ID   C1QR1_HUMAN             Reviewed;         652 AA.
AC   Q9NPY3; O00274;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 3.
DT   27-MAR-2024, entry version 207.
DE   RecName: Full=Complement component C1q receptor;
DE   AltName: Full=C1q/MBL/SPA receptor;
DE            Short=C1qR;
DE            Short=C1qR(p);
DE            Short=C1qRp;
DE   AltName: Full=CDw93;
DE   AltName: Full=Complement component 1 q subcomponent receptor 1;
DE   AltName: Full=Matrix-remodeling-associated protein 4;
DE   AltName: CD_antigen=CD93;
DE   Flags: Precursor;
GN   Name=CD93; Synonyms=C1QR1, MXRA4;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT SER-541.
RX   PubMed=9047234; DOI=10.1016/s1074-7613(00)80419-7;
RA   Nepomuceno R.R., Henschen-Edman A.H., Burgess W.H., Tenner A.J.;
RT   "cDNA cloning and primary structure analysis of C1qR(P), the human
RT   C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro.";
RL   Immunity 6:119-129(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-318.
RX   PubMed=11781389;
RA   Steinberger P., Szekeres A., Wille S., Stockl J., Selenko N., Prager E.,
RA   Staffler G., Madic O., Stockinger H., Knapp W.;
RT   "Identification of human CD93 as the phagocytic C1q receptor (C1qRp) by
RT   expression cloning.";
RL   J. Leukoc. Biol. 71:133-140(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Leukocyte;
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   [5]
RP   INTERACTION WITH C1QBP.
RX   PubMed=9233640;
RA   Ghebrehiwet B., Lu P.D., Zhang W., Keilbaugh S.A., Leigh L.E., Eggleton P.,
RA   Reid K.B., Peerschke E.I.;
RT   "Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-R,
RT   associate to form a complex.";
RL   J. Immunol. 159:1429-1436(1997).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=11994479; DOI=10.4049/jimmunol.168.10.5222;
RA   McGreal E.P., Ikewaki N., Akatsu H., Morgan B.P., Gasque P.;
RT   "Human C1qRp is identical with CD93 and the mNI-11 antigen but does not
RT   bind C1q.";
RL   J. Immunol. 168:5222-5232(2002).
RN   [7]
RP   GLYCOSYLATION.
RX   PubMed=10092817;
RA   Nepomuceno R.R., Ruiz S., Park M., Tenner A.J.;
RT   "C1qRP is a heavily O-glycosylated cell surface protein involved in the
RT   regulation of phagocytic activity.";
RL   J. Immunol. 162:3583-3589(1999).
RN   [8]
RP   INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
RX   PubMed=11086025; DOI=10.1172/jci10323;
RA   Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J., Hahn Y.S.;
RT   "Interaction between complement receptor gC1qR and hepatitis C virus core
RT   protein inhibits T-lymphocyte proliferation.";
RL   J. Clin. Invest. 106:1239-1249(2000).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-220.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Receptor (or element of a larger receptor complex) for C1q,
CC       mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA).
CC       May mediate the enhancement of phagocytosis in monocytes and
CC       macrophages upon interaction with soluble defense collagens. May play a
CC       role in intercellular adhesion.
CC   -!- SUBUNIT: Interacts with C1QBP; the association may represent a cell
CC       surface C1q receptor. {ECO:0000269|PubMed:9233640}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with hepatitis virus C/HCV
CC       core protein. {ECO:0000269|PubMed:11086025}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in endothelial cells, platelets,
CC       cells of myeloid origin, such as monocytes and neutrophils. Not
CC       expressed in cells of lymphoid origin.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:10092817}.
CC   -!- CAUTION: Has been sometimes referred to as a collectin receptor.
CC       {ECO:0000305}.
CC   -!- CAUTION: PubMed:11994479 reported that C1q is not a ligand for C1QR1.
CC       {ECO:0000305}.
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DR   EMBL; U94333; AAB53110.1; -; mRNA.
DR   EMBL; AL118508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC028075; AAH28075.1; -; mRNA.
DR   CCDS; CCDS13149.1; -.
DR   RefSeq; NP_036204.2; NM_012072.3.
DR   PDB; 8A59; X-ray; 1.92 A; A=22-257.
DR   PDBsum; 8A59; -.
DR   AlphaFoldDB; Q9NPY3; -.
DR   SMR; Q9NPY3; -.
DR   BioGRID; 116580; 30.
DR   IntAct; Q9NPY3; 18.
DR   STRING; 9606.ENSP00000246006; -.
DR   UniLectin; Q9NPY3; -.
DR   GlyCosmos; Q9NPY3; 3 sites, 1 glycan.
DR   GlyGen; Q9NPY3; 5 sites, 2 O-linked glycans (4 sites).
DR   iPTMnet; Q9NPY3; -.
DR   PhosphoSitePlus; Q9NPY3; -.
DR   BioMuta; CD93; -.
DR   DMDM; 21759074; -.
DR   jPOST; Q9NPY3; -.
DR   MassIVE; Q9NPY3; -.
DR   PaxDb; 9606-ENSP00000246006; -.
DR   PeptideAtlas; Q9NPY3; -.
DR   ProteomicsDB; 82049; -.
DR   TopDownProteomics; Q9NPY3; -.
DR   ABCD; Q9NPY3; 1 sequenced antibody.
DR   Antibodypedia; 2408; 609 antibodies from 33 providers.
DR   DNASU; 22918; -.
DR   Ensembl; ENST00000246006.5; ENSP00000246006.4; ENSG00000125810.10.
DR   GeneID; 22918; -.
DR   KEGG; hsa:22918; -.
DR   MANE-Select; ENST00000246006.5; ENSP00000246006.4; NM_012072.4; NP_036204.2.
DR   UCSC; uc002wsv.4; human.
DR   AGR; HGNC:15855; -.
DR   CTD; 22918; -.
DR   DisGeNET; 22918; -.
DR   GeneCards; CD93; -.
DR   HGNC; HGNC:15855; CD93.
DR   HPA; ENSG00000125810; Tissue enhanced (placenta).
DR   MIM; 120577; gene.
DR   neXtProt; NX_Q9NPY3; -.
DR   OpenTargets; ENSG00000125810; -.
DR   PharmGKB; PA25627; -.
DR   VEuPathDB; HostDB:ENSG00000125810; -.
DR   eggNOG; ENOG502QUVB; Eukaryota.
DR   GeneTree; ENSGT00940000156996; -.
DR   HOGENOM; CLU_027075_1_0_1; -.
DR   InParanoid; Q9NPY3; -.
DR   OMA; YCWVSSG; -.
DR   OrthoDB; 19806at2759; -.
DR   PhylomeDB; Q9NPY3; -.
DR   TreeFam; TF330714; -.
DR   PathwayCommons; Q9NPY3; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q9NPY3; -.
DR   BioGRID-ORCS; 22918; 19 hits in 1147 CRISPR screens.
DR   GeneWiki; CD93; -.
DR   GenomeRNAi; 22918; -.
DR   Pharos; Q9NPY3; Tbio.
DR   PRO; PR:Q9NPY3; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9NPY3; Protein.
DR   Bgee; ENSG00000125810; Expressed in visceral pleura and 194 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
DR   GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0001849; F:complement component C1q complex binding; IDA:UniProtKB.
DR   GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0042116; P:macrophage activation; NAS:UniProtKB.
DR   GO; GO:0006909; P:phagocytosis; NAS:UniProtKB.
DR   CDD; cd03600; CLECT_thrombomodulin_like; 1.
DR   CDD; cd00054; EGF_CA; 3.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   PANTHER; PTHR14789:SF7; CD93 MOLECULE; 1.
DR   PANTHER; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 5.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   Genevisible; Q9NPY3; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Host-virus interaction; Lectin; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT   CHAIN           22..652
FT                   /note="Complement component C1q receptor"
FT                   /id="PRO_0000017367"
FT   TOPO_DOM        24..580
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        602..652
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..174
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DOMAIN          260..301
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          302..344
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          345..384
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          385..426
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          427..468
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          472..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         627
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ET61"
FT   MOD_RES         644
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O89103"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        141..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        264..275
FT                   /evidence="ECO:0000250"
FT   DISULFID        271..285
FT                   /evidence="ECO:0000250"
FT   DISULFID        287..300
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..317
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        311..328
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        330..343
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..358
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        354..367
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        369..383
FT                   /evidence="ECO:0000250"
FT   DISULFID        389..400
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        396..409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        411..425
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        431..443
FT                   /evidence="ECO:0000250"
FT   DISULFID        439..452
FT                   /evidence="ECO:0000250"
FT   DISULFID        454..467
FT                   /evidence="ECO:0000250"
FT   VARIANT         220
FT                   /note="A -> V (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs138932459)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036400"
FT   VARIANT         318
FT                   /note="V -> A"
FT                   /evidence="ECO:0000269|PubMed:11781389"
FT                   /id="VAR_013573"
FT   VARIANT         541
FT                   /note="P -> S (in dbSNP:rs3746731)"
FT                   /evidence="ECO:0000269|PubMed:9047234"
FT                   /id="VAR_050102"
FT   CONFLICT        22
FT                   /note="T -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="C -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        38..39
FT                   /note="TA -> RI (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="S -> N (in Ref. 1; AAB53110)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        186
FT                   /note="G -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        492
FT                   /note="S -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        496
FT                   /note="R -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504
FT                   /note="R -> G (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          35..41
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   HELIX           46..55
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   HELIX           66..82
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          89..99
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   TURN            110..113
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          140..147
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          175..183
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          213..216
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:8A59"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:8A59"
SQ   SEQUENCE   652 AA;  68560 MW;  EECA0FEAC55FCAC2 CRC64;
     MATSMGLLLL LLLLLTQPGA GTGADTEAVV CVGTACYTAH SGKLSAAEAQ NHCNQNGGNL
     ATVKSKEEAQ HVQRVLAQLL RREAALTARM SKFWIGLQRE KGKCLDPSLP LKGFSWVGGG
     EDTPYSNWHK ELRNSCISKR CVSLLLDLSQ PLLPSRLPKW SEGPCGSPGS PGSNIEGFVC
     KFSFKGMCRP LALGGPGQVT YTTPFQTTSS SLEAVPFASA ANVACGEGDK DETQSHYFLC
     KEKAPDVFDW GSSGPLCVSP KYGCNFNNGG CHQDCFEGGD GSFLCGCRPG FRLLDDLVTC
     ASRNPCSSSP CRGGATCVLG PHGKNYTCRC PQGYQLDSSQ LDCVDVDECQ DSPCAQECVN
     TPGGFRCECW VGYEPGGPGE GACQDVDECA LGRSPCAQGC TNTDGSFHCS CEEGYVLAGE
     DGTQCQDVDE CVGPGGPLCD SLCFNTQGSF HCGCLPGWVL APNGVSCTMG PVSLGPPSGP
     PDEEDKGEKE GSTVPRAATA SPTRGPEGTP KATPTTSRPS LSSDAPITSA PLKMLAPSGS
     PGVWREPSIH HATAASGPQE PAGGDSSVAT QNNDGTDGQK LLLFYILGTV VAILLLLALA
     LGLLVYRKRR AKREEKKEKK PQNAADSYSW VPERAESRAM ENQYSPTPGT DC
//