C1QC_HUMAN
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 03-AUG-2022, entry version 215.
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 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 [8]
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 [9]
RP VARIANT C1QD 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 -!- 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: 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 {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 SASBDB; P02747; -.
DR SMR; P02747; -.
DR BioGRID; 107175; 137.
DR ComplexPortal; CPX-1919; Complement component C1q complex.
DR CORUM; P02747; -.
DR IntAct; P02747; 12.
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 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; P02747; -.
DR PeptideAtlas; P02747; -.
DR PRIDE; P02747; -.
DR ProteomicsDB; 51563; -.
DR Antibodypedia; 691; 315 antibodies from 34 providers.
DR DNASU; 714; -.
DR Ensembl; ENST00000374637.1; ENSP00000363768.1; ENSG00000159189.12.
DR Ensembl; ENST00000374639.7; ENSP00000363770.3; ENSG00000159189.12.
DR Ensembl; ENST00000374640.9; ENSP00000363771.4; ENSG00000159189.12.
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 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; 613652; 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; 1258047at2759; -.
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 1070 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 169 other tissues.
DR ExpressionAtlas; P02747; baseline and differential.
DR Genevisible; P02747; HS.
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; IC: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 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 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 C1QD; dbSNP:rs200206736)"
FT /evidence="ECO:0000269|PubMed:8630118"
FT /id="VAR_008542"
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
