ID SUCO_HUMAN Reviewed; 1254 AA. AC Q9UBS9; B2RNU4; Q9BQB9; Q9BXQ2; Q9UL04; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 155. DE RecName: Full=SUN domain-containing ossification factor; DE AltName: Full=Membrane protein CH1; DE AltName: Full=Protein osteopotentia homolog; DE AltName: Full=SUN-like protein 1; DE Flags: Precursor; GN Name=SUCO; Synonyms=C1orf9, CH1, OPT, SLP1; 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] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=10673381; DOI=10.1006/bbrc.1999.2016; RA Roesok O., Pedeutour F., Odeberg J., Lundeberg J., Aasheim H.-C.; RT "The C1orf9 gene encodes a putative transmembrane member of a novel protein RT family."; RL Biochem. Biophys. Res. Commun. 267:855-862(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Mammary gland; RA Chen L.-C., Cheung J., Moore D., Ljung B.-M., Kuo W.-L., Collins C., RA Gray J.W., Smith H.S.; RT "Cloning of an overexpressed gene on chromosome 1 in breast cancer defines RT a new gene family."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Rhodes S.; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. 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] (ISOFORM 1). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-244. RX PubMed=11158380; DOI=10.1093/oxfordjournals.molbev.a003795; RA Yu N., Zhao Z., Fu Y.-X., Sambuughin N., Ramsay M., Jenkins T., RA Leskinen E., Patthy L., Jorde L.B., Kuromori T., Li W.-H.; RT "Global patterns of human DNA sequence variation in a 10-kb region on RT chromosome 1."; RL Mol. Biol. Evol. 18:214-222(2001). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP GLYCOSYLATION. RX PubMed=28512129; DOI=10.1074/jbc.m117.794487; RA Larsen I.S.B., Narimatsu Y., Joshi H.J., Yang Z., Harrison O.J., Brasch J., RA Shapiro L., Honig B., Vakhrushev S.Y., Clausen H., Halim A.; RT "Mammalian O-mannosylation of cadherins and plexins is independent of RT protein O-mannosyltransferases 1 and 2."; RL J. Biol. Chem. 292:11586-11598(2017). CC -!- FUNCTION: Required for bone modeling during late embryogenesis. CC Regulates type I collagen synthesis in osteoblasts during their CC postnatal maturation (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UBS9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UBS9-2; Sequence=VSP_027921, VSP_027922, VSP_027923; CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and testis and to a CC lower extent in prostate, ovary, heart, thymus, small intestine and CC spleen. {ECO:0000269|PubMed:10673381}. CC -!- PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by CC POMGNT1. {ECO:0000269|PubMed:28512129}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8C341}. 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; AJ250075; CAB57360.1; -; mRNA. DR EMBL; AF097535; AAF04619.1; -; mRNA. DR EMBL; AL035291; CAA22894.1; -; mRNA. DR EMBL; Z96050; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z94054; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC137125; AAI37126.1; -; mRNA. DR EMBL; CH471067; EAW90931.1; -; Genomic_DNA. DR EMBL; AF310265; AAK28742.1; -; Genomic_DNA. DR EMBL; AF310266; AAK28743.1; -; Genomic_DNA. DR EMBL; AF310267; AAK28744.1; -; Genomic_DNA. DR EMBL; AF310268; AAK28745.1; -; Genomic_DNA. DR EMBL; AF310269; AAK28746.1; -; Genomic_DNA. DR EMBL; AF310270; AAK28747.1; -; Genomic_DNA. DR EMBL; AF310271; AAK28748.1; -; Genomic_DNA. DR EMBL; AF310272; AAK28749.1; -; Genomic_DNA. DR EMBL; AF310273; AAK28750.1; -; Genomic_DNA. DR EMBL; AF310274; AAK28751.1; -; Genomic_DNA. DR EMBL; AF310275; AAK28752.1; -; Genomic_DNA. DR EMBL; AF310276; AAK28753.1; -; Genomic_DNA. DR EMBL; AF310277; AAK28754.1; -; Genomic_DNA. DR EMBL; AF310278; AAK28755.1; -; Genomic_DNA. DR EMBL; AF310279; AAK28756.1; -; Genomic_DNA. DR EMBL; AF310280; AAK28757.1; -; Genomic_DNA. DR EMBL; AF310281; AAK28758.1; -; Genomic_DNA. DR EMBL; AF310282; AAK28759.1; -; Genomic_DNA. DR EMBL; AF310283; AAK28760.1; -; Genomic_DNA. DR EMBL; AF310284; AAK28761.1; -; Genomic_DNA. DR EMBL; AF310285; AAK28762.1; -; Genomic_DNA. DR EMBL; AF310286; AAK28763.1; -; Genomic_DNA. DR EMBL; AF310287; AAK28764.1; -; Genomic_DNA. DR EMBL; AF310288; AAK28765.1; -; Genomic_DNA. DR EMBL; AF310289; AAK28766.1; -; Genomic_DNA. DR EMBL; AF310290; AAK28767.1; -; Genomic_DNA. DR EMBL; AF310291; AAK28768.1; -; Genomic_DNA. DR EMBL; AF310292; AAK28769.1; -; Genomic_DNA. DR EMBL; AF310293; AAK28770.1; -; Genomic_DNA. DR EMBL; AF310294; AAK28771.1; -; Genomic_DNA. DR EMBL; AF310295; AAK28772.1; -; Genomic_DNA. DR EMBL; AF310296; AAK28773.1; -; Genomic_DNA. DR EMBL; AF310297; AAK28774.1; -; Genomic_DNA. DR EMBL; AF310298; AAK28775.1; -; Genomic_DNA. DR EMBL; AF310299; AAK28776.1; -; Genomic_DNA. DR EMBL; AF310300; AAK28777.1; -; Genomic_DNA. DR EMBL; AF310301; AAK28778.1; -; Genomic_DNA. DR EMBL; AF310302; AAK28779.1; -; Genomic_DNA. DR EMBL; AF310303; AAK28780.1; -; Genomic_DNA. DR EMBL; AF310304; AAK28781.1; -; Genomic_DNA. DR EMBL; AF310305; AAK28782.1; -; Genomic_DNA. DR EMBL; AF310306; AAK28783.1; -; Genomic_DNA. DR EMBL; AF310307; AAK28784.1; -; Genomic_DNA. DR EMBL; AF310308; AAK28785.1; -; Genomic_DNA. DR EMBL; AF310309; AAK28786.1; -; Genomic_DNA. DR EMBL; AF310310; AAK28787.1; -; Genomic_DNA. DR EMBL; AF310311; AAK28788.1; -; Genomic_DNA. DR EMBL; AF310312; AAK28789.1; -; Genomic_DNA. DR EMBL; AF310313; AAK28790.1; -; Genomic_DNA. DR EMBL; AF310314; AAK28791.1; -; Genomic_DNA. DR EMBL; AF310315; AAK28792.1; -; Genomic_DNA. DR EMBL; AF310316; AAK28793.1; -; Genomic_DNA. DR EMBL; AF310317; AAK28794.1; -; Genomic_DNA. DR EMBL; AF310318; AAK28795.1; -; Genomic_DNA. DR EMBL; AF310319; AAK28796.1; -; Genomic_DNA. DR EMBL; AF310320; AAK28797.1; -; Genomic_DNA. DR EMBL; AF310321; AAK28798.1; -; Genomic_DNA. DR EMBL; AF310322; AAK28799.1; -; Genomic_DNA. DR EMBL; AF310323; AAK28800.1; -; Genomic_DNA. DR EMBL; AF310324; AAK28801.1; -; Genomic_DNA. DR EMBL; AF310325; AAK28802.1; -; Genomic_DNA. DR CCDS; CCDS1303.1; -. [Q9UBS9-1] DR CCDS; CCDS65726.1; -. [Q9UBS9-2] DR PIR; JC7185; JC7185. DR RefSeq; NP_001269679.1; NM_001282750.1. DR RefSeq; NP_001269680.1; NM_001282751.1. DR RefSeq; NP_055098.1; NM_014283.4. [Q9UBS9-1] DR RefSeq; NP_057311.3; NM_016227.3. [Q9UBS9-2] DR AlphaFoldDB; Q9UBS9; -. DR SMR; Q9UBS9; -. DR BioGRID; 119536; 63. DR IntAct; Q9UBS9; 30. DR STRING; 9606.ENSP00000356696; -. DR GlyConnect; 1775; 6 N-Linked glycans (5 sites). DR GlyCosmos; Q9UBS9; 7 sites, 6 glycans. DR GlyGen; Q9UBS9; 12 sites, 6 N-linked glycans (5 sites), 2 O-linked glycans (5 sites). DR iPTMnet; Q9UBS9; -. DR PhosphoSitePlus; Q9UBS9; -. DR SwissPalm; Q9UBS9; -. DR BioMuta; SUCO; -. DR DMDM; 74761893; -. DR EPD; Q9UBS9; -. DR jPOST; Q9UBS9; -. DR MassIVE; Q9UBS9; -. DR MaxQB; Q9UBS9; -. DR PaxDb; 9606-ENSP00000356696; -. DR PeptideAtlas; Q9UBS9; -. DR ProteomicsDB; 84053; -. [Q9UBS9-1] DR ProteomicsDB; 84054; -. [Q9UBS9-2] DR Pumba; Q9UBS9; -. DR Antibodypedia; 63320; 8 antibodies from 7 providers. DR DNASU; 51430; -. DR Ensembl; ENST00000263688.4; ENSP00000263688.3; ENSG00000094975.15. [Q9UBS9-1] DR Ensembl; ENST00000367723.8; ENSP00000356696.4; ENSG00000094975.15. [Q9UBS9-2] DR GeneID; 51430; -. DR KEGG; hsa:51430; -. DR MANE-Select; ENST00000263688.4; ENSP00000263688.3; NM_014283.5; NP_055098.1. DR UCSC; uc001giq.6; human. [Q9UBS9-1] DR AGR; HGNC:1240; -. DR CTD; 51430; -. DR DisGeNET; 51430; -. DR GeneCards; SUCO; -. DR HGNC; HGNC:1240; SUCO. DR HPA; ENSG00000094975; Tissue enhanced (bone). DR MIM; 619434; gene. DR neXtProt; NX_Q9UBS9; -. DR OpenTargets; ENSG00000094975; -. DR PharmGKB; PA25621; -. DR VEuPathDB; HostDB:ENSG00000094975; -. DR eggNOG; KOG1396; Eukaryota. DR GeneTree; ENSGT00390000013502; -. DR HOGENOM; CLU_006401_0_0_1; -. DR InParanoid; Q9UBS9; -. DR OMA; MASTEPH; -. DR OrthoDB; 103878at2759; -. DR PhylomeDB; Q9UBS9; -. DR TreeFam; TF105817; -. DR PathwayCommons; Q9UBS9; -. DR SignaLink; Q9UBS9; -. DR BioGRID-ORCS; 51430; 118 hits in 1157 CRISPR screens. DR ChiTaRS; SUCO; human. DR GenomeRNAi; 51430; -. DR Pharos; Q9UBS9; Tdark. DR PRO; PR:Q9UBS9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UBS9; Protein. DR Bgee; ENSG00000094975; Expressed in corpus epididymis and 212 other cell types or tissues. DR ExpressionAtlas; Q9UBS9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:UniProtKB. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB. DR GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR045120; Suco/Slp1-like. DR InterPro; IPR012919; SUN_dom. DR PANTHER; PTHR12953; MEMBRANE PROTEIN CH1 RELATED; 1. DR PANTHER; PTHR12953:SF0; SUN DOMAIN-CONTAINING OSSIFICATION FACTOR; 1. DR Pfam; PF07738; Sad1_UNC; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR PROSITE; PS51469; SUN; 1. DR Genevisible; Q9UBS9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Developmental protein; KW Endoplasmic reticulum; Glycoprotein; Membrane; Osteogenesis; KW Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..1254 FT /note="SUN domain-containing ossification factor" FT /id="PRO_5000065707" FT TRANSMEM 1011..1031 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 284..453 FT /note="SUN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802" FT REGION 58..88 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 118..270 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 282..304 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 530..553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 583..605 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 759..788 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1152..1172 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 909..1009 FT /evidence="ECO:0000255" FT COMPBIAS 123..144 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 229..252 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 288..304 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 585..601 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1081 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 202 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 236 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 524 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 928 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 955 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1 FT /note="M -> MRGFLARPFLSTNQHLAQWGSPLPQGKGLVQLPSQHTRHSRPFHELC FT SKEENSATVPKLISLVVSSETIDFSNKTMDSRRDWEREKRILEGKLQLPKALARTQRAR FT DEGRAWTSRWLQRRRSPESCEAPLSAPLWGPQRGLPGREPLRSRSASAIALRTIGHILA FT LLLRLLHLGLGSGGCREDVPPSGRGKKEEKM (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_027921" FT VAR_SEQ 60..96 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_027922" FT VAR_SEQ 421..427 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_027923" FT CONFLICT 452 FT /note="S -> N (in Ref. 2; AAF04619)" FT /evidence="ECO:0000305" FT CONFLICT 811 FT /note="V -> M (in Ref. 2; AAF04619)" FT /evidence="ECO:0000305" SQ SEQUENCE 1254 AA; 139430 MW; 4EBA1ABCC27DAAB1 CRC64; MKKHRRALAL VSCLFLCSLV WLPSWRVCCK ESSSASASSY YSQDDNCALE NEDVQFQKKD EREGPINAES LGKSGSNLPI SPKEHKLKDD SIVDVQNTES KKLSPPVVET LPTVDLHEES SNAVVDSETV ENISSSSTSE ITPISKLDEI EKSGTIPIAK PSETEQSETD CDVGEALDAS APIEQPSFVS PPDSLVGQHI ENVSSSHGKG KITKSEFESK VSASEQGGGD PKSALNASDN LKNESSDYTK PGDIDPTSVA SPKDPEDIPT FDEWKKKVME VEKEKSQSMH ASSNGGSHAT KKVQKNRNNY ASVECGAKIL AANPEAKSTS AILIENMDLY MLNPCSTKIW FVIELCEPIQ VKQLDIANYE LFSSTPKDFL VSISDRYPTN KWIKLGTFHG RDERNVQSFP LDEQMYAKYV KMFIKYIKVE LLSHFGSEHF CPLSLIRVFG TSMVEEYEEI ADSQYHSERQ ELFDEDYDYP LDYNTGEDKS SKNLLGSATN AILNMVNIAA NILGAKTEDL TEGNKSISEN ATATAAPKMP ESTPVSTPVP SPEYVTTEVH THDMEPSTPD TPKESPIVQL VQEEEEEASP STVTLLGSGE QEDESSPWFE SETQIFCSEL TTICCISSFS EYIYKWCSVR VALYRQRSRT ALSKGKDYLV LAQPPLLLPA ESVDVSVLQP LSGELENTNI EREAETVVLG DLSSSMHQDD LVNHTVDAVE LEPSHSQTLS QSLLLDITPE INPLPKIEVS ESVEYEAGHI PSPVIPQESS VEIDNETEQK SESFSSIEKP SITYETNKVN ELMDNIIKED VNSMQIFTKL SETIVPPINT ATVPDNEDGE AKMNIADTAK QTLISVVDSS SLPEVKEEEQ SPEDALLRGL QRTATDFYAE LQNSTDLGYA NGNLVHGSNQ KESVFMRLNN RIKALEVNMS LSGRYLEELS QRYRKQMEEM QKAFNKTIVK LQNTSRIAEE QDQRQTEAIQ LLQAQLTNMT QLVSNLSATV AELKREVSDR QSYLVISLVL CVVLGLMLCM QRCRNTSQFD GDYISKLPKS NQYPSPKRCF SSYDDMNLKR RTSFPLMRSK SLQLTGKEVD PNDLYIVEPL KFSPEKKKKR CKYKIEKIET IKPEEPLHPI ANGDIKGRKP FTNQRDFSNM GEVYHSSYKG PPSEGSSETS SQSEESYFCG ISACTSLCNG QSQKTKTEKR ALKRRRSKVQ DQGKLIKTLI QTKSGSLPSL HDIIKGNKEI TVGTFGVTAV SGHI //