ID   COJA1_HUMAN             Reviewed;        1142 AA.
AC   Q14993; Q00559; Q05850; Q12885; Q13676; Q14DH1; Q5JUF0; Q5T424; Q9H572;
AC   Q9NPZ2; Q9NQP2;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 3.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Collagen alpha-1(XIX) chain;
DE   AltName: Full=Collagen alpha-1(Y) chain;
DE   Flags: Precursor;
GN   Name=COL19A1;
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].
RX   PubMed=7775380; DOI=10.1093/oxfordjournals.jbchem.a124700;
RA   Inoguchi K., Yoshioka H., Khaleduzzaman M., Ninomiya Y.;
RT   "The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, contains
RT   a long unusual 3' untranslated region and displays many unique splicing
RT   variants.";
RL   J. Biochem. 117:137-146(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9344653; DOI=10.1006/geno.1997.4921;
RA   Khaleduzzaman M., Sumiyoshi H., Ueki Y., Inoguchi K., Ninomiya Y.,
RA   Yoshioka H.;
RT   "Structure of the human type XIX collagen (COL19A1) gene, which suggests it
RT   has arisen from an ancestor gene of the FACIT family.";
RL   Genomics 45:304-312(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   NUCLEOTIDE SEQUENCE [MRNA] OF 26-624.
RC   TISSUE=Rhabdomyosarcoma;
RX   PubMed=1639419; DOI=10.1016/0888-7543(92)90176-s;
RA   Yoshioka H., Zhang H., Ramirez F., Mattei M.-G., Moradi-Ameli M.,
RA   van der Rest M., Gordon M.K.;
RT   "Synteny between the loci for a novel FACIT-like collagen locus (D6S228E)
RT   and alpha 1 (IX) collagen (COL9A1) on 6q12-q14 in humans.";
RL   Genomics 13:884-886(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 106-1020.
RX   PubMed=7916703; DOI=10.1016/0378-1119(93)90126-n;
RA   Myers J.C., Sun M.J., D'Ippolito J.A., Jabs E.W., Neilson E.G., Dion A.S.;
RT   "Human cDNA clones transcribed from an unusually high-molecular-weight RNA
RT   encode a new collagen chain.";
RL   Gene 123:211-217(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 738-1142.
RC   TISSUE=Skin;
RX   PubMed=8034603; DOI=10.1016/s0021-9258(17)32344-x;
RA   Myers J.C., Yang H., D'Ippolito J.A., Presente A., Miller M.K., Dion A.S.;
RT   "The triple-helical region of human type XIX collagen consists of multiple
RT   collagenous subdomains and exhibits limited sequence homology to alpha
RT   1(XVI).";
RL   J. Biol. Chem. 269:18549-18557(1994).
RN   [8]
RP   FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DOMAIN.
RX   PubMed=12788917; DOI=10.1074/jbc.m304629200;
RA   Myers J.C., Li D., Amenta P.S., Clark C.C., Nagaswami C., Weisel J.W.;
RT   "Type XIX collagen purified from human umbilical cord is characterized by
RT   multiple sharp kinks delineating collagenous subdomains and by
RT   intermolecular aggregates via globular, disulfide-linked, and heparin-
RT   binding amino termini.";
RL   J. Biol. Chem. 278:32047-32057(2003).
RN   [9]
RP   VARIANTS [LARGE SCALE ANALYSIS] ASP-361 AND ASN-1019.
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: May act as a cross-bridge between fibrils and other
CC       extracellular matrix molecules. Involved in skeletal myogenesis in the
CC       developing esophagus. May play a role in organization of the
CC       pericellular matrix or the sphinteric smooth muscle.
CC       {ECO:0000269|PubMed:12788917}.
CC   -!- SUBUNIT: Oligomer; disulfide-linked. {ECO:0000269|PubMed:12788917}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Localized to vascular, neuronal, mesenchymal, and
CC       some epithelial basement membrane zones in umbilical cord.
CC       {ECO:0000269|PubMed:12788917}.
CC   -!- DOMAIN: The numerous interruptions in the triple helix may make this
CC       molecule either elastic or flexible. {ECO:0000269|PubMed:12788917}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC       (G-X-Y) are hydroxylated in some or all of the chains.
CC   -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC       helices (FACIT) family. {ECO:0000305}.
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DR   EMBL; D38163; BAA07368.1; -; mRNA.
DR   EMBL; AB004629; BAA23309.1; -; Genomic_DNA.
DR   EMBL; AL118519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL133388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL160262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC113362; AAI13363.1; -; mRNA.
DR   EMBL; BC113364; AAI13365.1; -; mRNA.
DR   EMBL; M63597; AAA58468.1; -; mRNA.
DR   EMBL; L12347; AAA36358.1; -; mRNA.
DR   EMBL; U09279; AAA21146.1; -; mRNA.
DR   EMBL; AH000850; AAA21147.1; -; Genomic_DNA.
DR   CCDS; CCDS4970.1; -.
DR   PIR; JX0369; JX0369.
DR   RefSeq; NP_001849.2; NM_001858.5.
DR   RefSeq; XP_011533740.1; XM_011535438.2.
DR   RefSeq; XP_016865744.1; XM_017010255.1.
DR   AlphaFoldDB; Q14993; -.
DR   BioGRID; 107705; 1.
DR   ComplexPortal; CPX-1760; Collagen type XIX trimer.
DR   IntAct; Q14993; 1.
DR   STRING; 9606.ENSP00000480474; -.
DR   GlyGen; Q14993; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q14993; -.
DR   PhosphoSitePlus; Q14993; -.
DR   BioMuta; COL19A1; -.
DR   DMDM; 68840003; -.
DR   jPOST; Q14993; -.
DR   MassIVE; Q14993; -.
DR   PaxDb; 9606-ENSP00000480474; -.
DR   PeptideAtlas; Q14993; -.
DR   ProteomicsDB; 60277; -.
DR   Antibodypedia; 31201; 222 antibodies from 27 providers.
DR   DNASU; 1310; -.
DR   Ensembl; ENST00000620364.5; ENSP00000480474.1; ENSG00000082293.13.
DR   GeneID; 1310; -.
DR   KEGG; hsa:1310; -.
DR   MANE-Select; ENST00000620364.5; ENSP00000480474.1; NM_001858.6; NP_001849.2.
DR   UCSC; uc032xam.2; human.
DR   AGR; HGNC:2196; -.
DR   CTD; 1310; -.
DR   DisGeNET; 1310; -.
DR   GeneCards; COL19A1; -.
DR   HGNC; HGNC:2196; COL19A1.
DR   HPA; ENSG00000082293; Tissue enhanced (brain, lymphoid tissue, urinary bladder).
DR   MIM; 120165; gene.
DR   neXtProt; NX_Q14993; -.
DR   OpenTargets; ENSG00000082293; -.
DR   PharmGKB; PA26712; -.
DR   VEuPathDB; HostDB:ENSG00000082293; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000158276; -.
DR   HOGENOM; CLU_282267_0_0_1; -.
DR   InParanoid; Q14993; -.
DR   OMA; FMFQATE; -.
DR   OrthoDB; 3809795at2759; -.
DR   PhylomeDB; Q14993; -.
DR   TreeFam; TF351778; -.
DR   PathwayCommons; Q14993; -.
DR   Reactome; R-HSA-1442490; Collagen degradation.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-HSA-8948216; Collagen chain trimerization.
DR   SignaLink; Q14993; -.
DR   BioGRID-ORCS; 1310; 12 hits in 1149 CRISPR screens.
DR   ChiTaRS; COL19A1; human.
DR   GeneWiki; Collagen,_type_XIX,_alpha_1; -.
DR   GenomeRNAi; 1310; -.
DR   Pharos; Q14993; Tbio.
DR   PRO; PR:Q14993; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q14993; Protein.
DR   Bgee; ENSG00000082293; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 110 other cell types or tissues.
DR   ExpressionAtlas; Q14993; baseline and differential.
DR   GO; GO:0005581; C:collagen trimer; TAS:ProtInc.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF938; COLLAGEN ALPHA-1(XIX) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 10.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   Genevisible; Q14993; HS.
PE   1: Evidence at protein level;
KW   Cell adhesion; Collagen; Developmental protein; Differentiation;
KW   Disulfide bond; Extracellular matrix; Hydroxylation; Myogenesis;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1142
FT                   /note="Collagen alpha-1(XIX) chain"
FT                   /id="PRO_0000005797"
FT   DOMAIN          50..234
FT                   /note="Laminin G-like"
FT   DOMAIN          292..349
FT                   /note="Collagen-like 1"
FT   DOMAIN          350..391
FT                   /note="Collagen-like 2"
FT   DOMAIN          392..433
FT                   /note="Collagen-like 3"
FT   DOMAIN          474..516
FT                   /note="Collagen-like 4"
FT   DOMAIN          568..624
FT                   /note="Collagen-like 5"
FT   DOMAIN          626..678
FT                   /note="Collagen-like 6"
FT   DOMAIN          728..778
FT                   /note="Collagen-like 7"
FT   DOMAIN          779..814
FT                   /note="Collagen-like 8"
FT   DOMAIN          845..903
FT                   /note="Collagen-like 9"
FT   DOMAIN          904..947
FT                   /note="Collagen-like 10"
FT   DOMAIN          948..1004
FT                   /note="Collagen-like 11"
FT   REGION          288..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..351
FT                   /note="Triple-helical region 1 (COL1)"
FT   REGION          370..429
FT                   /note="Triple-helical region 2 (COL2)"
FT   REGION          448..688
FT                   /note="Triple-helical region 3 (COL3)"
FT   REGION          700..818
FT                   /note="Triple-helical region 4 (COL4)"
FT   REGION          704..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..1012
FT                   /note="Triple-helical region 5 (COL5)"
FT   REGION          1053..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1054..1111
FT                   /note="Triple-helical region 6 (COL6)"
FT   MOTIF           952..954
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        334..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..391
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..430
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..854
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         352
FT                   /note="A -> G (in dbSNP:rs2273426)"
FT                   /id="VAR_024419"
FT   VARIANT         361
FT                   /note="G -> D (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs1313704586)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035746"
FT   VARIANT         406
FT                   /note="G -> E (in dbSNP:rs13204209)"
FT                   /id="VAR_048782"
FT   VARIANT         496
FT                   /note="E -> G (in dbSNP:rs13204209)"
FT                   /id="VAR_048783"
FT   VARIANT         1019
FT                   /note="K -> N (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs771562232)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035747"
FT   CONFLICT        89
FT                   /note="I -> MY (in Ref. 2; BAA23309)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106..119
FT                   /note="FRVRRNAKKERWFL -> ETTVPFWRFFVLET (in Ref. 6;
FT                   AAA36358)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279
FT                   /note="Q -> L (in Ref. 1; BAA07368)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354..355
FT                   /note="AG -> GC (in Ref. 5; AAA58468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365
FT                   /note="D -> V (in Ref. 1; BAA07368 and 5; AAA58468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441..442
FT                   /note="YY -> DD (in Ref. 1; BAA07368 and 5; AAA58468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        622..624
FT                   /note="PQG -> QRD (in Ref. 5; AAA58468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        816..823
FT                   /note="GIPFNERN -> VSCSRLKI (in Ref. 6; AAA36358)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        937
FT                   /note="Q -> E (in Ref. 1; BAA07368)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1140
FT                   /note="G -> C (in Ref. 2; BAA23309)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1142 AA;  115221 MW;  F1153CE751387943 CRC64;
     MRLTGPWKLW LWMSIFLLPA STSVTVRDKT EESCPILRIE GHQLTYDNIN KLEVSGFDLG
     DSFSLRRAFC ESDKTCFKLG SALLIRDTIK IFPKGLPEEY SVAAMFRVRR NAKKERWFLW
     QVLNQQNIPQ ISIVVDGGKK VVEFMFQATE GDVLNYIFRN RELRPLFDRQ WHKLGISIQS
     QVISLYMDCN LIARRQTDEK DTVDFHGRTV IATRASDGKP VDIELHQLKI YCSANLIAQE
     TCCEISDTKC PEQDGFGNIA SSWVTAHASK MSSYLPAKQE LKDQCQCIPN KGEAGLPGAP
     GSPGQKGHKG EPGENGLHGA PGFPGQKGEQ GFEGSKGETG EKGEQGEKGD PALAGLNGEN
     GLKGDLGPHG PPGPKGEKGD TGPPGPPALP GSLGIQGPQG PPGKEGQRGR RGKTGPPGKP
     GPPGPPGPPG IQGIHQTLGG YYNKDNKGND EHEAGGLKGD KGETGLPGFP GSVGPKGQKG
     EPGEPFTKGE KGDRGEPGVI GSQGVKGEPG DPGPPGLIGS PGLKGQQGSA GSMGPRGPPG
     DVGLPGEHGI PGKQGIKGEK GDPGGIIGPP GLPGPKGEAG PPGKSLPGEP GLDGNPGAPG
     PRGPKGERGL PGVHGSPGDI GPQGIGIPGR TGAQGPAGEP GIQGPRGLPG LPGTPGTPGN
     DGVPGRDGKP GLPGPPGDPI ALPLLGDIGA LLKNFCGNCQ ASVPGLKSNK GEEGGAGEPG
     KYDSMARKGD IGPRGPPGIP GREGPKGSKG ERGYPGIPGE KGDEGLQGIP GIPGAPGPTG
     PPGLMGRTGH PGPTGAKGEK GSDGPPGKPG PPGPPGIPFN ERNGMSSLYK IKGGVNVPSY
     PGPPGPPGPK GDPGPVGEPG AMGLPGLEGF PGVKGDRGPA GPPGIAGMSG KPGAPGPPGV
     PGEPGERGPV GDIGFPGPEG PSGKPGINGK DGIPGAQGIM GKPGDRGPKG ERGDQGIPGD
     RGSQGERGKP GLTGMKGAIG PMGPPGNKGS MGSPGHQGPP GSPGIPGIPA DAVSFEEIKK
     YINQEVLRIF EERMAVFLSQ LKLPAAMLAA QAYGRPGPPG KDGLPGPPGD PGPQGYRGQK
     GERGEPGIGL PGSPGLPGTS ALGLPGSPGA PGPQGPPGPS GRCNPEDCLY PVSHAHQRTG
     GN
//