ID   C1QC_HUMAN              Reviewed;         245 AA.
AC   P02747; Q7Z502; Q96DL2; Q96H05;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 3.
DT   24-JAN-2024, entry version 222.
DE   RecName: Full=Complement C1q subcomponent subunit C;
DE   Flags: Precursor;
GN   Name=C1QC; Synonyms=C1QG;
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   Dai F.Y., Yu L., Wan Y.Z., Zhang H.L., Huang J., Zhao S.Y.;
RT   "Cloning and characterization of a novel human cDNA homology to murine C1q
RT   C-chain mRNA.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [6]
RP   PROTEIN SEQUENCE OF 29-122, AND HYDROXYLATION AT PRO-36; PRO-39; PRO-42;
RP   PRO-45; PRO-54; PRO-63; LYS-75; PRO-81; PRO-93; PRO-96; PRO-99 AND PRO-105.
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   [7]
RP   INTERACTION WITH IMMUNOGLOBULIN MU.
RX   PubMed=12847249; DOI=10.4049/jimmunol.171.2.812;
RA   Kishore U., Gupta S.K., Perdikoulis M.V., Kojouharova M.S., Urban B.C.,
RA   Reid K.B.;
RT   "Modular organization of the carboxyl-terminal, globular head region of
RT   human C1q A, B, and C chains.";
RL   J. Immunol. 171:812-820(2003).
RN   [8]
RP   INTERACTION WITH IMMUNOGLOBULIN MU, AND MUTAGENESIS OF HIS-129 AND LYS-198.
RX   PubMed=19006321; DOI=10.1021/bi801131h;
RA   Gadjeva M.G., Rouseva M.M., Zlatarova A.S., Reid K.B., Kishore U.,
RA   Kojouharova M.S.;
RT   "Interaction of human C1q with IgG and IgM: revisited.";
RL   Biochemistry 47:13093-13102(2008).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 117-245.
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).
RN   [10]
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   [11]
RP   VARIANT C1QD3 ARG-34.
RX   PubMed=8630118; DOI=10.1002/art.1780390419;
RA   Slingsby J.H., Norsworthy P., Pearce G., Vaishnaw A.K., Issler H.,
RA   Morley B.J., Walport M.J.;
RT   "Homozygous hereditary C1q deficiency and systemic lupus erythematosus. A
RT   new family and the molecular basis of C1q deficiency in three families.";
RL   Arthritis Rheum. 39:663-670(1996).
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       Antigen-bound IgM (via the Fc region) interacts with the globular
CC       domains of C1q component of the complement system, all three modules
CC       C1QA, C1QB and C1QC being involved in IgM binding; this interaction is
CC       multivalent. It initiates the classical complement pathway
CC       (PubMed:12847249, PubMed:19006321). {ECO:0000269|PubMed:12847249,
CC       ECO:0000269|PubMed:19006321}.
CC   -!- INTERACTION:
CC       P02747; PRO_0000018590 [Q07021]: C1QBP; NbExp=4; IntAct=EBI-1220222, EBI-14032968;
CC       P02747; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-1220222, EBI-947187;
CC       P02747; Q76KX8: ZNF534; NbExp=3; IntAct=EBI-1220222, EBI-17208605;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O-linked glycans consist of Glc-Gal disaccharides bound to the
CC       oxygen atom of post-translationally added hydroxyl groups.
CC   -!- DISEASE: C1q deficiency 3 (C1QD3) [MIM:620322]: An autosomal recessive
CC       disorder caused by impaired activation of the complement classical
CC       pathway. It generally leads to severe immune complex disease
CC       characterized by recurrent skin lesions, chronic infections, an
CC       increased risk of systemic lupus erythematosus, and glomerulonephritis.
CC       {ECO:0000269|PubMed:8630118}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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DR   EMBL; AF087892; AAP97191.1; -; mRNA.
DR   EMBL; AK057792; BAB71575.1; -; mRNA.
DR   EMBL; AL158086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009016; AAH09016.1; -; mRNA.
DR   CCDS; CCDS227.1; -.
DR   PIR; S14351; C1HUQC.
DR   RefSeq; NP_001107573.1; NM_001114101.2.
DR   RefSeq; NP_001334548.1; NM_001347619.1.
DR   RefSeq; NP_758957.2; NM_172369.4.
DR   PDB; 1PK6; X-ray; 1.85 A; C=117-245.
DR   PDB; 2JG8; X-ray; 2.05 A; C/F=115-245.
DR   PDB; 2JG9; X-ray; 1.90 A; C/F=115-245.
DR   PDB; 2WNU; X-ray; 2.30 A; C/F=115-245.
DR   PDB; 2WNV; X-ray; 1.25 A; C/F=115-245.
DR   PDB; 5HKJ; X-ray; 1.35 A; A=115-245.
DR   PDB; 5HZF; X-ray; 1.55 A; A=115-245.
DR   PDB; 6FCZ; EM; 10.00 A; C=117-245.
DR   PDB; 6Z6V; X-ray; 2.19 A; C/F=115-245.
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; P02747; -.
DR   EMDB; EMD-4232; -.
DR   SASBDB; P02747; -.
DR   SMR; P02747; -.
DR   BioGRID; 107175; 138.
DR   ComplexPortal; CPX-1919; Complement component C1q complex.
DR   CORUM; P02747; -.
DR   IntAct; P02747; 11.
DR   MINT; P02747; -.
DR   STRING; 9606.ENSP00000363770; -.
DR   DrugBank; DB00112; Bevacizumab.
DR   DrugBank; DB00002; Cetuximab.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB00111; Daclizumab.
DR   DrugBank; DB00005; Etanercept.
DR   DrugBank; DB00110; Palivizumab.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   GlyCosmos; P02747; 1 site, No reported glycans.
DR   GlyGen; P02747; 1 site.
DR   PhosphoSitePlus; P02747; -.
DR   BioMuta; C1QC; -.
DR   DMDM; 20178281; -.
DR   CPTAC; non-CPTAC-2652; -.
DR   jPOST; P02747; -.
DR   MassIVE; P02747; -.
DR   PaxDb; 9606-ENSP00000363770; -.
DR   PeptideAtlas; P02747; -.
DR   ProteomicsDB; 51563; -.
DR   Antibodypedia; 691; 344 antibodies from 34 providers.
DR   DNASU; 714; -.
DR   Ensembl; ENST00000374637.1; ENSP00000363768.1; ENSG00000159189.13.
DR   Ensembl; ENST00000374639.7; ENSP00000363770.3; ENSG00000159189.13.
DR   Ensembl; ENST00000374640.9; ENSP00000363771.4; ENSG00000159189.13.
DR   Ensembl; ENST00000695751.1; ENSP00000512144.1; ENSG00000159189.13.
DR   GeneID; 714; -.
DR   KEGG; hsa:714; -.
DR   MANE-Select; ENST00000374640.9; ENSP00000363771.4; NM_172369.5; NP_758957.2.
DR   UCSC; uc001bga.5; human.
DR   AGR; HGNC:1245; -.
DR   CTD; 714; -.
DR   DisGeNET; 714; -.
DR   GeneCards; C1QC; -.
DR   HGNC; HGNC:1245; C1QC.
DR   HPA; ENSG00000159189; Tissue enhanced (lymphoid).
DR   MalaCards; C1QC; -.
DR   MIM; 120575; gene.
DR   MIM; 620322; phenotype.
DR   neXtProt; NX_P02747; -.
DR   OpenTargets; ENSG00000159189; -.
DR   Orphanet; 169147; Immunodeficiency due to a classical component pathway complement deficiency.
DR   PharmGKB; PA25626; -.
DR   VEuPathDB; HostDB:ENSG00000159189; -.
DR   eggNOG; ENOG502RZM2; Eukaryota.
DR   GeneTree; ENSGT00940000161227; -.
DR   HOGENOM; CLU_001074_0_2_1; -.
DR   InParanoid; P02747; -.
DR   OMA; RGTNEYP; -.
DR   OrthoDB; 3683851at2759; -.
DR   PhylomeDB; P02747; -.
DR   TreeFam; TF329591; -.
DR   PathwayCommons; P02747; -.
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; P02747; -.
DR   SIGNOR; P02747; -.
DR   BioGRID-ORCS; 714; 8 hits in 1148 CRISPR screens.
DR   ChiTaRS; C1QC; human.
DR   EvolutionaryTrace; P02747; -.
DR   GenomeRNAi; 714; -.
DR   Pharos; P02747; Tbio.
DR   PRO; PR:P02747; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P02747; Protein.
DR   Bgee; ENSG00000159189; Expressed in decidua and 170 other cell types or tissues.
DR   ExpressionAtlas; P02747; baseline and differential.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
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; NAS:ComplexPortal.
DR   GO; GO:0062167; C:complement component C1q complex; IPI:ComplexPortal.
DR   GO; GO:0005576; C:extracellular region; IDA:ComplexPortal.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; ISS:ARUK-UCL.
DR   GO; GO:0045202; C:synapse; ISS:ARUK-UCL.
DR   GO; GO:0006958; P:complement activation, classical pathway; IDA:ComplexPortal.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0030853; P:negative regulation of granulocyte differentiation; IDA:BHF-UCL.
DR   GO; GO:0045650; P:negative regulation of macrophage differentiation; IDA:BHF-UCL.
DR   GO; GO:0098883; P:synapse pruning; ISS:ARUK-UCL.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR15427:SF29; COMPLEMENT C1Q SUBCOMPONENT SUBUNIT C; 1.
DR   PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS50871; C1Q; 1.
DR   Genevisible; P02747; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Collagen; Complement pathway; Direct protein sequencing;
KW   Disease variant; Disulfide bond; Glycoprotein; Hydroxylation; Immunity;
KW   Innate immunity; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   CHAIN           29..245
FT                   /note="Complement C1q subcomponent subunit C"
FT                   /id="PRO_0000003524"
FT   DOMAIN          31..112
FT                   /note="Collagen-like"
FT   DOMAIN          115..245
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          45..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..103
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         39
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         42
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         54
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         63
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         75
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         81
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         93
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         96
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         99
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   MOD_RES         105
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:486087"
FT   CARBOHYD        75
FT                   /note="O-linked (Gal...) hydroxylysine"
FT   DISULFID        32
FT                   /note="Interchain"
FT   VARIANT         34
FT                   /note="G -> R (in C1QD3; dbSNP:rs200206736)"
FT                   /evidence="ECO:0000269|PubMed:8630118"
FT                   /id="VAR_008542"
FT   MUTAGEN         129
FT                   /note="H->A: Has no effect on binding to IgM."
FT                   /evidence="ECO:0000269|PubMed:19006321"
FT   MUTAGEN         198
FT                   /note="K->E: Decreases binding to IgM."
FT                   /evidence="ECO:0000269|PubMed:19006321"
FT   CONFLICT        14
FT                   /note="K -> R (in Ref. 3; BAB71575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="P -> A (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26..27
FT                   /note="GQ -> AK (in Ref. 2; AAP97191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="K -> P (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="P -> K (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="K -> P (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="P -> K (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="N -> D (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="M -> N (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="I -> F (in Ref. 2; AAP97191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="G -> E (in Ref. 2; AAP97191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="E -> G (in Ref. 3; BAB71575)"
FT                   /evidence="ECO:0000305"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:5HZF"
FT   STRAND          121..125
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   TURN            153..155
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:5HKJ"
FT   STRAND          164..176
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          178..184
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          187..194
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          201..211
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          216..225
FT                   /evidence="ECO:0007829|PDB:2WNV"
FT   STRAND          236..244
FT                   /evidence="ECO:0007829|PDB:2WNV"
SQ   SEQUENCE   245 AA;  25774 MW;  FA17117EB7ABFC12 CRC64;
     MDVGPSSLPH LGLKLLLLLL LLPLRGQANT GCYGIPGMPG LPGAPGKDGY DGLPGPKGEP
     GIPAIPGIRG PKGQKGEPGL PGHPGKNGPM GPPGMPGVPG PMGIPGEPGE EGRYKQKFQS
     VFTVTRQTHQ PPAPNSLIRF NAVLTNPQGD YDTSTGKFTC KVPGLYYFVY HASHTANLCV
     LLYRSGVKVV TFCGHTSKTN QVNSGGVLLR LQVGEEVWLA VNDYYDMVGI QGSDSVFSGF
     LLFPD
//