NSF1C_RAT
ID NSF1C_RAT Reviewed; 370 AA.
AC O35987;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=NSFL1 cofactor p47;
DE AltName: Full=XY body-associated protein XY40;
DE AltName: Full=p97 cofactor p47;
GN Name=Nsfl1c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 200-209; 283-292 AND
RP 323-328, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Spermatocyte;
RX PubMed=9297509; DOI=10.1007/s004120050252;
RA Alsheimer M., Imamichi Y., Heid H., Benavente R.;
RT "Molecular characterization and expression pattern of XY body-associated
RT protein XY40 of the rat.";
RL Chromosoma 106:308-314(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-22; 94-101; 157-172;
RP 189-214; 260-282; 323-346 AND 357-368, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, INTERACTION WITH VCP, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9214505; DOI=10.1038/40411;
RA Kondo H., Rabouille C., Newman R., Levine T.P., Pappin D., Freemont P.,
RA Warren G.;
RT "p47 is a cofactor for p97-mediated membrane fusion.";
RL Nature 388:75-78(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP PROTEIN SEQUENCE OF 200-214 AND 283-301, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=1495983; DOI=10.1073/pnas.89.15.6938;
RA Smith A., Benavente R.;
RT "Meiosis-specific protein selectively associated with sex chromosomes of
RT rat pachytene spermatocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6938-6942(1992).
RN [6]
RP INTERACTION WITH STX5A.
RX PubMed=9506515; DOI=10.1016/s0092-8674(00)81128-9;
RA Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G.;
RT "Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly
RT pathways of Golgi cisternae from mitotic Golgi fragments in vitro.";
RL Cell 92:603-610(1998).
RN [7]
RP FUNCTION.
RX PubMed=9824302; DOI=10.1016/s0014-5793(98)01232-0;
RA Meyer H.H., Kondo H., Warren G.;
RT "The p47 co-factor regulates the ATPase activity of the membrane fusion
RT protein, p97.";
RL FEBS Lett. 437:255-257(1998).
RN [8]
RP INTERACTION WITH VCP.
RX PubMed=10811609; DOI=10.1093/emboj/19.10.2181;
RA Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.;
RT "A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
RT ubiquitin and nuclear transport pathways.";
RL EMBO J. 19:2181-2192(2000).
RN [9]
RP FUNCTION.
RX PubMed=10930451; DOI=10.1091/mbc.11.8.2529;
RA Roy L., Bergeron J.J.M., Lavoie C., Hendriks R., Gushue J., Fazel A.,
RA Pelletier A., Morre D.J., Subramaniam V.N., Hong W., Paiement J.;
RT "Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic
RT reticulum.";
RL Mol. Biol. Cell 11:2529-2542(2000).
RN [10]
RP INTERACTION WITH MEMBRANES.
RX PubMed=12146947; DOI=10.1021/bi0259195;
RA Pecheur E.-I., Martin I., Maier O., Bakowsky U., Ruysschaert J.-M.,
RA Hoekstra D.;
RT "Phospholipid species act as modulators in p97/p47-mediated fusion of Golgi
RT membranes.";
RL Biochemistry 41:9813-9823(2002).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF PHE-41.
RX PubMed=12411482; DOI=10.1093/emboj/cdf579;
RA Meyer H.H., Wang Y., Warren G.;
RT "Direct binding of ubiquitin conjugates by the mammalian p97 adaptor
RT complexes, p47 and Ufd1-Npl4.";
RL EMBO J. 21:5645-5652(2002).
RN [12]
RP INTERACTION WITH VCIP135.
RX PubMed=12473691; DOI=10.1083/jcb.200208112;
RA Uchiyama K., Jokitalo E., Kano F., Murata M., Zhang X., Canas B.,
RA Newman R., Rabouille C., Pappin D., Freemont P., Kondo H.;
RT "VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is
RT required for Golgi and ER assembly in vivo.";
RL J. Cell Biol. 159:855-866(2002).
RN [13]
RP PHOSPHORYLATION AT SER-140, MUTAGENESIS OF THR-57; LYS-112; SER-114;
RP SER-140; ARG-173 AND SER-272, AND SUBCELLULAR LOCATION.
RX PubMed=12810701; DOI=10.1083/jcb.200303048;
RA Uchiyama K., Jokitalo E., Lindman M., Jackman M., Kano F., Murata M.,
RA Zhang X., Kondo H.;
RT "The localization and phosphorylation of p47 are important for Golgi
RT disassembly-assembly during the cell cycle.";
RL J. Cell Biol. 161:1067-1079(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=23649807; DOI=10.1083/jcb.201209107;
RA Kress E., Schwager F., Holtackers R., Seiler J., Prodon F., Zanin E.,
RA Eiteneuer A., Toya M., Sugimoto A., Meyer H., Meraldi P., Gotta M.;
RT "The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the
RT centrosomal recruitment of Aurora A.";
RL J. Cell Biol. 201:559-575(2013).
RN [17]
RP STRUCTURE BY NMR OF 282-370, AND INTERACTION WITH VCP.
RX PubMed=11478859; DOI=10.1006/jmbi.2001.4864;
RA Yuan X., Shaw A., Zhang X., Kondo H., Lally J., Freemont P.S., Matthews S.;
RT "Solution structure and interaction surface of the C-terminal domain from
RT p47: a major p97-cofactor involved in SNARE disassembly.";
RL J. Mol. Biol. 311:255-263(2001).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 244-370, INTERACTION WITH VCP, AND
RP MUTAGENESIS OF ARG-301; 342-THR--ASN-345; PHE-343 AND ASN-345.
RX PubMed=14988733; DOI=10.1038/sj.emboj.7600139;
RA Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S.;
RT "Structural basis of the interaction between the AAA ATPase p97/VCP and its
RT adaptor protein p47.";
RL EMBO J. 23:1030-1039(2004).
RN [19]
RP STRUCTURE BY NMR OF 1-46 IN COMPLEX WITH UBIQUITIN, STRUCTURE BY NMR OF
RP 171-246, AND INTERACTION WITH VCP.
RX PubMed=15029246; DOI=10.1038/sj.emboj.7600152;
RA Yuan X., Simpson P., McKeown C., Kondo H., Uchiyama K., Wallis R.,
RA Dreveny I., Keetch C., Zhang X., Robinson C., Freemont P., Matthews S.;
RT "Structure, dynamics and interactions of p47, a major adaptor of the AAA
RT ATPase, p97.";
RL EMBO J. 23:1463-1473(2004).
CC -!- FUNCTION: Reduces the ATPase activity of VCP (PubMed:9824302,
CC PubMed:9214505). Necessary for the fragmentation of Golgi stacks during
CC mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis
CC (PubMed:12411482). May play a role in VCP-mediated formation of
CC transitional endoplasmic reticulum (tER) (PubMed:10930451). Inhibits
CC the activity of CTSL (in vitro) (By similarity). Together with
CC UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A
CC during mitotic progression by promoting AURKA removal from centrosomes
CC in prophase (By similarity). Also, regulates spindle orientation during
CC mitosis (By similarity). {ECO:0000250|UniProtKB:Q9UNZ2,
CC ECO:0000269|PubMed:10930451, ECO:0000269|PubMed:12411482,
CC ECO:0000269|PubMed:9214505, ECO:0000269|PubMed:9824302}.
CC -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and VCP.
CC NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer.
CC The complex binds to membranes enriched in phosphatidylethanolamine-
CC containing lipids and promotes Golgi membrane fusion. Interaction with
CC VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP.
CC Binds ubiquitin and mono-ubiquitinated proteins via its N-terminal UBA-
CC like domain when bound to VCP. {ECO:0000269|PubMed:10811609,
CC ECO:0000269|PubMed:11478859, ECO:0000269|PubMed:12146947,
CC ECO:0000269|PubMed:12473691, ECO:0000269|PubMed:14988733,
CC ECO:0000269|PubMed:15029246, ECO:0000269|PubMed:9214505,
CC ECO:0000269|PubMed:9506515}.
CC -!- INTERACTION:
CC O35987; P46462: Vcp; NbExp=12; IntAct=EBI-1993760, EBI-399011;
CC O35987; Q01853: Vcp; Xeno; NbExp=8; IntAct=EBI-1993760, EBI-80597;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12810701}. Golgi
CC apparatus, Golgi stack {ECO:0000269|PubMed:12810701,
CC ECO:0000269|PubMed:9214505}. Chromosome {ECO:0000269|PubMed:1495983}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:23649807}. Note=Predominantly nuclear in interphase
CC cells (PubMed:12810701). Bound to the axial elements of sex chromosomes
CC in pachytene spermatocytes (PubMed:1495983). A small proportion of the
CC protein is cytoplasmic, associated with Golgi stacks (PubMed:12810701).
CC Localizes to centrosome during mitotic prophase and metaphase
CC (PubMed:23649807). {ECO:0000269|PubMed:12810701,
CC ECO:0000269|PubMed:1495983, ECO:0000269|PubMed:23649807}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung,
CC liver, muscle, kidney and testis. {ECO:0000269|PubMed:1495983,
CC ECO:0000269|PubMed:9214505, ECO:0000269|PubMed:9297509}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in pachytene spermatocytes during
CC spermatogenesis.
CC -!- PTM: Phosphorylated during mitosis. Phosphorylation inhibits
CC interaction with Golgi membranes and is required for the fragmentation
CC of the Golgi stacks during mitosis. {ECO:0000269|PubMed:12810701}.
CC -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
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DR EMBL; Y10769; CAA71742.1; -; mRNA.
DR EMBL; AB002086; BAA21659.1; -; mRNA.
DR EMBL; BC072464; AAH72464.1; -; mRNA.
DR RefSeq; NP_114187.1; NM_031981.2.
DR PDB; 1I42; NMR; -; A=282-370.
DR PDB; 1JRU; NMR; -; A=282-370.
DR PDB; 1S3S; X-ray; 2.90 A; G/H/I=244-370.
DR PDB; 1V92; NMR; -; A=1-46.
DR PDB; 1VAZ; NMR; -; A=171-246.
DR PDB; 7R7S; EM; 4.23 A; I/J=1-370.
DR PDB; 7R7T; EM; 4.50 A; I=1-370.
DR PDBsum; 1I42; -.
DR PDBsum; 1JRU; -.
DR PDBsum; 1S3S; -.
DR PDBsum; 1V92; -.
DR PDBsum; 1VAZ; -.
DR PDBsum; 7R7S; -.
DR PDBsum; 7R7T; -.
DR AlphaFoldDB; O35987; -.
DR BMRB; O35987; -.
DR SMR; O35987; -.
DR BioGRID; 249844; 4.
DR ComplexPortal; CPX-263; Nsfl1c-Vcp complex.
DR CORUM; O35987; -.
DR IntAct; O35987; 18.
DR MINT; O35987; -.
DR STRING; 10116.ENSRNOP00000011654; -.
DR iPTMnet; O35987; -.
DR PhosphoSitePlus; O35987; -.
DR jPOST; O35987; -.
DR PaxDb; O35987; -.
DR PRIDE; O35987; -.
DR GeneID; 83809; -.
DR KEGG; rno:83809; -.
DR UCSC; RGD:619952; rat.
DR CTD; 55968; -.
DR RGD; 619952; Nsfl1c.
DR VEuPathDB; HostDB:ENSRNOG00000008604; -.
DR eggNOG; KOG2086; Eukaryota.
DR InParanoid; O35987; -.
DR OMA; EHQAFYA; -.
DR OrthoDB; 1175850at2759; -.
DR PhylomeDB; O35987; -.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR EvolutionaryTrace; O35987; -.
DR PRO; PR:O35987; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000008604; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; O35987; baseline and differential.
DR Genevisible; O35987; RN.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
DR GO; GO:1990730; C:VCP-NSFL1C complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; IDA:RGD.
DR GO; GO:0061025; P:membrane fusion; IDA:RGD.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; ISO:RGD.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.420.210; -; 1.
DR IDEAL; IID50026; -.
DR InterPro; IPR036241; NSFL1C_SEP_dom_sf.
DR InterPro; IPR012989; SEP_domain.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF08059; SEP; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00553; SEP; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF102848; SSF102848; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Golgi apparatus; Lipid-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..370
FT /note="NSFL1 cofactor p47"
FT /id="PRO_0000210990"
FT DOMAIN 179..244
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 291..368
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..115
FT /note="Nuclear localization signal"
FT MOTIF 172..175
FT /note="Nuclear localization signal"
FT COMPBIAS 54..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 140
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:12810701"
FT MOD_RES 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ44"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
FT MUTAGEN 41
FT /note="F->A: Reduces ubiquitin binding and Golgi
FT reassembly."
FT /evidence="ECO:0000269|PubMed:12411482"
FT MUTAGEN 57
FT /note="T->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12810701"
FT MUTAGEN 112
FT /note="K->T: Strongly reduces nuclear location."
FT /evidence="ECO:0000269|PubMed:12810701"
FT MUTAGEN 114
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12810701"
FT MUTAGEN 140
FT /note="S->A: Abolishes phosphorylation by CDK1."
FT /evidence="ECO:0000269|PubMed:12810701"
FT MUTAGEN 140
FT /note="S->D: Strongly reduces binding to Golgi membranes."
FT /evidence="ECO:0000269|PubMed:12810701"
FT MUTAGEN 173
FT /note="R->T: Strongly reduces nuclear location."
FT /evidence="ECO:0000269|PubMed:12810701"
FT MUTAGEN 272
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12810701"
FT MUTAGEN 301
FT /note="R->A: Reduced interaction with VCP."
FT /evidence="ECO:0000269|PubMed:14988733"
FT MUTAGEN 342..345
FT /note="TFPN->AG: Strongly reduced interaction with VCP."
FT /evidence="ECO:0000269|PubMed:14988733"
FT MUTAGEN 343
FT /note="F->S: Reduced interaction with VCP."
FT /evidence="ECO:0000269|PubMed:14988733"
FT MUTAGEN 345
FT /note="N->A: Reduced interaction with VCP."
FT /evidence="ECO:0000269|PubMed:14988733"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:1V92"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:1V92"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1V92"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1VAZ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1VAZ"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1VAZ"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:1VAZ"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:1VAZ"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1VAZ"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1VAZ"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1VAZ"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1S3S"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1I42"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:1S3S"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1S3S"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:1S3S"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:1S3S"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:1S3S"
SQ SEQUENCE 370 AA; 40680 MW; 60C81402E5C58134 CRC64;
MAEERQDALR EFVAVTGAEE DRARFFLESA GWDLQIALAS FYEDGGDEDI VTISQATPSS
VSRGTAPSDN RVTSFRDLIH DQDEEEEEEE GQRFYAGGSE RSGQQIVGPP RKKSPNELVD
DLFKGAKEHG AVAVERVTKS PGETSKPRPF AGGGYRLGAA PEEESAYVAG ERRRHSGQDV
HVVLKLWKTG FSLDNGDLRS YQDPSNAQFL ESIRRGEVPA ELRRLAHGGQ VNLDMEDHRD
EDFVKPKGAF KAFTGEGQKL GSTAPQVLNT SSPAQQAENE AKASSSILIN EAEPTTNIQI
RLADGGRLVQ KFNHSHRISD IRLFIVDARP AMAATSFVLM TTFPNKELAD ENQTLKEANL
LNAVIVQRLT
