ID   FMOD_HUMAN              Reviewed;         376 AA.
AC   Q06828; Q15331; Q8IV47;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Fibromodulin;
DE            Short=FM;
DE   AltName: Full=Collagen-binding 59 kDa protein;
DE   AltName: Full=Keratan sulfate proteoglycan fibromodulin;
DE            Short=KSPG fibromodulin;
DE   Flags: Precursor;
GN   Name=FMOD; Synonyms=FM, SLRR2E;
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 [GENOMIC DNA].
RX   PubMed=8357838; DOI=10.1016/0167-4781(93)90117-v;
RA   Antonsson P., Heinegaard D., Oldberg A.;
RT   "Structure and deduced amino acid sequence of the human fibromodulin
RT   gene.";
RL   Biochim. Biophys. Acta 1174:204-206(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8093006; DOI=10.1042/bj3020527;
RA   Hildebrand A., Romaris M., Rasmussen L.M., Heinegard D., Twardzik D.R.,
RA   Border W.A., Ruoslahti E.;
RT   "Interaction of the small interstitial proteoglycans biglycan, decorin and
RT   fibromodulin with transforming growth factor beta.";
RL   Biochem. J. 302:527-534(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [7]
RP   SULFATION AT TYR-20; TYR-38; TYR-39; TYR-45; TYR-47; TYR-53 AND TYR-55,
RP   LACK OF SULFATION AT TYR-63 AND TYR-65, PYROGLUTAMATE FORMATION AT GLN-19,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14551184; DOI=10.1074/jbc.m308689200;
RA   Onnerfjord P., Heathfield T.F., Heinegaard D.;
RT   "Identification of tyrosine sulfation in extracellular leucine-rich repeat
RT   proteins using mass spectrometry.";
RL   J. Biol. Chem. 279:26-33(2004).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
CC   -!- FUNCTION: Affects the rate of fibrils formation. May have a primary
CC       role in collagen fibrillogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to type I and type II collagen. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- PTM: Binds keratan sulfate chains. {ECO:0000269|PubMed:14551184}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class II subfamily. {ECO:0000305}.
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DR   EMBL; X72913; CAA51418.1; -; Genomic_DNA.
DR   EMBL; X75546; CAA53233.1; -; mRNA.
DR   EMBL; AK291632; BAF84321.1; -; mRNA.
DR   EMBL; AL359837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91477.1; -; Genomic_DNA.
DR   EMBL; BC035281; AAH35281.1; -; mRNA.
DR   CCDS; CCDS30976.1; -.
DR   PIR; S55275; S55275.
DR   RefSeq; NP_002014.2; NM_002023.4.
DR   PDB; 5MX0; X-ray; 2.21 A; A/B=18-376.
DR   PDBsum; 5MX0; -.
DR   AlphaFoldDB; Q06828; -.
DR   SMR; Q06828; -.
DR   BioGRID; 108618; 48.
DR   IntAct; Q06828; 5.
DR   MINT; Q06828; -.
DR   STRING; 9606.ENSP00000347041; -.
DR   GlyConnect; 1242; 54 N-Linked glycans (3 sites).
DR   GlyCosmos; Q06828; 6 sites, 64 glycans.
DR   GlyGen; Q06828; 7 sites, 62 N-linked glycans (3 sites), 2 O-linked glycans (1 site).
DR   iPTMnet; Q06828; -.
DR   PhosphoSitePlus; Q06828; -.
DR   BioMuta; FMOD; -.
DR   DMDM; 223590208; -.
DR   jPOST; Q06828; -.
DR   MassIVE; Q06828; -.
DR   PaxDb; 9606-ENSP00000347041; -.
DR   PeptideAtlas; Q06828; -.
DR   ProteomicsDB; 58485; -.
DR   Antibodypedia; 34544; 317 antibodies from 28 providers.
DR   DNASU; 2331; -.
DR   Ensembl; ENST00000354955.5; ENSP00000347041.4; ENSG00000122176.12.
DR   GeneID; 2331; -.
DR   KEGG; hsa:2331; -.
DR   MANE-Select; ENST00000354955.5; ENSP00000347041.4; NM_002023.5; NP_002014.2.
DR   UCSC; uc001gzr.5; human.
DR   AGR; HGNC:3774; -.
DR   CTD; 2331; -.
DR   DisGeNET; 2331; -.
DR   GeneCards; FMOD; -.
DR   HGNC; HGNC:3774; FMOD.
DR   HPA; ENSG00000122176; Low tissue specificity.
DR   MIM; 600245; gene.
DR   neXtProt; NX_Q06828; -.
DR   OpenTargets; ENSG00000122176; -.
DR   PharmGKB; PA28190; -.
DR   VEuPathDB; HostDB:ENSG00000122176; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000157007; -.
DR   HOGENOM; CLU_000288_186_4_1; -.
DR   InParanoid; Q06828; -.
DR   OMA; KLLYVRM; -.
DR   OrthoDB; 521898at2759; -.
DR   PhylomeDB; Q06828; -.
DR   TreeFam; TF334562; -.
DR   PathwayCommons; Q06828; -.
DR   Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-HSA-2022857; Keratan sulfate degradation.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-3656225; Defective CHST6 causes MCDC1.
DR   Reactome; R-HSA-3656243; Defective ST3GAL3 causes MCT12 and EIEE15.
DR   Reactome; R-HSA-3656244; Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
DR   SignaLink; Q06828; -.
DR   BioGRID-ORCS; 2331; 5 hits in 1144 CRISPR screens.
DR   ChiTaRS; FMOD; human.
DR   GeneWiki; FMOD_(gene); -.
DR   GenomeRNAi; 2331; -.
DR   Pharos; Q06828; Tbio.
DR   PRO; PR:Q06828; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q06828; Protein.
DR   Bgee; ENSG00000122176; Expressed in calcaneal tendon and 173 other cell types or tissues.
DR   ExpressionAtlas; Q06828; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; TAS:ProtInc.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   PANTHER; PTHR45712; AGAP008170-PA; 1.
DR   PANTHER; PTHR45712:SF4; FIBROMODULIN; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF01462; LRRNT; 1.
DR   SMART; SM00364; LRR_BAC; 5.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 10.
DR   Genevisible; Q06828; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Leucine-rich repeat; Proteoglycan; Pyrrolidone carboxylic acid;
KW   Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..376
FT                   /note="Fibromodulin"
FT                   /id="PRO_0000032739"
FT   DOMAIN          67..105
FT                   /note="LRRNT"
FT   REPEAT          106..127
FT                   /note="LRR 1"
FT   REPEAT          130..151
FT                   /note="LRR 2"
FT   REPEAT          156..176
FT                   /note="LRR 3"
FT   REPEAT          177..198
FT                   /note="LRR 4"
FT   REPEAT          201..222
FT                   /note="LRR 5"
FT   REPEAT          224..245
FT                   /note="LRR 6"
FT   REPEAT          246..266
FT                   /note="LRR 7"
FT   REPEAT          269..289
FT                   /note="LRR 8"
FT   REPEAT          294..315
FT                   /note="LRR 9"
FT   REPEAT          316..335
FT                   /note="LRR 10"
FT   REPEAT          344..365
FT                   /note="LRR 11"
FT   SITE            63
FT                   /note="Not sulfated"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   SITE            65
FT                   /note="Not sulfated"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   MOD_RES         19
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   MOD_RES         20
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   MOD_RES         38
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         39
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         45
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         47
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         53
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   MOD_RES         55
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        334..367
FT                   /evidence="ECO:0000250"
FT   CONFLICT        4
FT                   /note="T -> A (in Ref. 2; CAA53233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="P -> L (in Ref. 2; CAA53233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="N -> D (in Ref. 2; CAA53233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="I -> Y (in Ref. 1; CAA51418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="K -> Q (in Ref. 1; CAA51418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        348
FT                   /note="L -> V (in Ref. 1; CAA51418 and 2; CAA53233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="I -> M (in Ref. 1; CAA51418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="D -> E (in Ref. 1; CAA51418)"
FT                   /evidence="ECO:0000305"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   TURN            122..125
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   TURN            148..153
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          179..182
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   TURN            193..198
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   TURN            216..221
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   TURN            261..266
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   HELIX           282..284
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   TURN            287..290
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          317..319
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   HELIX           330..332
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          338..340
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          347..349
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   HELIX           357..359
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   HELIX           364..366
FT                   /evidence="ECO:0007829|PDB:5MX0"
FT   STRAND          373..375
FT                   /evidence="ECO:0007829|PDB:5MX0"
SQ   SEQUENCE   376 AA;  43179 MW;  DC19D5E6724AB004 CRC64;
     MQWTSLLLLA GLFSLSQAQY EDDPHWWFHY LRSQQSTYYD PYDPYPYETY EPYPYGVDEG
     PAYTYGSPSP PDPRDCPQEC DCPPNFPTAM YCDNRNLKYL PFVPSRMKYV YFQNNQITSI
     QEGVFDNATG LLWIALHGNQ ITSDKVGRKV FSKLRHLERL YLDHNNLTRM PGPLPRSLRE
     LHLDHNQISR VPNNALEGLE NLTALYLQHN EIQEVGSSMR GLRSLILLDL SYNHLRKVPD
     GLPSALEQLY MEHNNVYTVP DSYFRGAPKL LYVRLSHNSL TNNGLASNTF NSSSLLELDL
     SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVV NFSKLQVLRL DGNEIKRSAM
     PADAPLCLRL ASLIEI
//