COIA1_HUMAN
ID COIA1_HUMAN Reviewed; 1754 AA.
AC P39060; A8MVI4; Q58EX6; Q6RZ39; Q6RZ40; Q6RZ41; Q8N4S4; Q8WXI5; Q96T70;
AC Q9UK38; Q9Y6Q7; Q9Y6Q8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 5.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000305};
DE Contains:
DE RecName: Full=Endostatin {ECO:0000305};
DE Contains:
DE RecName: Full=Non-collagenous domain 1 {ECO:0000305};
DE Short=NC1;
DE Flags: Precursor;
GN Name=COL18A1 {ECO:0000312|HGNC:HGNC:2195};
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] (ISOFORMS 2 AND 3), AND VARIANT ILE-1076.
RX PubMed=9503365; DOI=10.1016/s0945-053x(98)90003-8;
RA Saarela J., Ylikarppa R., Rehn M., Purmonen S., Pihlajaniemi T.;
RT "Complete primary structure of two variant forms of human type XVIII
RT collagen and tissue-specific differences in the expression of the
RT corresponding transcripts.";
RL Matrix Biol. 16:319-328(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP ILE-1076 AND ASN-1675.
RX PubMed=14614989; DOI=10.1016/s0945-053x(03)00073-8;
RA Elamaa H., Snellman A., Rehn M., Autio-Harmainen H., Pihlajaniemi T.;
RT "Characterization of the human type XVIII collagen gene and proteolytic
RT processing and tissue location of the variant containing a frizzled
RT motif.";
RL Matrix Biol. 22:427-442(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ILE-1076.
RC TISSUE=Kidney, and PNS;
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 1069-1754, AND VARIANT ARG-1121.
RX PubMed=8188291; DOI=10.1006/geno.1994.1098;
RA Oh S.P., Warman M.L., Seldin M.F., Cheng S., Knoll J.H., Timmons S.,
RA Olsen B.R.;
RT "Cloning of cDNA and genomic DNA encoding human type XVIII collagen and
RT localization of the alpha 1(XVIII) collagen gene to mouse chromosome 10 and
RT human chromosome 21.";
RL Genomics 19:494-499(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1568-1754.
RX PubMed=11517600;
RA Feng Y., Cui L.B., Liu C.X., Ma Q.J.;
RT "Inhibition effect in vitro of purified endostatin expressed in Pichia
RT pastoris.";
RL Sheng Wu Gong Cheng Xue Bao 17:278-282(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1572-1754, AND VARIANT ASN-1675.
RC TISSUE=Placenta;
RA Zhi-Yong H., Biao L., Wei-Jie Z., Xiang-Fu W.;
RT "Cloning and expression of human endostatin gene in Escherichia coli.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1642-1743.
RA Deininger M.H., Trautmann K., Schluesener H.J.;
RT "Endostatin promotes delayed secondary damage following traumatic brain
RT injury.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION.
RX PubMed=9459295; DOI=10.1016/s0014-5793(97)01503-2;
RA Staendker L., Schrader M., Kanse S.M., Juergens M., Forssmann W.G.,
RA Preissner K.T.;
RT "Isolation and characterization of the circulating form of human
RT endostatin.";
RL FEBS Lett. 420:129-133(1997).
RN [10]
RP GLYCOSYLATION AT THR-1567, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=10441114; DOI=10.1021/bi990787+;
RA John H., Preissner K.T., Forssmann W.G., Staendker L.;
RT "Novel glycosylated forms of human plasma endostatin and circulating
RT endostatin-related fragments of collagen XV.";
RL Biochemistry 38:10217-10224(1999).
RN [11]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=10626789;
RA Wen W., Moses M.A., Wiederschain D., Arbiser J.L., Folkman J.;
RT "The generation of endostatin is mediated by elastase.";
RL Cancer Res. 59:6052-6056(1999).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11257123; DOI=10.1083/jcb.152.6.1233;
RA Kuo C.J., LaMontagne K.R. Jr., Garcia-Cardena G., Ackley B.D., Kalman D.,
RA Park S., Christofferson R., Kamihara J., Ding Y.H., Lo K.M., Gillies S.,
RA Folkman J., Mulligan R.C., Javaherian K.;
RT "Oligomerization-dependent regulation of motility and morphogenesis by the
RT collagen XVIII NC1/endostatin domain.";
RL J. Cell Biol. 152:1233-1246(2001).
RN [13]
RP BIOTECHNOLOGY.
RX PubMed=17644065; DOI=10.1016/j.bbrc.2007.06.155;
RA Ling Y., Yang Y., Lu N., You Q.D., Wang S., Gao Y., Chen Y., Guo Q.L.;
RT "Endostar, a novel recombinant human endostatin, exerts antiangiogenic
RT effect via blocking VEGF-induced tyrosine phosphorylation of KDR/Flk-1 of
RT endothelial cells.";
RL Biochem. Biophys. Res. Commun. 361:79-84(2007).
RN [14]
RP INVOLVEMENT IN KNO1.
RX PubMed=23667181; DOI=10.1136/jmedgenet-2013-101755;
RA Aldahmesh M.A., Khan A.O., Mohamed J.Y., Levin A.V., Wuthisiri W.,
RA Lynch S., McCreery K., Alkuraya F.S.;
RT "No evidence for locus heterogeneity in Knobloch syndrome.";
RL J. Med. Genet. 50:565-566(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-696, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1572-1749, AND ZINC-BINDING SITE.
RX PubMed=9724722; DOI=10.1073/pnas.95.18.10443;
RA Ding Y.-H., Javaherian K., Lo K.-M., Chopra R., Boehm T., Lanciotti J.,
RA Harris B.A., Li Y., Shapiro R., Hohenester E., Timpl R., Folkman J.,
RA Wiley D.C.;
RT "Zinc-dependent dimers observed in crystals of human endostatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10443-10448(1998).
RN [17]
RP INVOLVEMENT IN KNO1, AND FUNCTION.
RX PubMed=10942434; DOI=10.1093/hmg/9.13.2051;
RA Sertie A.L., Sossi V., Camargo A.A., Zatz M., Brahe C., Passos-Bueno M.R.;
RT "Collagen XVIII, containing an endogenous inhibitor of angiogenesis and
RT tumor growth, plays a critical role in the maintenance of retinal structure
RT and in neural tube closure.";
RL Hum. Mol. Genet. 9:2051-2058(2000).
RN [18]
RP VARIANTS ILE-1076 AND ASN-1675.
RX PubMed=11606364;
RA Iughetti P., Suzuki O., Godoi P.H., Alves V.A., Sertie A.L., Zorick T.,
RA Soares F., Camargo A.A., Moreira E.S., di Loreto C., Moreira-Filho C.A.,
RA Simpson A., Oliva G., Passos-Bueno M.R.;
RT "A polymorphism in endostatin, an angiogenesis inhibitor, predisposes for
RT the development of prostatic adenocarcinoma.";
RL Cancer Res. 61:7375-7378(2001).
RN [19]
RP VARIANTS LEU-49; ARG-111; ILE-1076 AND ARG-1121, AND CHARACTERIZATION OF
RP VARIANT ASN-1675.
RX PubMed=14695535; DOI=10.1002/humu.10284;
RA Menzel O., Bekkeheien R.C.J., Reymond A., Fukai N., Boye E.,
RA Kosztolanyi G., Aftimos S., Deutsch S., Scott H.S., Olsen B.R.,
RA Antonarakis S.E., Guipponi M.;
RT "Knobloch syndrome: novel mutations in COL18A1, evidence for genetic
RT heterogeneity, and a functionally impaired polymorphism in endostatin.";
RL Hum. Mutat. 23:77-84(2004).
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-1121.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
RN [21]
RP INVOLVEMENT IN GLCC, AND VARIANT GLCC LYS-184.
RX PubMed=30007336; DOI=10.1093/hmg/ddy256;
RA Suri F., Yazdani S., Chapi M., Safari I., Rasooli P., Daftarian N.,
RA Jafarinasab M.R., Ghasemi Firouzabadi S., Alehabib E., Darvish H.,
RA Klotzle B., Fan J.B., Turk C., Elahi E.;
RT "COL18A1 is a candidate eye iridocorneal angle-closure gene in humans.";
RL Hum. Mol. Genet. 27:3772-3786(2018).
CC -!- FUNCTION: Probably plays a major role in determining the retinal
CC structure as well as in the closure of the neural tube.
CC {ECO:0000269|PubMed:10942434}.
CC -!- FUNCTION: [Non-collagenous domain 1]: May regulate extracellular
CC matrix-dependent motility and morphogenesis of endothelial and non-
CC endothelial cells; the function requires homotrimerization and
CC implicates MAPK signaling. {ECO:0000269|PubMed:11257123}.
CC -!- FUNCTION: [Endostatin]: Potently inhibits endothelial cell
CC proliferation and angiogenesis (PubMed:9459295). May inhibit
CC angiogenesis by binding to the heparan sulfate proteoglycans involved
CC in growth factor signaling (By similarity). Inhibits VEGFA-induced
CC endothelial cell proliferation and migration. Seems to inhibit VEGFA-
CC mediated signaling by blocking the interaction of VEGFA to its receptor
CC KDR/VEGFR2. Modulates endothelial cell migration in an integrin-
CC dependent manner implicating integrin ITGA5:ITGB1 and to a lesser
CC extent ITGAV:ITGB3 and ITGAV:ITGB5 (By similarity). May negatively
CC regulate the activity of homotrimeric non-collagenous domain 1
CC (PubMed:11257123). {ECO:0000250|UniProtKB:P39061,
CC ECO:0000269|PubMed:11257123, ECO:0000269|PubMed:9459295}.
CC -!- SUBUNIT: [Non-collagenous domain 1]: Forms homotrimers
CC (PubMed:11257123). Recombinant non-collagenous domain 1 has stronger
CC affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower affinity
CC to FBLN1 and FBLN2 than endostatin (By similarity).
CC {ECO:0000250|UniProtKB:P39061, ECO:0000269|PubMed:11257123}.
CC -!- SUBUNIT: [Endostatin]: Monomeric (PubMed:11257123). Interacts with
CC KDR/VEGFR2. Interacts with the ITGA5:ITGB1 complex. Interacts with
CC NID1, HSPG2, laminin-1:NID1 complex, FBLN1 and FBLN2 (By similarity).
CC {ECO:0000250|UniProtKB:P39061, ECO:0000269|PubMed:11257123}.
CC -!- INTERACTION:
CC PRO_0000005794; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-2566375, EBI-821758;
CC PRO_0000005794; PRO_0000005794 [P39060]: COL18A1; NbExp=6; IntAct=EBI-2566375, EBI-2566375;
CC PRO_0000005794; P19338: NCL; NbExp=12; IntAct=EBI-2566375, EBI-346967;
CC PRO_0000005794; Q15113: PCOLCE; NbExp=4; IntAct=EBI-2566375, EBI-8869614;
CC PRO_0000005794; P21980: TGM2; NbExp=2; IntAct=EBI-2566375, EBI-727668;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250|UniProtKB:P39061}.
CC -!- SUBCELLULAR LOCATION: [Non-collagenous domain 1]: Secreted,
CC extracellular space, extracellular matrix, basement membrane
CC {ECO:0000250|UniProtKB:P39061}. Secreted
CC {ECO:0000250|UniProtKB:P39061}.
CC -!- SUBCELLULAR LOCATION: [Endostatin]: Secreted
CC {ECO:0000269|PubMed:10441114}. Secreted, extracellular space,
CC extracellular matrix, basement membrane {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NC1-728;
CC IsoId=P39060-3; Sequence=Displayed;
CC Name=2; Synonyms=Long, NC-493;
CC IsoId=P39060-1; Sequence=VSP_023131;
CC Name=3; Synonyms=Short, NC1-303;
CC IsoId=P39060-2; Sequence=VSP_023130, VSP_023132;
CC -!- TISSUE SPECIFICITY: Present in multiple organs with highest levels in
CC liver, lung and kidney.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) of the triple-helical regions are hydroxylated.
CC -!- PTM: Circulating endostatins are found as sialoglycoprotein and
CC asialoglycoprotein structures. {ECO:0000269|PubMed:10441114}.
CC -!- PTM: Undergoes proteolytic processing by CTSL/cathepsin-L and elastase-
CC like proteases to generate both non-collagenous domain 1 trimers and
CC endostatin monomers (PubMed:10626789). In tissue extracts (brain,
CC skeletal muscle, heart, kidney, testis and liver) predominantly bands
CC of approximately 38 kDa are detected; recombinant non-collagenous
CC domain 1 shows similar mobility. In vitro, several proteolytic cleavage
CC sites in the non-collagenous domain 1 hinge region generating different
CC endostatin-like peptides are reported (By similarity).
CC {ECO:0000250|UniProtKB:P39061, ECO:0000269|PubMed:10626789}.
CC -!- POLYMORPHISM: There is an association between a polymorphism in
CC position 1675 and prostate cancer. Heterozygous Asn-1675 individuals
CC have a 2.5 times increased chance of developing prostate cancer as
CC compared with homozygous Asp-1675 individuals.
CC -!- DISEASE: Knobloch syndrome 1 (KNO1) [MIM:267750]: A developmental
CC disorder primarily characterized by typical eye abnormalities,
CC including high myopia, cataracts, dislocated lens, vitreoretinal
CC degeneration, and retinal detachment, with occipital skull defects,
CC which can range from occipital encephalocele to occult cutis aplasia.
CC {ECO:0000269|PubMed:10942434, ECO:0000269|PubMed:23667181}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Glaucoma, primary closed-angle (GLCC) [MIM:618880]: An
CC autosomal dominant form of primary glaucoma, an ocular disease
CC characterized by a marked increase of intraocular pressure causing
CC damage to eye structures and function. GLCC is characterized by
CC elevated intraocular pressure due to iridocorneal angle closure with
CC retention of the aqueous humor in the anterior chamber. Iridocorneal
CC angle changes are apparent in the fourth to fifth decade of life, and
CC patients manifest age-related variation in the severity of glaucomatous
CC damage. {ECO:0000269|PubMed:30007336}. Note=The disease may be caused
CC by variants affecting the gene represented in this entry.
CC -!- BIOTECHNOLOGY: [Endostatin]: Available under the name Endostar (Jiangsu
CC Simcere Pharmaceutical) for the treatment of non-small-cell lung
CC cancer. {ECO:0000269|PubMed:17644065, ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family. {ECO:0000305}.
CC -!- CAUTION: Non-collagenous domain 1 seems to be the predominant tissue
CC form from which endostatin is cleaved. However, the proteolytic
CC cleavage site to generate non-collagenous domain 1 is not known.
CC Soluble recombinant non-collagenous domain 1 amenable to biochemical
CC studies has been used instead. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF018081; AAC39658.1; -; mRNA.
DR EMBL; AF018082; AAC39659.1; -; mRNA.
DR EMBL; AY484971; AAR83296.1; -; Genomic_DNA.
DR EMBL; AY484968; AAR83296.1; JOINED; Genomic_DNA.
DR EMBL; AY484969; AAR83296.1; JOINED; Genomic_DNA.
DR EMBL; AY484970; AAR83296.1; JOINED; Genomic_DNA.
DR EMBL; AY484971; AAR83297.1; -; Genomic_DNA.
DR EMBL; AY484968; AAR83297.1; JOINED; Genomic_DNA.
DR EMBL; AY484969; AAR83297.1; JOINED; Genomic_DNA.
DR EMBL; AY484970; AAR83297.1; JOINED; Genomic_DNA.
DR EMBL; AY484971; AAR83298.1; -; Genomic_DNA.
DR EMBL; AY484967; AAR83298.1; JOINED; Genomic_DNA.
DR EMBL; AY484969; AAR83298.1; JOINED; Genomic_DNA.
DR EMBL; AY484970; AAR83298.1; JOINED; Genomic_DNA.
DR EMBL; AL163302; CAB90482.1; -; Genomic_DNA.
DR EMBL; BX322561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033715; AAH33715.1; -; mRNA.
DR EMBL; BC063833; AAH63833.1; -; mRNA.
DR EMBL; L22548; AAA51864.1; -; mRNA.
DR EMBL; AF416592; AAL37720.1; -; mRNA.
DR EMBL; AF184060; AAF01310.1; -; mRNA.
DR EMBL; AF333247; AAK50626.1; -; mRNA.
DR CCDS; CCDS42971.1; -. [P39060-2]
DR RefSeq; NP_085059.2; NM_030582.3.
DR RefSeq; NP_569711.2; NM_130444.2.
DR RefSeq; NP_569712.2; NM_130445.3.
DR PDB; 1BNL; X-ray; 2.90 A; A/B/C/D=1572-1749.
DR PDB; 3HON; X-ray; 3.00 A; A=1441-1496.
DR PDB; 3HSH; X-ray; 1.80 A; A/B/C/D/E/F=1441-1496.
DR PDBsum; 1BNL; -.
DR PDBsum; 3HON; -.
DR PDBsum; 3HSH; -.
DR AlphaFoldDB; P39060; -.
DR SMR; P39060; -.
DR BioGRID; 123311; 121.
DR ComplexPortal; CPX-1759; Collagen type XVIII trimer.
DR CORUM; P39060; -.
DR IntAct; P39060; 30.
DR MINT; P39060; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyConnect; 127; 1 N-Linked glycan (1 site), 1 O-Linked glycan (1 site).
DR GlyGen; P39060; 29 sites, 1 N-linked glycan (1 site), 9 O-linked glycans (25 sites).
DR iPTMnet; P39060; -.
DR PhosphoSitePlus; P39060; -.
DR BioMuta; COL18A1; -.
DR DMDM; 215274264; -.
DR EPD; P39060; -.
DR jPOST; P39060; -.
DR MassIVE; P39060; -.
DR MaxQB; P39060; -.
DR PaxDb; P39060; -.
DR PeptideAtlas; P39060; -.
DR PRIDE; P39060; -.
DR ProteomicsDB; 55311; -. [P39060-3]
DR ProteomicsDB; 55312; -. [P39060-1]
DR ProteomicsDB; 55313; -. [P39060-2]
DR Antibodypedia; 2814; 606 antibodies from 37 providers.
DR DNASU; 80781; -.
DR Ensembl; ENST00000355480.10; ENSP00000347665.5; ENSG00000182871.16. [P39060-1]
DR Ensembl; ENST00000359759.8; ENSP00000352798.4; ENSG00000182871.16. [P39060-3]
DR Ensembl; ENST00000651438.1; ENSP00000498485.1; ENSG00000182871.16. [P39060-2]
DR GeneID; 80781; -.
DR KEGG; hsa:80781; -.
DR MANE-Select; ENST00000651438.1; ENSP00000498485.1; NM_001379500.1; NP_001366429.1. [P39060-2]
DR UCSC; uc062awf.1; human. [P39060-3]
DR CTD; 80781; -.
DR DisGeNET; 80781; -.
DR GeneCards; COL18A1; -.
DR HGNC; HGNC:2195; COL18A1.
DR HPA; ENSG00000182871; Tissue enhanced (liver).
DR MalaCards; COL18A1; -.
DR MIM; 120328; gene.
DR MIM; 267750; phenotype.
DR MIM; 618880; phenotype.
DR neXtProt; NX_P39060; -.
DR OpenTargets; ENSG00000182871; -.
DR Orphanet; 1571; Knobloch syndrome.
DR PharmGKB; PA26711; -.
DR VEuPathDB; HostDB:ENSG00000182871; -.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000158212; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR InParanoid; P39060; -.
DR OMA; AFTGQWT; -.
DR OrthoDB; 1362001at2759; -.
DR PhylomeDB; P39060; -.
DR TreeFam; TF315821; -.
DR PathwayCommons; P39060; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; P39060; -.
DR SIGNOR; P39060; -.
DR BioGRID-ORCS; 80781; 6 hits in 1076 CRISPR screens.
DR ChiTaRS; COL18A1; human.
DR EvolutionaryTrace; P39060; -.
DR GeneWiki; Collagen,_type_XVIII,_alpha_1; -.
DR GenomeRNAi; 80781; -.
DR Pharos; P39060; Tbio.
DR PRO; PR:P39060; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P39060; protein.
DR Bgee; ENSG00000182871; Expressed in right coronary artery and 188 other tissues.
DR ExpressionAtlas; P39060; baseline and differential.
DR Genevisible; P39060; HS.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; TAS:ProtInc.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd07455; CRD_Collagen_XVIII; 1.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR035523; Collagen_XVIII_Fz.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR010363; DUF959_COL18_N.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Basement membrane; Cell adhesion; Collagen; Disulfide bond;
KW Extracellular matrix; Glaucoma; Glycoprotein; Hydroxylation; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1754
FT /note="Collagen alpha-1(XVIII) chain"
FT /id="PRO_0000005793"
FT CHAIN 1572..1754
FT /note="Endostatin"
FT /id="PRO_0000005794"
FT CHAIN ?..1754
FT /note="Non-collagenous domain 1"
FT /id="PRO_0000441861"
FT DOMAIN 329..446
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 456..644
FT /note="Laminin G-like"
FT REGION 42..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..751
FT /note="Nonhelical region 1 (NC1)"
FT REGION 752..785
FT /note="Triple-helical region 1 (COL1)"
FT REGION 786..795
FT /note="Nonhelical region 2 (NC2)"
FT REGION 796..875
FT /note="Triple-helical region 2 (COL2)"
FT REGION 876..899
FT /note="Nonhelical region 3 (NC3)"
FT REGION 900..1021
FT /note="Triple-helical region 3 (COL3)"
FT REGION 1022..1044
FT /note="Nonhelical region 4 (NC4)"
FT REGION 1045..1127
FT /note="Triple-helical region 4 (COL4)"
FT REGION 1128..1141
FT /note="Nonhelical region 5 (NC5)"
FT REGION 1142..1183
FT /note="Triple-helical region 5 (COL5)"
FT REGION 1184..1196
FT /note="Nonhelical region 6 (NC6)"
FT REGION 1197..1269
FT /note="Triple-helical region 6 (COL6)"
FT REGION 1270..1279
FT /note="Nonhelical region 7 (NC7)"
FT REGION 1280..1312
FT /note="Triple-helical region 7 (COL7)"
FT REGION 1313..1324
FT /note="Nonhelical region 8 (NC8)"
FT REGION 1325..1346
FT /note="Triple-helical region 8 (COL8)"
FT REGION 1347..1353
FT /note="Nonhelical region 9 (NC9)"
FT REGION 1354..1411
FT /note="Triple-helical region 9 (COL9)"
FT REGION 1412..1424
FT /note="Nonhelical region 10 (NC10)"
FT REGION 1425..1442
FT /note="Triple-helical region 10 (COL10)"
FT REGION 1443..1754
FT /note="Nonhelical region 11 (NC11)"
FT REGION 1456..1501
FT /note="Non-collagenous domain 1 association domain"
FT /evidence="ECO:0000250|UniProtKB:P39061"
FT REGION 1502..1571
FT /note="Non-collagenous domain 1 hinge region"
FT /evidence="ECO:0000250|UniProtKB:P39061"
FT REGION 1511..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1330..1332
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 54..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..962
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1369
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 696
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1567
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:10441114"
FT /id="CAR_000150"
FT DISULFID 334..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 344..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 381..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 408..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 412..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 1604..1744
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 1706..1736
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT VAR_SEQ 1..415
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9503365"
FT /id="VSP_023130"
FT VAR_SEQ 216..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9503365"
FT /id="VSP_023131"
FT VAR_SEQ 416..450
FT /note="QDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAA -> MAPRCPWPWPRRR
FT RLLDVLAPLVLLLGVRAASAEP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9503365"
FT /id="VSP_023132"
FT VARIANT 49
FT /note="Q -> L (in dbSNP:rs61735029)"
FT /evidence="ECO:0000269|PubMed:14695535"
FT /id="VAR_018053"
FT VARIANT 111
FT /note="G -> R (in dbSNP:rs114139997)"
FT /evidence="ECO:0000269|PubMed:14695535"
FT /id="VAR_018054"
FT VARIANT 184
FT /note="E -> K (in GLCC; unknown pathological significance;
FT dbSNP:rs749957649)"
FT /evidence="ECO:0000269|PubMed:30007336"
FT /id="VAR_084282"
FT VARIANT 288
FT /note="A -> T (in dbSNP:rs11702494)"
FT /id="VAR_059232"
FT VARIANT 379
FT /note="T -> M (in dbSNP:rs8133886)"
FT /id="VAR_061115"
FT VARIANT 1076
FT /note="V -> I (in dbSNP:rs62000962)"
FT /evidence="ECO:0000269|PubMed:11606364,
FT ECO:0000269|PubMed:14614989, ECO:0000269|PubMed:14695535,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9503365"
FT /id="VAR_018055"
FT VARIANT 1121
FT /note="P -> R (in dbSNP:rs79980197)"
FT /evidence="ECO:0000269|PubMed:14695535,
FT ECO:0000269|PubMed:18987736, ECO:0000269|PubMed:8188291"
FT /id="VAR_018056"
FT VARIANT 1195
FT /note="Q -> H (in dbSNP:rs2230693)"
FT /id="VAR_059233"
FT VARIANT 1675
FT /note="D -> N (may be associated with increased risk for
FT prostate cancer; results in decreased affinity for laminin;
FT dbSNP:rs12483377)"
FT /evidence="ECO:0000269|PubMed:11606364,
FT ECO:0000269|PubMed:14614989, ECO:0000269|PubMed:14695535,
FT ECO:0000269|Ref.7"
FT /id="VAR_012709"
FT CONFLICT 299
FT /note="R -> K (in Ref. 2; AAR83296)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="S -> F (in Ref. 1; AAC39658/AAC39659)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112
FT /note="V -> L (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1147
FT /note="P -> R (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1168
FT /note="R -> L (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1210
FT /note="P -> L (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1299
FT /note="A -> P (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="L -> K (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1355
FT /note="P -> A (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1358
FT /note="P -> A (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1362..1364
FT /note="Missing (in Ref. 1; AAC39658/AAC39659, 2; AAR83296/
FT AAR83297/AAR83298, 4; AAH33715/AAH63833 and 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1444
FT /note="G -> GQ (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1542
FT /note="R -> G (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1552
FT /note="A -> G (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1561..1562
FT /note="LR -> CG (in Ref. 5; AAA51864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1681
FT /note="R -> T (in Ref. 7; AAF01310)"
FT /evidence="ECO:0000305"
FT CONFLICT 1685
FT /note="W -> R (in Ref. 8; AAK50626)"
FT /evidence="ECO:0000305"
FT CONFLICT 1721
FT /note="S -> Y (in Ref. 7; AAF01310)"
FT /evidence="ECO:0000305"
FT CONFLICT 1736
FT /note="C -> S (in Ref. 8; AAK50626)"
FT /evidence="ECO:0000305"
FT STRAND 1445..1450
FT /evidence="ECO:0007829|PDB:3HSH"
FT HELIX 1451..1457
FT /evidence="ECO:0007829|PDB:3HSH"
FT HELIX 1458..1460
FT /evidence="ECO:0007829|PDB:3HSH"
FT STRAND 1466..1469
FT /evidence="ECO:0007829|PDB:3HSH"
FT TURN 1470..1473
FT /evidence="ECO:0007829|PDB:3HSH"
FT STRAND 1474..1479
FT /evidence="ECO:0007829|PDB:3HSH"
FT STRAND 1482..1486
FT /evidence="ECO:0007829|PDB:3HSH"
FT STRAND 1488..1493
FT /evidence="ECO:0007829|PDB:3HSH"
FT STRAND 1581..1585
FT /evidence="ECO:0007829|PDB:1BNL"
FT HELIX 1597..1610
FT /evidence="ECO:0007829|PDB:1BNL"
FT STRAND 1617..1621
FT /evidence="ECO:0007829|PDB:1BNL"
FT HELIX 1629..1631
FT /evidence="ECO:0007829|PDB:1BNL"
FT HELIX 1634..1636
FT /evidence="ECO:0007829|PDB:1BNL"
FT STRAND 1649..1652
FT /evidence="ECO:0007829|PDB:1BNL"
FT HELIX 1654..1657
FT /evidence="ECO:0007829|PDB:1BNL"
FT HELIX 1679..1681
FT /evidence="ECO:0007829|PDB:1BNL"
FT STRAND 1689..1691
FT /evidence="ECO:0007829|PDB:1BNL"
FT HELIX 1706..1709
FT /evidence="ECO:0007829|PDB:1BNL"
FT STRAND 1716..1722
FT /evidence="ECO:0007829|PDB:1BNL"
FT HELIX 1723..1725
FT /evidence="ECO:0007829|PDB:1BNL"
FT STRAND 1727..1729
FT /evidence="ECO:0007829|PDB:1BNL"
FT STRAND 1732..1735
FT /evidence="ECO:0007829|PDB:1BNL"
FT STRAND 1743..1747
FT /evidence="ECO:0007829|PDB:1BNL"
SQ SEQUENCE 1754 AA; 178188 MW; 23A327DCBD3B328D CRC64;
MAPYPCGCHI LLLLFCCLAA ARANLLNLNW LWFNNEDTSH AATTIPEPQG PLPVQPTADT
TTHVTPRNGS TEPATAPGSP EPPSELLEDG QDTPTSAESP DAPEENIAGV GAEILNVAKG
IRSFVQLWND TVPTESLARA ETLVLETPVG PLALAGPSST PQENGTTLWP SRGIPSSPGA
HTTEAGTLPA PTPSPPSLGR PWAPLTGPSV PPPSSGRASL SSLLGGAPPW GSLQDPDSQG
LSPAAAAPSQ QLQRPDVRLR TPLLHPLVMG SLGKHAAPSA FSSGLPGALS QVAVTTLTRD
SGAWVSHVAN SVGPGLANNS ALLGADPEAP AGRCLPLPPS LPVCGHLGIS RFWLPNHLHH
ESGEQVRAGA RAWGGLLQTH CHPFLAWFFC LLLVPPCGSV PPPAPPPCCQ FCEALQDACW
SRLGGGRLPV ACASLPTQED GYCVLIGPAA ERISEEVGLL QLLGDPPPQQ VTQTDDPDVG
LAYVFGPDAN SGQVARYHFP SLFFRDFSLL FHIRPATEGP GVLFAITDSA QAMVLLGVKL
SGVQDGHQDI SLLYTEPGAG QTHTAASFRL PAFVGQWTHL ALSVAGGFVA LYVDCEEFQR
MPLARSSRGL ELEPGAGLFV AQAGGADPDK FQGVIAELKV RRDPQVSPMH CLDEEGDDSD
GASGDSGSGL GDARELLREE TGAALKPRLP APPPVTTPPL AGGSSTEDSR SEEVEEQTTV
ASLGAQTLPG SDSVSTWDGS VRTPGGRVKE GGLKGQKGEP GVPGPPGRAG PPGSPCLPGP
PGLPCPVSPL GPAGPALQTV PGPQGPPGPP GRDGTPGRDG EPGDPGEDGK PGDTGPQGFP
GTPGDVGPKG DKGDPGVGER GPPGPQGPPG PPGPSFRHDK LTFIDMEGSG FGGDLEALRG
PRGFPGPPGP PGVPGLPGEP GRFGVNSSDV PGPAGLPGVP GREGPPGFPG LPGPPGPPGR
EGPPGRTGQK GSLGEAGAPG HKGSKGAPGP AGARGESGLA GAPGPAGPPG PPGPPGPPGP
GLPAGFDDME GSGGPFWSTA RSADGPQGPP GLPGLKGDPG VPGLPGAKGE VGADGVPGFP
GLPGREGIAG PQGPKGDRGS RGEKGDPGKD GVGQPGLPGP PGPPGPVVYV SEQDGSVLSV
PGPEGRPGFA GFPGPAGPKG NLGSKGERGS PGPKGEKGEP GSIFSPDGGA LGPAQKGAKG
EPGFRGPPGP YGRPGYKGEI GFPGRPGRPG MNGLKGEKGE PGDASLGFGM RGMPGPPGPP
GPPGPPGTPV YDSNVFAESS RPGPPGLPGN QGPPGPKGAK GEVGPPGPPG QFPFDFLQLE
AEMKGEKGDR GDAGQKGERG EPGGGGFFGS SLPGPPGPPG PPGPRGYPGI PGPKGESIRG
QPGPPGPQGP PGIGYEGRQG PPGPPGPPGP PSFPGPHRQT ISVPGPPGPP GPPGPPGTMG
ASSGVRLWAT RQAMLGQVHE VPEGWLIFVA EQEELYVRVQ NGFRKVQLEA RTPLPRGTDN
EVAALQPPVV QLHDSNPYPR REHPHPTARP WRADDILASP PRLPEPQPYP GAPHHSSYVH
LRPARPTSPP AHSHRDFQPV LHLVALNSPL SGGMRGIRGA DFQCFQQARA VGLAGTFRAF
LSSRLQDLYS IVRRADRAAV PIVNLKDELL FPSWEALFSG SEGPLKPGAR IFSFDGKDVL
RHPTWPQKSV WHGSDPNGRR LTESYCETWR TEAPSATGQA SSLLGGRLLG QSAASCHHAY
IVLCIENSFM TASK
