SUCO_HUMAN
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 03-AUG-2022, entry version 147.
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}.
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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; 60.
DR IntAct; Q9UBS9; 30.
DR STRING; 9606.ENSP00000356696; -.
DR GlyConnect; 1775; 6 N-Linked glycans (5 sites).
DR GlyGen; Q9UBS9; 7 sites, 6 N-linked glycans (5 sites).
DR iPTMnet; Q9UBS9; -.
DR PhosphoSitePlus; Q9UBS9; -.
DR BioMuta; SUCO; -.
DR DMDM; 74761893; -.
DR EPD; Q9UBS9; -.
DR jPOST; Q9UBS9; -.
DR MassIVE; Q9UBS9; -.
DR MaxQB; Q9UBS9; -.
DR PaxDb; Q9UBS9; -.
DR PeptideAtlas; Q9UBS9; -.
DR PRIDE; Q9UBS9; -.
DR ProteomicsDB; 84053; -. [Q9UBS9-1]
DR ProteomicsDB; 84054; -. [Q9UBS9-2]
DR Antibodypedia; 63320; 8 antibodies from 7 providers.
DR DNASU; 51430; -.
DR Ensembl; ENST00000263688.4; ENSP00000263688.3; ENSG00000094975.14. [Q9UBS9-1]
DR Ensembl; ENST00000367723.8; ENSP00000356696.4; ENSG00000094975.14. [Q9UBS9-2]
DR Ensembl; ENST00000608151.5; ENSP00000477484.2; ENSG00000094975.14. [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 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; MNHTVDA; -.
DR PhylomeDB; Q9UBS9; -.
DR TreeFam; TF105817; -.
DR PathwayCommons; Q9UBS9; -.
DR SignaLink; Q9UBS9; -.
DR BioGRID-ORCS; 51430; 108 hits in 1077 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 210 other tissues.
DR ExpressionAtlas; Q9UBS9; baseline and differential.
DR Genevisible; Q9UBS9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR045120; Suco/Slp1-like.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12953; PTHR12953; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51469; SUN; 1.
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
