ID A0A3P8YQV5_ESOLU Unreviewed; 704 AA.
AC A0A3P8YQV5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=complement subcomponent C1r {ECO:0000256|ARBA:ARBA00011907};
DE EC=3.4.21.41 {ECO:0000256|ARBA:ARBA00011907};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000018282.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000018282.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000018282.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_010883291.1; XM_010884989.3.
DR RefSeq; XP_012994781.1; XM_013139327.2.
DR RefSeq; XP_019896520.1; XM_020040961.1.
DR AlphaFoldDB; A0A3P8YQV5; -.
DR STRING; 8010.ENSELUP00000018282; -.
DR Ensembl; ENSELUT00000040520.2; ENSELUP00000018282.1; ENSELUG00000017805.2.
DR GeneID; 105019078; -.
DR KEGG; els:105019078; -.
DR GeneTree; ENSGT00950000183084; -.
DR InParanoid; A0A3P8YQV5; -.
DR OMA; RIPACLP; -.
DR OrthoDB; 5394076at2759; -.
DR Proteomes; UP000265140; LG20.
DR Bgee; ENSELUG00000017805; Expressed in liver and 13 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:0048856; P:anatomical structure development; IEA:UniProt.
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 4: Predicted;
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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..704
FT /note="complement subcomponent C1r"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018311208"
FT DOMAIN 18..141
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 189..304
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 306..371
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 372..440
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 455..701
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 494
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 548
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 651
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT MOD_RES 163
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT MOD_RES 202
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT DISULFID 74..92
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 146..161
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 157..170
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 172..185
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 189..216
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 249..267
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 308..356
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 336..369
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 374..420
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 403..438
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 442..568
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 612..636
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 647..677
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
SQ SEQUENCE 704 AA; 78301 MW; 02CC74476A1D2CED CRC64;
MNWTPPFIWL LCLSVCECWR VTRSLPALHG QVESPNFPQP YQASLSQQWD ISVPEGYQVQ
LSFTHLDIEP SANCYYDSLT VLYNQKVLGK FCGQENSADG HHPGNQPLLS PSNSLTLVFQ
TDDMNPEQHQ HLGFSIHYQA KDIDECSALD TKDGPVCSQL CHNTLGSYIC SCHHGYELRP
DQRTCVLSCG GGIFNEPEGT LSSPGYPAPS PHGLACQYVI SLELGFIITL NFTDRFHIES
IDTQNGPSCL YHWLQMSIPE KEPQKLCGGQ SPGLVPINSN TVQLDYHTDW EGLSQGWSLH
YTTQRVQCAS PMSVTKGRVT PNFSQYFYRD YIQVRCDDGY KLMMDGKEIK SYASMCQNNG
QWHLSLPECH IIDCGEPEPL LNGQITPLSG SQNQYKSSIQ YQCNTPFYSL LGESTRRYTC
AKDRMWRDDL GISVFPSCIP VCGKPTVSIS GIRRIMGGDR APANSIPWQV MLNVDGGRGG
AMVIGDRWIM TAAHNLVKEG KPAEKDKVRV FVGDVDAVKL SKSPHLGVAS LHPHPEYNNQ
NFANYNHDIA LIKLQQPVTF HAAIMPLCLP PEDAVYTSHQ TGIVSGFGIK EDDMIANELR
YIRLPVVDQN ICETSINEAK KGQKENIPFL TDNMFCVGVP EGGKDSCQGD SGGAYALKNA
RDGSFWAAGI VSWGVGCGMR GRYGVYTRVA KYIDWINKTM EENK
//
