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C1QA_HUMAN
ID   C1QA_HUMAN              Reviewed;         245 AA.
AC   P02745; B2R4X2; Q5T963;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 223.
DE   RecName: Full=Complement C1q subcomponent subunit A;
DE   Flags: Precursor;
GN   Name=C1QA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Monocyte;
RX   PubMed=1706597; DOI=10.1042/bj2740481;
RA   Sellar G.C., Blake D.J., Reid K.B.M.;
RT   "Characterization and organization of the genes encoding the A-, B- and C-
RT   chains of human complement subcomponent C1q. The complete derived amino
RT   acid sequence of human C1q.";
RL   Biochem. J. 274:481-490(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wan T., Zhang W., Cao X.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-23.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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).
RN   [8]
RP   PROTEIN SEQUENCE OF 23-130, HYDROXYLATION AT LYS-33; PRO-39; PRO-45;
RP   LYS-48; PRO-54; PRO-57; LYS-67; PRO-73; PRO-79; PRO-85 AND LYS-100, AND
RP   GLYCOSYLATION AT LYS-33; LYS-48; LYS-67 AND LYS-100.
RX   PubMed=486087; DOI=10.1042/bj1790367;
RA   Reid K.B.M.;
RT   "Complete amino acid sequences of the three collagen-like regions present
RT   in subcomponent C1q of the first component of human complement.";
RL   Biochem. J. 179:367-371(1979).
RN   [9]
RP   PROTEIN SEQUENCE OF 131-245.
RX   PubMed=6981411; DOI=10.1042/bj2030559;
RA   Reid K.B.M., Gagnon J., Frampton J.;
RT   "Completion of the amino acid sequences of the A and B chains of
RT   subcomponent C1q of the first component of human complement.";
RL   Biochem. J. 203:559-569(1982).
RN   [10]
RP   INTERACTION WITH CR1.
RX   PubMed=9324355; DOI=10.1016/s1074-7613(00)80356-8;
RA   Klickstein L.B., Barbashov S.F., Liu T., Jack R.M., Nicholson-Weller A.;
RT   "Complement receptor type 1 (CR1, CD35) is a receptor for C1q.";
RL   Immunity 7:345-355(1997).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [13]
RP   REVIEW ON C1Q DEFICIENCY.
RX   PubMed=9777412; DOI=10.1016/s0171-2985(98)80033-8;
RA   Petry F.;
RT   "Molecular basis of hereditary C1q deficiency.";
RL   Immunobiology 199:286-294(1998).
RN   [14]
RP   INTERACTION WITH STAPHYLOCOCCUS AUREUS CNA (MICROBIAL INFECTION).
RX   PubMed=23720782; DOI=10.1074/jbc.m113.454462;
RA   Kang M., Ko Y.P., Liang X., Ross C.L., Liu Q., Murray B.E., Hoeoek M.;
RT   "Collagen-binding microbial surface components recognizing adhesive matrix
RT   molecule (MSCRAMM) of Gram-positive bacteria inhibit complement activation
RT   via the classical pathway.";
RL   J. Biol. Chem. 288:20520-20531(2013).
RN   [15]
RP   INTERACTION WITH CD33.
RX   PubMed=28325905; DOI=10.1038/s41598-017-00290-w;
RA   Son M., Diamond B., Volpe B.T., Aranow C.B., Mackay M.C.,
RA   Santiago-Schwarz F.;
RT   "Evidence for C1q-mediated crosslinking of CD33/LAIR-1 inhibitory
RT   immunoreceptors and biological control of CD33/LAIR-1 expression.";
RL   Sci. Rep. 7:270-270(2017).
RN   [16]
RP   INTERACTION WITH CR1.
RX   PubMed=29563915; DOI=10.3389/fimmu.2018.00453;
RA   Jacquet M., Cioci G., Fouet G., Bally I., Thielens N.M., Gaboriaud C.,
RA   Rossi V.;
RT   "C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on
RT   CCP24-25 Modules.";
RL   Front. Immunol. 9:453-453(2018).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 112-244.
RX   PubMed=12960167; DOI=10.1074/jbc.m307764200;
RA   Gaboriaud C., Juanhuix J., Gruez A., Lacroix M., Darnault C., Pignol D.,
RA   Verger D., Fontecilla-Camps J.-C., Arlaud G.J.;
RT   "The crystal structure of the globular head of complement protein C1q
RT   provides a basis for its versatile recognition properties.";
RL   J. Biol. Chem. 278:46974-46982(2003).
CC   -!- FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1,
CC       the first component of the serum complement system. The collagen-like
CC       regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2)
CC       proenzyme complex, and efficient activation of C1 takes place on
CC       interaction of the globular heads of C1q with the Fc regions of IgG or
CC       IgM antibody present in immune complexes.
CC   -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, R and S
CC       in the molar ration of 1:2:2. C1q subcomponent is composed of nine
CC       subunits, six of which are disulfide-linked dimers of the A and B
CC       chains, and three of which are disulfide-linked dimers of the C chain.
CC       Interacts (via C-terminus) with CD33; this interaction activates CD33
CC       inhibitory motifs (PubMed:28325905). Interacts with CR1 (via Sushi 24
CC       and Sushi 25 domains) (PubMed:29563915, PubMed:9324355).
CC       {ECO:0000269|PubMed:28325905, ECO:0000269|PubMed:29563915,
CC       ECO:0000269|PubMed:9324355}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC       protein Cna; this interaction results in the inhibition of the
CC       classical complement pathway. {ECO:0000269|PubMed:23720782}.
CC   -!- INTERACTION:
CC       P02745; P02746: C1QB; NbExp=4; IntAct=EBI-1220209, EBI-2813376;
CC       P02745; PRO_0000018590 [Q07021]: C1QBP; NbExp=6; IntAct=EBI-1220209, EBI-14032968;
CC       P02745; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-1220209, EBI-744081;
CC       P02745; Q9UHD9: UBQLN2; NbExp=6; IntAct=EBI-1220209, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O-linked glycans are assumed to be the Glc-Gal disaccharides
CC       typically found as secondary modifications of hydroxylated lysines in
CC       collagen-like domains. {ECO:0000269|PubMed:486087}.
CC   -!- DISEASE: Complement component C1q deficiency (C1QD) [MIM:613652]: A
CC       disorder caused by impaired activation of the complement classical
CC       pathway. It generally leads to severe immune complex disease with
CC       features of systemic lupus erythematosus and glomerulonephritis.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- WEB RESOURCE: Name=C1QAbase; Note=C1QA mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/C1QAbase/";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/c1qa/";
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DR   EMBL; AF135157; AAD32626.1; -; mRNA.
DR   EMBL; AY789471; AAV40828.1; -; Genomic_DNA.
DR   EMBL; AL158086; CAI22892.1; -; Genomic_DNA.
DR   EMBL; AK311980; BAG34919.1; -; mRNA.
DR   EMBL; AL158086; CAI22893.1; -; Genomic_DNA.
DR   EMBL; CH471134; EAW95014.1; -; Genomic_DNA.
DR   EMBL; BC030153; AAH30153.1; -; mRNA.
DR   EMBL; BC071986; AAH71986.1; -; mRNA.
DR   CCDS; CCDS226.1; -.
DR   PIR; S14350; C1HUQA.
DR   RefSeq; NP_001334394.1; NM_001347465.1.
DR   RefSeq; NP_001334395.1; NM_001347466.1.
DR   RefSeq; NP_057075.1; NM_015991.3.
DR   PDB; 1PK6; X-ray; 1.85 A; A=112-244.
DR   PDB; 2JG8; X-ray; 2.05 A; A/D=112-245.
DR   PDB; 2JG9; X-ray; 1.90 A; A/D=112-245.
DR   PDB; 2WNU; X-ray; 2.30 A; A/D=112-245.
DR   PDB; 2WNV; X-ray; 1.25 A; A/D=112-245.
DR   PDB; 5HKJ; X-ray; 1.35 A; A=110-245.
DR   PDB; 5HZF; X-ray; 1.55 A; A=110-245.
DR   PDB; 6FCZ; EM; 10.00 A; A=112-244.
DR   PDB; 6Z6V; X-ray; 2.19 A; A/D=110-245.
DR   PDBsum; 1PK6; -.
DR   PDBsum; 2JG8; -.
DR   PDBsum; 2JG9; -.
DR   PDBsum; 2WNU; -.
DR   PDBsum; 2WNV; -.
DR   PDBsum; 5HKJ; -.
DR   PDBsum; 5HZF; -.
DR   PDBsum; 6FCZ; -.
DR   PDBsum; 6Z6V; -.
DR   AlphaFoldDB; P02745; -.
DR   SASBDB; P02745; -.
DR   SMR; P02745; -.
DR   BioGRID; 107173; 207.
DR   ComplexPortal; CPX-1919; Complement component C1q complex.
DR   CORUM; P02745; -.
DR   IntAct; P02745; 23.
DR   MINT; P02745; -.
DR   STRING; 9606.ENSP00000363773; -.
DR   DrugBank; DB00112; Bevacizumab.
DR   DrugBank; DB00002; Cetuximab.
DR   DrugBank; DB00111; Daclizumab.
DR   DrugBank; DB00005; Etanercept.
DR   DrugBank; DB00110; Palivizumab.
DR   GlyConnect; 1142; 7 N-Linked glycans (1 site).
DR   GlyGen; P02745; 5 sites, 11 N-linked glycans (1 site).
DR   iPTMnet; P02745; -.
DR   PhosphoSitePlus; P02745; -.
DR   BioMuta; C1QA; -.
DR   DMDM; 399138; -.
DR   jPOST; P02745; -.
DR   MassIVE; P02745; -.
DR   PaxDb; P02745; -.
DR   PeptideAtlas; P02745; -.
DR   PRIDE; P02745; -.
DR   ProteomicsDB; 51561; -.
DR   Antibodypedia; 707; 451 antibodies from 35 providers.
DR   DNASU; 712; -.
DR   Ensembl; ENST00000374642.8; ENSP00000363773.3; ENSG00000173372.17.
DR   Ensembl; ENST00000402322.1; ENSP00000385564.1; ENSG00000173372.17.
DR   GeneID; 712; -.
DR   KEGG; hsa:712; -.
DR   MANE-Select; ENST00000374642.8; ENSP00000363773.3; NM_015991.4; NP_057075.1.
DR   UCSC; uc001bfy.4; human.
DR   CTD; 712; -.
DR   DisGeNET; 712; -.
DR   GeneCards; C1QA; -.
DR   HGNC; HGNC:1241; C1QA.
DR   HPA; ENSG00000173372; Tissue enhanced (lymphoid).
DR   MalaCards; C1QA; -.
DR   MIM; 120550; gene.
DR   MIM; 613652; phenotype.
DR   neXtProt; NX_P02745; -.
DR   OpenTargets; ENSG00000173372; -.
DR   Orphanet; 300345; Autosomal systemic lupus erythematosus.
DR   Orphanet; 169147; Immunodeficiency due to a classical component pathway complement deficiency.
DR   PharmGKB; PA25622; -.
DR   VEuPathDB; HostDB:ENSG00000173372; -.
DR   eggNOG; ENOG502RZM2; Eukaryota.
DR   GeneTree; ENSGT00940000162143; -.
DR   HOGENOM; CLU_001074_3_1_1; -.
DR   InParanoid; P02745; -.
DR   OMA; DMVITNQ; -.
DR   OrthoDB; 1258047at2759; -.
DR   PhylomeDB; P02745; -.
DR   TreeFam; TF329591; -.
DR   PathwayCommons; P02745; -.
DR   Reactome; R-HSA-166663; Initial triggering of complement.
DR   Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SignaLink; P02745; -.
DR   SIGNOR; P02745; -.
DR   BioGRID-ORCS; 712; 10 hits in 1072 CRISPR screens.
DR   ChiTaRS; C1QA; human.
DR   EvolutionaryTrace; P02745; -.
DR   GeneWiki; C1QA; -.
DR   GenomeRNAi; 712; -.
DR   Pharos; P02745; Tbio.
DR   PRO; PR:P02745; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P02745; protein.
DR   Bgee; ENSG00000173372; Expressed in spleen and 183 other tissues.
DR   ExpressionAtlas; P02745; baseline and differential.
DR   Genevisible; P02745; HS.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005602; C:complement component C1 complex; TAS:ProtInc.
DR   GO; GO:0062167; C:complement component C1q complex; IPI:ComplexPortal.
DR   GO; GO:0005576; C:extracellular region; IDA:ComplexPortal.
DR   GO; GO:0098794; C:postsynapse; ISS:ARUK-UCL.
DR   GO; GO:0045202; C:synapse; ISS:ARUK-UCL.
DR   GO; GO:0001540; F:amyloid-beta binding; TAS:ARUK-UCL.
DR   GO; GO:0007568; P:aging; ISS:ARUK-UCL.
DR   GO; GO:0048143; P:astrocyte activation; ISS:ARUK-UCL.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0006956; P:complement activation; TAS:ProtInc.
DR   GO; GO:0006958; P:complement activation, classical pathway; IDA:ComplexPortal.
DR   GO; GO:0150062; P:complement-mediated synapse pruning; ISS:ARUK-UCL.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0001774; P:microglial cell activation; ISS:ARUK-UCL.
DR   GO; GO:0016322; P:neuron remodeling; ISS:ARUK-UCL.
DR   GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
DR   GO; GO:0050808; P:synapse organization; ISS:ARUK-UCL.
DR   GO; GO:0098883; P:synapse pruning; ISS:ARUK-UCL.
DR   GO; GO:0150064; P:vertebrate eye-specific patterning; ISS:ARUK-UCL.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR037572; Complement_C1q_A.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR15427:SF26; PTHR15427:SF26; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; SSF49842; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Collagen; Complement pathway; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Host-virus interaction; Hydroxylation;
KW   Immunity; Innate immunity; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   CHAIN           23..245
FT                   /note="Complement C1q subcomponent subunit A"
FT                   /id="PRO_0000003517"
FT   DOMAIN          31..109
FT                   /note="Collagen-like"
FT   DOMAIN          110..245
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          27..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         33
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         39
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         45
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         48
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         54
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         57
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         67
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         73
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         79
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         85
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         100
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   CARBOHYD        33
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   CARBOHYD        48
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   CARBOHYD        67
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   CARBOHYD        100
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218"
FT   DISULFID        26
FT                   /note="Interchain (with C-29 in B chain)"
FT   VARIANT         23
FT                   /note="E -> K (in dbSNP:rs17887074)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_021090"
FT   CONFLICT        97
FT                   /note="P -> K (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="K -> P (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="C -> N (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="S -> W (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240..243
FT                   /note="LIFP -> ILPGF (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:5HKJ"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:2JG9"
FT   STRAND          157..169
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          171..179
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          195..197
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          199..209
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          214..224
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          235..243
FT                   /evidence="ECO:0007829|PDB:2WNV"
SQ   SEQUENCE   245 AA;  26017 MW;  8FF6B6AE02D49C4C CRC64;
     MEGPRGWLVL CVLAISLASM VTEDLCRAPD GKKGEAGRPG RRGRPGLKGE QGEPGAPGIR
     TGIQGLKGDQ GEPGPSGNPG KVGYPGPSGP LGARGIPGIK GTKGSPGNIK DQPRPAFSAI
     RRNPPMGGNV VIFDTVITNQ EEPYQNHSGR FVCTVPGYYY FTFQVLSQWE ICLSIVSSSR
     GQVRRSLGFC DTTNKGLFQV VSGGMVLQLQ QGDQVWVEKD PKKGHIYQGS EADSVFSGFL
     IFPSA
 
 
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