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