OS9_YEAST
ID OS9_YEAST Reviewed; 542 AA.
AC Q99220; D6VS43; Q04313;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein OS-9 homolog;
DE Flags: Precursor;
GN Name=YOS9; OrderedLocusNames=YDR057W; ORFNames=D4222;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8789263;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u;
RA Brandt P., Ramlow S., Otto B., Bloecker H.;
RT "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT Saccharomyces cerevisiae chromosome IV.";
RL Yeast 12:85-90(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH GAS1 AND MKC7.
RX PubMed=12077121; DOI=10.1074/jbc.m201044200;
RA Friedmann E., Salzberg Y., Weinberger A., Shaltiel S., Gerst J.E.;
RT "YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is
RT involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored
RT proteins.";
RL J. Biol. Chem. 277:35274-35281(2002).
RN [5]
RP FUNCTION.
RX PubMed=15556621; DOI=10.1016/j.febslet.2004.10.039;
RA Buschhorn B.A., Kostova Z., Medicherla B., Wolf D.H.;
RT "A genome-wide screen identifies Yos9p as essential for ER-associated
RT degradation of glycoproteins.";
RL FEBS Lett. 577:422-426(2004).
RN [6]
RP FUNCTION, DOMAIN, INTERACTION WITH MISFOLDED PRC1, AND MUTAGENESIS OF
RP ARG-200; GLU-223 AND TYR-229.
RX PubMed=16168370; DOI=10.1016/j.molcel.2005.07.027;
RA Bhamidipati A., Denic V., Quan E.M., Weissman J.S.;
RT "Exploration of the topological requirements of ERAD identifies Yos9p as a
RT lectin sensor of misfolded glycoproteins in the ER lumen.";
RL Mol. Cell 19:741-751(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MISFOLDED PRC1.
RX PubMed=16168371; DOI=10.1016/j.molcel.2005.08.010;
RA Kim W., Spear E.D., Ng D.T.W.;
RT "Yos9p detects and targets misfolded glycoproteins for ER-associated
RT degradation.";
RL Mol. Cell 19:753-764(2005).
RN [8]
RP FUNCTION, DOMAIN, INTERACTION WITH MISFOLDED PRC1, AND MUTAGENESIS OF
RP TYR-127; GLN-137; HIS-139; ARG-200; GLU-223 AND TYR-229.
RX PubMed=16168372; DOI=10.1016/j.molcel.2005.08.015;
RA Szathmary R., Bielmann R., Nita-Lazar M., Burda P., Jakob C.A.;
RT "Yos9 protein is essential for degradation of misfolded glycoproteins and
RT may function as lectin in ERAD.";
RL Mol. Cell 19:765-775(2005).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE HRD1 COMPLEX, INTERACTION WITH KAR2 AND
RP EMP47, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-200.
RX PubMed=16873065; DOI=10.1016/j.cell.2006.05.045;
RA Denic V., Quan E.M., Weissman J.S.;
RT "A luminal surveillance complex that selects misfolded glycoproteins for
RT ER-associated degradation.";
RL Cell 126:349-359(2006).
RN [10]
RP IDENTIFICATION IN THE HRD1 COMPLEX.
RX PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
RA Carvalho P., Goder V., Rapoport T.A.;
RT "Distinct ubiquitin-ligase complexes define convergent pathways for the
RT degradation of ER proteins.";
RL Cell 126:361-373(2006).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=21074049; DOI=10.1016/j.cell.2010.10.028;
RA Carvalho P., Stanley A.M., Rapoport T.A.;
RT "Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-
RT ligase Hrd1p.";
RL Cell 143:579-591(2010).
RN [12] {ECO:0007744|PDB:2YMA}
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 266-424, SUBUNIT, INTERACTION
RP WITH HRD3, AND MUTAGENESIS OF ASN-380 AND LEU-393.
RX PubMed=22262864; DOI=10.1074/jbc.m111.317644;
RA Hanna J., Schuetz A., Zimmermann F., Behlke J., Sommer T., Heinemann U.;
RT "Structural and biochemical basis of Yos9 protein dimerization and possible
RT contribution to self-association of 3-hydroxy-3-methylglutaryl-coenzyme A
RT reductase degradation ubiquitin-ligase complex.";
RL J. Biol. Chem. 287:8633-8640(2012).
RN [13] {ECO:0007744|PDB:6VK3}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) IN COMPLEX WITH HRD3,
RP FUNCTION, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=32327568; DOI=10.1126/science.aaz2449;
RA Wu X., Siggel M., Ovchinnikov S., Mi W., Svetlov V., Nudler E., Liao M.,
RA Hummer G., Rapoport T.A.;
RT "Structural basis of ER-associated protein degradation mediated by the Hrd1
RT ubiquitin ligase complex.";
RL Science 368:0-0(2020).
CC -!- FUNCTION: Lectin involved in the quality control of the secretory
CC pathway. As a member of the endoplasmic reticulum-associated
CC degradation lumenal (ERAD-L) surveillance system, targets misfolded
CC endoplasmic reticulum lumenal glycoproteins for degradation. The
CC recognition of targets is N-glycan specific. Functions in recruiting
CC misfolded protein substrates in conjunction with HRD3
CC (PubMed:32327568). {ECO:0000269|PubMed:12077121,
CC ECO:0000269|PubMed:15556621, ECO:0000269|PubMed:16168370,
CC ECO:0000269|PubMed:16168371, ECO:0000269|PubMed:16168372,
CC ECO:0000269|PubMed:16873065, ECO:0000269|PubMed:32327568}.
CC -!- SUBUNIT: Homodimer (PubMed:22262864). Component of the HRD1 ubiquitin
CC ligase complex which contains the E3 ligase HRD1, its cofactors HRD3,
CC USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding
CC protein UBX2 (PubMed:16873065, PubMed:16873066). Within the complex,
CC interacts (via N-terminus) with HRD3 (PubMed:22262864). In ERAD-L, HRD3
CC and YOS9 jointly bind misfolded glycoproteins in the endoplasmic
CC reticulum (ER) lumen (PubMed:32327568). Movement of ERAD-L substrates
CC through the ER membrane is facilitated by HRD1 and DER1 which have
CC lateral gates facing each other and which distort the membrane region
CC between the lateral gates, making it much thinner than a normal
CC phospholipid bilayer (PubMed:32327568). Substrates insert into the
CC membrane as a hairpin loop with one strand interacting with DER1 and
CC the other with HRD1 (PubMed:32327568). The HRD1 complex interacts with
CC the heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by
CC UBX2 via its interaction with CDC48 and which moves ubiquitinated
CC substrates to the cytosol for targeting to the proteasome
CC (PubMed:16873065, PubMed:16873066). Interacts with KAR2 and EMP47
CC (PubMed:16873065). Interacts with misfolded ER lumenal proteins like
CC PCR1 (PubMed:16168370, PubMed:16168371, PubMed:16168372). Interacts
CC with the GPI-anchored proteins GAS1 and MKC7 (PubMed:12077121).
CC {ECO:0000269|PubMed:12077121, ECO:0000269|PubMed:16168370,
CC ECO:0000269|PubMed:16168371, ECO:0000269|PubMed:16168372,
CC ECO:0000269|PubMed:16873065, ECO:0000269|PubMed:16873066,
CC ECO:0000269|PubMed:22262864, ECO:0000269|PubMed:32327568}.
CC -!- INTERACTION:
CC Q99220; Q08109: HRD1; NbExp=6; IntAct=EBI-34938, EBI-37613;
CC Q99220; Q05787: HRD3; NbExp=8; IntAct=EBI-34938, EBI-31647;
CC Q99220; P16474: KAR2; NbExp=2; IntAct=EBI-34938, EBI-7876;
CC Q99220; P00729: PRC1; NbExp=2; IntAct=EBI-34938, EBI-4153;
CC Q99220; Q04228: UBX2; NbExp=3; IntAct=EBI-34938, EBI-27730;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12077121,
CC ECO:0000269|PubMed:16168371}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12077121, ECO:0000269|PubMed:16168371}; Lumenal
CC side {ECO:0000269|PubMed:12077121, ECO:0000269|PubMed:16168371}.
CC -!- DOMAIN: The MRH (mannose 6-phosphate receptor homology) domain is
CC required for the ERAD-L activity. {ECO:0000269|PubMed:16168370,
CC ECO:0000269|PubMed:16168372}.
CC -!- DISRUPTION PHENOTYPE: Interaction of substrate with HRD1 is reduced; in
CC YOS9 and USA1 double mutants this interaction is completely abolished.
CC Interaction of substrate (either glycosylated or non-glycosylated) with
CC HRD3 is not affected. {ECO:0000269|PubMed:16873065,
CC ECO:0000269|PubMed:21074049}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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DR EMBL; X84162; CAA58973.1; -; Genomic_DNA.
DR EMBL; Z74353; CAA98875.1; -; Genomic_DNA.
DR EMBL; Z49209; CAA89086.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11903.1; -; Genomic_DNA.
DR PIR; S58837; S58837.
DR RefSeq; NP_010342.3; NM_001180365.3.
DR PDB; 2YMA; X-ray; 2.54 A; A/B=266-424.
DR PDB; 6VK3; EM; 3.70 A; B=1-542.
DR PDBsum; 2YMA; -.
DR PDBsum; 6VK3; -.
DR AlphaFoldDB; Q99220; -.
DR SMR; Q99220; -.
DR BioGRID; 32110; 129.
DR ComplexPortal; CPX-1280; Luminal surveillance complex.
DR ComplexPortal; CPX-3070; HRD1 ubiquitin ligase complex.
DR IntAct; Q99220; 11.
DR MINT; Q99220; -.
DR STRING; 4932.YDR057W; -.
DR TCDB; 3.A.16.1.2; the endoplasmic reticular retrotranslocon (er-rt) family.
DR TCDB; 8.A.67.1.5; the os-9 quality control (erad) protein (os-9) family.
DR iPTMnet; Q99220; -.
DR MaxQB; Q99220; -.
DR PaxDb; Q99220; -.
DR PRIDE; Q99220; -.
DR EnsemblFungi; YDR057W_mRNA; YDR057W; YDR057W.
DR GeneID; 851627; -.
DR KEGG; sce:YDR057W; -.
DR SGD; S000002464; YOS9.
DR VEuPathDB; FungiDB:YDR057W; -.
DR eggNOG; KOG3394; Eukaryota.
DR HOGENOM; CLU_502681_0_0_1; -.
DR InParanoid; Q99220; -.
DR OMA; PHEMEVI; -.
DR BioCyc; YEAST:G3O-29666-MON; -.
DR Reactome; R-SCE-5358346; Hedgehog ligand biogenesis.
DR PRO; PR:Q99220; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q99220; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; IPI:ComplexPortal.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IPI:SGD.
DR GO; GO:0034099; C:luminal surveillance complex; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:SGD.
DR GO; GO:0002235; P:detection of unfolded protein; IC:ComplexPortal.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; IMP:SGD.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR045149; OS-9-like.
DR InterPro; IPR012913; OS9-like_dom.
DR InterPro; IPR041039; Yos9_DD.
DR PANTHER; PTHR15414; PTHR15414; 1.
DR Pfam; PF07915; PRKCSH; 1.
DR Pfam; PF17880; Yos9_DD; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..542
FT /note="Protein OS-9 homolog"
FT /id="PRO_0000042758"
FT DOMAIN 115..241
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 497..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 539..542
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 511..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 137
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 194
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 200
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 223
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 229
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..258
FT /evidence="ECO:0000269|PubMed:32327568,
FT ECO:0007744|PDB:6VK3"
FT DISULFID 117..130
FT /evidence="ECO:0000269|PubMed:32327568,
FT ECO:0007744|PDB:6VK3"
FT DISULFID 193..227
FT /evidence="ECO:0000269|PubMed:32327568,
FT ECO:0007744|PDB:6VK3"
FT DISULFID 208..239
FT /evidence="ECO:0000269|PubMed:32327568,
FT ECO:0007744|PDB:6VK3"
FT MUTAGEN 127
FT /note="Y->A: Decrease of ER lumenal misfolded protein
FT degradation."
FT /evidence="ECO:0000269|PubMed:16168372"
FT MUTAGEN 137
FT /note="Q->E: Decrease of ER lumenal misfolded protein
FT degradation."
FT /evidence="ECO:0000269|PubMed:16168372"
FT MUTAGEN 139
FT /note="H->A: Decrease of ER lumenal misfolded protein
FT degradation."
FT /evidence="ECO:0000269|PubMed:16168372"
FT MUTAGEN 200
FT /note="R->A: Decrease of ER lumenal misfolded protein
FT degradation. No effect on interaction with CDC48, HRD3,
FT KAR2, UBX2, HRD1 or EMP47."
FT /evidence="ECO:0000269|PubMed:16168370,
FT ECO:0000269|PubMed:16168372, ECO:0000269|PubMed:16873065"
FT MUTAGEN 223
FT /note="E->N: Decrease of ER lumenal misfolded protein
FT degradation."
FT /evidence="ECO:0000269|PubMed:16168370,
FT ECO:0000269|PubMed:16168372"
FT MUTAGEN 229
FT /note="Y->A,F: Decrease of ER lumenal misfolded protein
FT degradation."
FT /evidence="ECO:0000269|PubMed:16168370,
FT ECO:0000269|PubMed:16168372"
FT MUTAGEN 380
FT /note="N->A: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:22262864"
FT MUTAGEN 393
FT /note="L->A: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:22262864"
FT CONFLICT 25
FT /note="P -> L (in Ref. 2; CAA89086)"
FT /evidence="ECO:0000305"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:2YMA"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:2YMA"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2YMA"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:2YMA"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2YMA"
FT HELIX 315..330
FT /evidence="ECO:0007829|PDB:2YMA"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:2YMA"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:2YMA"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2YMA"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:2YMA"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:2YMA"
SQ SEQUENCE 542 AA; 61258 MW; BF353A0278703BE8 CRC64;
MQAKIIYALS AISALIPLGS SLLAPIEDPI VSNKYLISYI DEDDWSDRIL QNQSVMNSGY
IVNMGDDLEC FIQNASTQLN DVLEDSNEHS NSEKTALLTK TLNQGVKTIF DKLNERCIFY
QAGFWIYEYC PGIEFVQFHG RVNTKTGEIV NRDESLVYRL GKPKANVEER EFELLYDDVG
YYISEIIGSG DICDVTGAER MVEIQYVCGG SNSGPSTIQW VRETKICVYE AQVTIPELCN
LELLAKNEDQ KNASPILCRM PAKSKIGSNS IDLITKYEPI FLGSGIYFLR PFNTDERDKL
MVTDNAMSNW DEITETYYQK FGNAINKMLS LRLVSLPNGH ILQPGDSCVW LAEVVDMKDR
FQTTLSLNIL NSQRAEIFFN KTFTFNEDNG NFLSYKIGDH GESTELGQIT HSNKADINTA
EIRSDEYLIN TDNELFLRIS KEIAEVKELL NEIVSPHEME VIFENMRNQP NNDFELALMN
KLKSSLNDDN KVEQINNARM DDDESTSHTT RDIGEAGSQT TGNTESEVTN VAAGVFIEHD
EL
