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C1R_PANTR
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   25-MAY-2022, entry version 113.
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   PaxDb; Q5R1W3; -.
DR   GeneID; 466939; -.
DR   KEGG; ptr:466939; -.
DR   CTD; 715; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; Q5R1W3; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
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; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 3.
DR   Gene3D; 2.60.120.290; -; 2.
DR   InterPro; IPR035707; Complement_C1r.
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; 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; PTHR24255:SF25; 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; SM00181; EGF; 1.
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; 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
 
 
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