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   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.
DR   Genevisible; O35206; MM.
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
//