ID C1R_PANTR Reviewed; 705 AA.
AC Q5R1W3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 08-NOV-2023, entry version 118.
DE RecName: Full=Complement C1r subcomponent;
DE EC=3.4.21.41;
DE AltName: Full=Complement component 1 subcomponent r;
DE Contains:
DE RecName: Full=Complement C1r subcomponent heavy chain;
DE Contains:
DE RecName: Full=Complement C1r subcomponent light chain;
DE Flags: Precursor;
GN Name=C1R;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RA Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y., Osada N.,
RA Hashimoto K.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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;
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 (By similarity). {ECO:0000250}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB188284; BAD74035.1; -; mRNA.
DR RefSeq; NP_001029292.1; NM_001034120.1.
DR AlphaFoldDB; Q5R1W3; -.
DR SMR; Q5R1W3; -.
DR STRING; 9598.ENSPTRP00000054792; -.
DR MEROPS; S01.192; -.
DR GlyCosmos; Q5R1W3; 4 sites, No reported glycans.
DR PaxDb; 9598-ENSPTRP00000054792; -.
DR GeneID; 466939; -.
DR KEGG; ptr:466939; -.
DR CTD; 715; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5R1W3; -.
DR OrthoDB; 5394076at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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; 3.
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; PS00010; ASX_HYDROXYL; 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 Complement pathway; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hydrolase; Hydroxylation; Immunity; Innate immunity; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Serine protease; Signal; Sushi.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..705
FT /note="Complement C1r subcomponent"
FT /id="PRO_0000027583"
FT CHAIN 18..463
FT /note="Complement C1r subcomponent heavy chain"
FT /id="PRO_0000027584"
FT CHAIN 464..705
FT /note="Complement C1r subcomponent light chain"
FT /id="PRO_0000027585"
FT DOMAIN 18..141
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 142..190
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255"
FT DOMAIN 193..305
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 307..373
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 374..449
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 464..702
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 502
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 557
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 654
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000250"
FT MOD_RES 206
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P00736"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..89
FT /evidence="ECO:0000250"
FT DISULFID 146..165
FT /evidence="ECO:0000250"
FT DISULFID 161..174
FT /evidence="ECO:0000250"
FT DISULFID 176..189
FT /evidence="ECO:0000250"
FT DISULFID 193..220
FT /evidence="ECO:0000250"
FT DISULFID 250..268
FT /evidence="ECO:0000250"
FT DISULFID 309..358
FT /evidence="ECO:0000250"
FT DISULFID 338..371
FT /evidence="ECO:0000250"
FT DISULFID 376..429
FT /evidence="ECO:0000250"
FT DISULFID 406..447
FT /evidence="ECO:0000250"
FT DISULFID 451..577
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 620..639
FT /evidence="ECO:0000250"
FT DISULFID 650..680
FT /evidence="ECO:0000250"
SQ SEQUENCE 705 AA; 80205 MW; 80189FF579BA28E1 CRC64;
MWLLYLLVPA LFCRAGGSIP IPQKLFGEVT SPLFPKPYPN NFETTTVITV PTGYRVKLVF
QQFDLEPSEG CFYDYVKISA DKKSLGRFCG QLGSPLGNPP GKKEFMSQGN KMLLTFHTDF
SNEENGTIMF YKGFLAYYQA VDLDECASRS KSGEEDPQPQ CQHLCHNYVG GYFCSCRPGY
ELQKDRHSCQ AECSSELYTE ASGYISSLEY PRSYPPDLRC NYSIRVERGL TLHLKFLEPF
DIDDHQQVHC PYDQLQIYAN GKNIGEFCGK QRPPDLDTSS NAVDLLFFTD ESGDSRGWKL
RYTTEIIKCP QPKTLDEFTI IQNLQPQYQF RDYFIATCKQ GYQLIEGKQV LHSFTAVCQD
DGTWHRAMPR CKIKDCGQPR NLPNGDFRYT TTMGVNTYKA RIQYYCHETY YKMQTRAGSR
ESEQGVYTCT AQGIWKNEQK GEKIPRCLPV CGKPVNPVEQ RQRIIGGQKA KMGNFPWQVF
TNIHGRGGGA LLGDRWILTA AHTLYPKEHE AQSNASLDVF LGHTNVEELM KLGNHPIRRV
SVHPDYRQDE SYNFEGDIAL LELENSVTLG PNLLPICLPD NETFYDLGLM GYVSGFGVME
EKIAHDLRFV RLPVANPQAC ENWLRGKNRM DVFSQNMFCA GHPSLKQDAC QGDSGGVFAV
RDPNTDRWVA TGIVSWGIGC SRGYGFYTKV LNYVDWIKKE MEEED
//
