProtKB:P09871}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF459019; AAO15558.1; -; mRNA.
DR EMBL; AF459017; AAO15556.1; -; Genomic_DNA.
DR EMBL; AF459015; AAO15556.1; JOINED; Genomic_DNA.
DR EMBL; AF459016; AAO15556.1; JOINED; Genomic_DNA.
DR EMBL; AK087522; BAC39910.1; ALT_INIT; mRNA.
DR EMBL; BC022123; AAH22123.1; -; mRNA.
DR EMBL; BC018319; AAH18319.1; -; mRNA.
DR RefSeq; NP_001091086.1; NM_001097617.1.
DR RefSeq; NP_659187.2; NM_144938.2.
DR AlphaFoldDB; Q8CG14; -.
DR SMR; Q8CG14; -.
DR ComplexPortal; CPX-4984; Complement C1 complex, C1ra-C1sa variant.
DR STRING; 10090.ENSMUSP00000125531; -.
DR MEROPS; S01.360; -.
DR GlyGen; Q8CG14; 2 sites.
DR iPTMnet; Q8CG14; -.
DR PhosphoSitePlus; Q8CG14; -.
DR CPTAC; non-CPTAC-5597; -.
DR MaxQB; Q8CG14; -.
DR PaxDb; Q8CG14; -.
DR PeptideAtlas; Q8CG14; -.
DR PRIDE; Q8CG14; -.
DR ProteomicsDB; 279066; -.
DR DNASU; 50908; -.
DR GeneID; 50908; -.
DR KEGG; mmu:50908; -.
DR CTD; 50908; -.
DR MGI; MGI:1355312; C1s1.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q8CG14; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; Q8CG14; -.
DR BioGRID-ORCS; 50908; 1 hit in 72 CRISPR screens.
DR ChiTaRS; C1s1; mouse.
DR PRO; PR:Q8CG14; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CG14; protein.
DR GO; GO:0005602; C:complement component C1 complex; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IC:ComplexPortal.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR035708; Complement_C1s_subcomponent.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24255:SF18; PTHR24255:SF18; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Calcium; Complement pathway; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hydrolase; Hydroxylation; Immunity; Innate immunity; Metal-binding;
KW Protease; Reference proteome; Repeat; Serine protease; Signal; Sushi.
FT SIGNAL 1..15
FT /evidence="ECO:0000250"
FT CHAIN 16..688
FT /note="Complement C1s-1 subcomponent"
FT /id="PRO_0000042193"
FT CHAIN 16..437
FT /note="Complement C1s-A subcomponent heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042194"
FT CHAIN 438..688
FT /note="Complement C1s-A subcomponent light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042195"
FT DOMAIN 16..130
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 131..172
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255"
FT DOMAIN 175..290
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 292..356
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 357..423
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 438..680
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 475
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 529
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 631
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 149
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..83
FT /evidence="ECO:0000250"
FT DISULFID 135..147
FT /evidence="ECO:0000250"
FT DISULFID 143..156
FT /evidence="ECO:0000250"
FT DISULFID 158..171
FT /evidence="ECO:0000250"
FT DISULFID 175..202
FT /evidence="ECO:0000250"
FT DISULFID 234..251
FT /evidence="ECO:0000250"
FT DISULFID 294..341
FT /evidence="ECO:0000250"
FT DISULFID 321..354
FT /evidence="ECO:0000250"
FT DISULFID 359..403
FT /evidence="ECO:0000250"
FT DISULFID 386..421
FT /evidence="ECO:0000250"
FT DISULFID 425..549
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00302"
FT DISULFID 595..618
FT /evidence="ECO:0000250"
FT DISULFID 627..659
FT /evidence="ECO:0000250"
FT CONFLICT 76
FT /note="G -> D (in Ref. 1; AAO15556 and 2; BAC39910)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="K -> R (in Ref. 1; AAO15556 and 2; BAC39910)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="E -> Q (in Ref. 1; AAO15556 and 2; BAC39910)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="F -> L (in Ref. 2; BAC39910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 688 AA; 76858 MW; BAC166C861CB8A25 CRC64;
MWCLVLFSLL ASFSAEPTMH GEILSPNYPQ AYPNDVVKSW DIEVPEGFGI HLYFTHVDIE
PSESCAYDSV QIISGGIEEG RLCGQKTSKS PNSPIIEEFQ FPYNKLQVVF TSDFSNEERF
TGFAAYYTAI DINECTDFTD VPCSHFCNNF IGGYFCSCPP EYFLHDDMRN CGVNCSGDVF
TALIGEISSP NYPNPYPENS RCEYQIQLQE GFQVVVTMQR EDFDVEPADS EGNCPDSLTF
ASKNQQFGPY CGNGFPGPLT IRTQSNTLGI VFQTDLMGQK KGWKLRYHGD PISCAKKITA
NSTWEPDKAK YVFKDVVKIT CVDGFEVVEG HVSSTSYYST CQSDGQWSNS GLKCQPVYCG
IPDPIANGKV EEPENSVFGT VVHYTCEEPY YYMEHEEGGE YRCAANGRWV NDQLGIELPR
CIPACGVPTE PFQVHQRIFG GQPAKIENFP WQVFFNHPRA SGALINEYWV LTAAHVLEKI
SDPLMYVGTM SVRTTLLENA QRLYSKRVFI HPSWKKEDDP NTRTNFDNDI ALVQLKDPVK
MGPKVSPICL PGTSSEYNVS PGDMGLISGW GSTEKKVFVI NLRGAKVPVT SLETCKQVKE
ENPTVRPEDY VFTDNMICAG EKGVDSCHGD SGGAFAFQVP NVTVPKFYVA GLVSWGKRCG
TYGVYTKVKN YVDWILKTMQ ENSGPRKD
