ID COFA1_MOUSE Reviewed; 1367 AA.
AC O35206; A2AJY3; Q3UZ71; Q9EQD9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Collagen alpha-1(XV) chain;
DE Contains:
DE RecName: Full=Restin;
DE AltName: Full=Endostatin-XV;
DE Flags: Precursor;
GN Name=Col15a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Kidney;
RX PubMed=9339358; DOI=10.1006/geno.1997.4884;
RA Haegg P.M., Horelli-Kuitunen N., Eklund L., Palotie A., Pihlajaniemi T.;
RT "Cloning of mouse type XV collagen sequences and mapping of the
RT corresponding gene to 4B1-3. Comparison of mouse and human alpha 1 (XV)
RT collagen sequences indicates divergence in the number of small collagenous
RT domains.";
RL Genomics 45:31-41(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11068203; DOI=10.1016/s0945-053x(00)00090-1;
RA Eklund L., Muona A., Lietard J., Pihlajaniemi T.;
RT "Structure of the mouse type XV collagen gene, Col15a1, comparison with the
RT human COL15A1 gene and functional analysis of the promoters of both
RT genes.";
RL Matrix Biol. 19:489-500(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP FUNCTION.
RX PubMed=10966814; DOI=10.1006/jmbi.2000.3996;
RA Sasaki T., Larsson H., Tisi D., Claesson-Welsh L., Hohenester E., Timpl R.;
RT "Endostatins derived from collagens XV and XVIII differ in structural and
RT binding properties, tissue distribution and anti-angiogenic activity.";
RL J. Mol. Biol. 301:1179-1190(2000).
RN [6]
RP FUNCTION.
RX PubMed=11158616; DOI=10.1073/pnas.98.3.1194;
RA Eklund L., Piuhola J., Komulainen J., Sormunen R., Ongvarrasopone C.,
RA Faessler R., Muona A., Ilves M., Ruskoaho H., Takala T.E.S.,
RA Pihlajaniemi T.;
RT "Lack of type XV collagen causes a skeletal myopathy and cardiovascular
RT defects in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1194-1199(2001).
RN [7]
RP INTERACTION WITH EFEMP2.
RX PubMed=17324935; DOI=10.1074/jbc.m611029200;
RA Kobayashi N., Kostka G., Garbe J.H., Keene D.R., Baechinger H.P.,
RA Hanisch F.G., Markova D., Tsuda T., Timpl R., Chu M.L., Sasaki T.;
RT "A comparative analysis of the fibulin protein family. Biochemical
RT characterization, binding interactions, and tissue localization.";
RL J. Biol. Chem. 282:11805-11816(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1192-1367, AND DISULFIDE BONDS.
RX PubMed=9501087; DOI=10.1093/emboj/17.6.1656;
RA Hohenester E., Sasaki T., Olsen B.R., Timpl R.;
RT "Crystal structure of the angiogenesis inhibitor endostatin at 1.5-A
RT resolution.";
RL EMBO J. 17:1656-1664(1998).
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC -!- FUNCTION: Restin potently inhibits angiogenesis.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBUNIT: [Restin]: Interacts moderately with EFEMP2.
CC {ECO:0000269|PubMed:17324935}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Secreted {ECO:0000250|UniProtKB:P39059}.
CC -!- TISSUE SPECIFICITY: Detected in testis, brain, heart, kidney, skeletal
CC muscle and skin (at protein level). Detected in heart and skeletal
CC muscle. {ECO:0000269|PubMed:9339358}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels from day 7 to 11 of
CC embryonic development. Levels are much increased and remain high from
CC day 15 to 17.
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. {ECO:0000250}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate.
CC {ECO:0000250|UniProtKB:P39059}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family. {ECO:0000305}.
CC -!- CAUTION: The name Restin has also been used for CAP-Gly domain-
CC containing linker protein 1 the product of the CLIP1 gene.
CC {ECO:0000305}.
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DR EMBL; AF011450; AAC53387.1; -; mRNA.
DR EMBL; AF261131; AAG27545.1; -; Genomic_DNA.
DR EMBL; AF261109; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261110; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261111; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261112; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261113; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261114; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261115; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261116; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261117; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261118; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261119; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261120; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261121; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261122; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261123; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261124; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261125; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261126; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261127; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261128; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261129; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AF261130; AAG27545.1; JOINED; Genomic_DNA.
DR EMBL; AK134030; BAE21987.1; -; mRNA.
DR EMBL; AL772232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18159.1; -.
DR RefSeq; NP_034058.2; NM_009928.3.
DR PDB; 1DY2; X-ray; 2.00 A; A=1192-1367.
DR PDBsum; 1DY2; -.
DR AlphaFoldDB; O35206; -.
DR SMR; O35206; -.
DR ComplexPortal; CPX-2993; Collagen type XV trimer.
DR IntAct; O35206; 1.
DR STRING; 10090.ENSMUSP00000099981; -.
DR GlyCosmos; O35206; 9 sites, No reported glycans.
DR GlyGen; O35206; 13 sites.
DR PhosphoSitePlus; O35206; -.
DR MaxQB; O35206; -.
DR PaxDb; 10090-ENSMUSP00000099981; -.
DR ProteomicsDB; 283486; -.
DR Antibodypedia; 14522; 147 antibodies from 20 providers.
DR DNASU; 12819; -.
DR Ensembl; ENSMUST00000102917.11; ENSMUSP00000099981.5; ENSMUSG00000028339.18.
DR GeneID; 12819; -.
DR KEGG; mmu:12819; -.
DR UCSC; uc008sum.1; mouse.
DR AGR; MGI:88449; -.
DR CTD; 1306; -.
DR MGI; MGI:88449; Col15a1.
DR VEuPathDB; HostDB:ENSMUSG00000028339; -.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000158302; -.
DR InParanoid; O35206; -.
DR OMA; FFMSGPP; -.
DR OrthoDB; 5363002at2759; -.
DR PhylomeDB; O35206; -.
DR TreeFam; TF315821; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12819; 0 hits in 78 CRISPR screens.
DR ChiTaRS; Col15a1; mouse.
DR EvolutionaryTrace; O35206; -.
DR PRO; PR:O35206; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O35206; Protein.
DR Bgee; ENSMUSG00000028339; Expressed in ascending aorta and 203 other cell types or tissues.
DR ExpressionAtlas; O35206; baseline and differential.
DR Genevisible; O35206; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
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:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF912; COLLAGEN ALPHA-1(XV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1367
FT /note="Collagen alpha-1(XV) chain"
FT /id="PRO_0000005790"
FT CHAIN 1177..1365
FT /note="Restin"
FT /id="PRO_0000005791"
FT DOMAIN 54..249
FT /note="Laminin G-like"
FT DOMAIN 605..665
FT /note="Collagen-like 1"
FT DOMAIN 666..717
FT /note="Collagen-like 2"
FT DOMAIN 808..850
FT /note="Collagen-like 3"
FT DOMAIN 863..912
FT /note="Collagen-like 4"
FT REGION 229..604
FT /note="Nonhelical region 1 (NC1)"
FT REGION 267..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..718
FT /note="Triple-helical region 1 (COL1)"
FT REGION 719..748
FT /note="Nonhelical region 2 (NC2)"
FT REGION 749..783
FT /note="Triple-helical region 2 (COL2)"
FT REGION 784..807
FT /note="Nonhelical region 3 (NC3)"
FT REGION 808..852
FT /note="Triple-helical region 3 (COL3)"
FT REGION 853..863
FT /note="Nonhelical region 4 (NC4)"
FT REGION 864..934
FT /note="Triple-helical region 4 (COL4)"
FT REGION 905..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..968
FT /note="Nonhelical region 5 (NC5)"
FT REGION 969..998
FT /note="Triple-helical region 5 (COL5)"
FT REGION 974..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1031
FT /note="Nonhelical region 6 (NC6)"
FT REGION 1032..1086
FT /note="Triple-helical region 6 (COL6)"
FT REGION 1055..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1096
FT /note="Nonhelical region 7 (NC7)"
FT REGION 1097..1111
FT /note="Triple-helical region 7 (COL7)"
FT REGION 1112..1367
FT /note="Nonhelical region 8 (NC8)"
FT COMPBIAS 305..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1089
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 243
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P39059"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P39059"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1216..1356
FT /evidence="ECO:0000269|PubMed:9501087"
FT DISULFID 1318..1348
FT /evidence="ECO:0000269|PubMed:9501087"
FT CONFLICT 380
FT /note="T -> L (in Ref. 1; AAC53387)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="T -> K (in Ref. 3; BAE21987)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="R -> K (in Ref. 2; AAG27545)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="S -> A (in Ref. 2; AAG27545)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="T -> P (in Ref. 1; AAC53387 and 2; AAG27545)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="L -> M (in Ref. 2; AAG27545)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="P -> R (in Ref. 1; AAC53387)"
FT /evidence="ECO:0000305"
FT CONFLICT 1116
FT /note="A -> G (in Ref. 1; AAC53387 and 2; AAG27545)"
FT /evidence="ECO:0000305"
FT CONFLICT 1309
FT /note="H -> Y (in Ref. 2; AAG27545)"
FT /evidence="ECO:0000305"
FT STRAND 1197..1201
FT /evidence="ECO:0007829|PDB:1DY2"
FT HELIX 1212..1222
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1229..1233
FT /evidence="ECO:0007829|PDB:1DY2"
FT HELIX 1240..1242
FT /evidence="ECO:0007829|PDB:1DY2"
FT HELIX 1246..1248
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1249..1251
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1261..1264
FT /evidence="ECO:0007829|PDB:1DY2"
FT HELIX 1267..1270
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1271..1273
FT /evidence="ECO:0007829|PDB:1DY2"
FT TURN 1291..1293
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1301..1303
FT /evidence="ECO:0007829|PDB:1DY2"
FT HELIX 1318..1321
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1329..1334
FT /evidence="ECO:0007829|PDB:1DY2"
FT HELIX 1335..1337
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1339..1341
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1344..1347
FT /evidence="ECO:0007829|PDB:1DY2"
FT STRAND 1355..1358
FT /evidence="ECO:0007829|PDB:1DY2"
SQ SEQUENCE 1367 AA; 140472 MW; BD92E26B5E99B607 CRC64;
MTHRRTAQGR RPRWLLSIIS ALLSAVLQTR AATGSASQVH LDLTVLIGVP LPSSVSFTTG
YGGFPAYSFG PGANVGRPAR TLIPPTFFRD FAIGVAVKPN SAQGGVLFAI TDAFQKVIYL
GLRLSSVEDG RQRVILYYTE PGSHVSREAA VFSVPVMTNR WNRFAVTVQG EEVALFMDCE
EQSQVRFQRS SWPLTFEPSA GIFVGNAGAM GLERFTGSIQ QLTIYSDPRT PEELCEAQES
SASGEASGFQ EMDEVAEIME AVTYTQAPPK ESHVDPISVP PTSSSPAEDS ELSGEPVPEG
TPETNLSIIG HSSPEQGSGE ILNDTLEVHA MDGDPGTDDG SGDGALLNVT DGQGLSATAT
GEASVPVTTV LEAENGSMPT GSPTLAMFTQ SIREVDTPDP ENLTTTASGD GEVPTSTDGD
TEADSSPTGG PTLKPREEAT LGSHGEEWLT PAVSKMPLKA FEEEEASGTA IDSLDVIFTP
TVVLEQVSRR PTDIQATFTP TVVLEETSGA PTDTQDALTP TVAPEQMFTA EPTDGGDLVA
STEEAEEEGS GSMPPSGPPL PTPTVTPKRQ VTLVGVEAEG SGPVGGLDEG SGSGDIVGNE
DLLRGPPGPP GPPGSPGIPG KPGTDVFMGP PGSPGEDGAP GEPGPQGPEG QPGLDGASGQ
QGMKGEKGAR GPNGSAGEKG DPGNRGLPGP PGKNGEVGTP GVMGPPGPPG PPGPPGPGCT
TELGFEIEGS GDVRLLSKPT ISGPTSPSGP KGEKGEQGAK GERGADGTST MGPPGPRGPP
GHVEVLSSSL INITNGSMNF SDIPELMGPP GPDGVPGLPG FPGPRGPKGD TGVPGFPGLK
GEQGEKGEPG AILTGDVPLE MMKGRKGEPG IHGAPGPMGP KGPPGHKGEF GLPGRPGRPG
LNGLKGAKGD RGVTLPGPPG LPGPPGPPGP PGAVVNIKGA VFPIPARPHC KTPVGTAHPG
DPELVTFHGV KGEKGSWGLP GSKGEKGDQG AQGPPGPPVD PAYLRHFLNS LKGENEDASF
RGESSNNLFV SGPPGLPGYP GLVGQKGEAV VGPQGPPGIP GLPGPPGFGR PGVPGPPGPP
GPPGPPAILG AAVALPGPPG PPGQPGLPGS RNLVTALSDM GDMLQKAHLV IEGTFIYLRD
SGEFFIRVRD GWKKLQLGEL IPIPADSPPP PALSSNPYQP QPPLNPILSA NYERPVLHLV
ALNTPVAGDI RADFQCFQQA RAAGLLSTFR AFLSSHLQDL STVVRKAERF GLPIVNLKGQ
VLFNNWDSIF SGDGGQFNTH IPIYSFDGRD VMTDPSWPQK VVWHGSNPHG VRLVDKYCEA
WRTTDMAVTG FASPLSTGKI LDQKAYSCAN RLIVLCIENS FMTDTRK
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