ID Q2VPN1_XENLA Unreviewed; 708 AA.
AC Q2VPN1;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=complement subcomponent C1r {ECO:0000256|ARBA:ARBA00011907};
DE EC=3.4.21.41 {ECO:0000256|ARBA:ARBA00011907};
GN Name=MGC130869.L {ECO:0000313|RefSeq:NP_001090130.1,
GN ECO:0000313|Xenbase:XB-GENE-995389};
GN Synonyms=MGC130869 {ECO:0000313|EMBL:AAI08508.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI08508.1};
RN [1] {ECO:0000313|RefSeq:NP_001090130.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI08508.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000313|EMBL:AAI08508.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001090130.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: C1r B chain is a serine protease that combines with C1q and
CC C1s to form C1, the first component of the classical pathway of the
CC complement system. {ECO:0000256|ARBA:ARBA00002304}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Lys(or Arg)-|-Ile bond in complement
CC subcomponent C1s to form the active form of C1s (EC 3.4.21.42).;
CC EC=3.4.21.41; Evidence={ECO:0000256|ARBA:ARBA00001057};
CC -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, C1r and
CC C1s in the molar ration of 1:2:2. C1r is a dimer of identical chains,
CC each of which is activated by cleavage into two chains, A and B,
CC connected by disulfide bonds. {ECO:0000256|ARBA:ARBA00025829}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000256|PIRSR:PIRSR001155-3}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; BC108507; AAI08508.1; -; mRNA.
DR RefSeq; NP_001090130.1; NM_001096661.1.
DR MEROPS; S01.189; -.
DR DNASU; 735208; -.
DR GeneID; 735208; -.
DR KEGG; xla:735208; -.
DR AGR; Xenbase:XB-GENE-995389; -.
DR CTD; 735208; -.
DR Xenbase; XB-GENE-995389; MGC130869.L.
DR OrthoDB; 5394076at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 735208; Expressed in liver and 15 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006956; P:complement activation; IEA:InterPro.
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; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
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:SF25; COMPLEMENT C1R SUBCOMPONENT; 1.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001155; C1r_C1s_MASP; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01186; EGF_2; 1.
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 {ECO:0000256|PIRSR:PIRSR001155-4};
KW Complement pathway {ECO:0000256|ARBA:ARBA00022875};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001155-2};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278,
KW ECO:0000256|PIRSR:PIRSR001155-3}; Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001155-4};
KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR001155-3};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001090130.1};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..708
FT /note="complement subcomponent C1r"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001090130.1"
FT /id="PRO_5033207151"
FT DOMAIN 9..136
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 187..299
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 301..367
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 368..438
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 453..705
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 491
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 545
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 658
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT MOD_RES 161
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT MOD_RES 200
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT DISULFID 68..86
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 141..159
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 155..168
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 170..183
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 187..214
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 244..262
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 303..352
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 332..365
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 370..418
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 400..436
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 440..565
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 612..640
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 654..683
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
SQ SEQUENCE 708 AA; 80182 MW; F22D6E326F7FA9E5 CRC64;
MWLWVVLLLG TVAYSQNNKR PLYGTITSPN YPKPYPNSNE STWNITVPEG YHISLNFLVF
DIEPSENCYY DFVKVMADGK ELGQFCGSVN SLTNPTRRQF VSTGTQMRIH FQSDFSNELD
GDIVPYKGFM AFYQAIDKDE CAPPSDNSAT WTPPCEHVCH NYVGGYFCSC FPGYHLQSDS
RSCKVECSSE MFTEESGFIS SPGYPEPYPP DLKCNYSIRL EEGLQISLSF QKPFEIDYHP
KARCPYDTLE VFAGDMMLNS FCGSDSPGMV MTRSHTVDIV FETDDSGDSK GWSLHYTSEA
IPCPNPKAWD KYTIISPKQN IYRMRDYIVV TCQTGYKIME DRKELGSFST ICQKDGTWHR
PIPRCEIVTC KDPPVLTNGQ YKFLTAPGNL EYESVIQYHC NEPYYKMVTA KDSDTFTCSA
QRQWKDESGG NKIPLCIPVC GKPDNPVTNF GRILHGKKAA PGNFPWQVFI SRMGRAGGAL
IGEHWVLTAA HVLQPENEEK EDNDPTKVHI FMRSLDVNQL LKIGNYPVEA FYVHPKYRRG
RYDNDIALIR LKNPVVMGEN VSPVCLPSPE DEDDIYQNHR NGYVSGYGQT ENRTIANELR
YVSVPVVSWS ACETYVNDKK LKVKDVSERQ KYSLTRNMFC AGFPEESLNK GDSCEGDSGG
AYTTPNRQDT WVATGLVSWG IGCGQGYGIY TKVSNYLDWI KSYTEKDE
//
