NEUS_HUMAN
ID NEUS_HUMAN Reviewed; 410 AA.
AC Q99574; A8K217; D3DNP1; Q6AHZ4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Neuroserpin;
DE AltName: Full=Peptidase inhibitor 12;
DE Short=PI-12;
DE AltName: Full=Serpin I1;
DE Flags: Precursor;
GN Name=SERPINI1; Synonyms=PI12;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=9070919; DOI=10.1006/geno.1996.4514;
RA Schrimpf S.P., Bleiker A.J., Brecevic L., Kozlov S.V., Berger P.,
RA Osterwalder T., Krueger S.R., Schinzel A., Sonderegger P.;
RT "Human neuroserpin (PI12): cDNA cloning and chromosomal localization to
RT 3q26.";
RL Genomics 40:55-62(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kinter J., Berger P., Kozlov S.V., Sonderegger P.;
RT "Genomic organization of the human neuroserpin (PI12) gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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 MRNA].
RC TISSUE=Brain cortex;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 (SEP-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 FUNCTION.
RX PubMed=9442076; DOI=10.1074/jbc.273.4.2312;
RA Osterwalder T., Cinelli P., Baici A., Pennella A., Krueger S.R.,
RA Schrimpf S.P., Meins M., Sonderegger P.;
RT "The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits
RT plasminogen activators and plasmin but not thrombin.";
RL J. Biol. Chem. 273:2312-2321(1998).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17040209; DOI=10.1042/bj20061170;
RA Ishigami S., Sandkvist M., Tsui F., Moore E., Coleman T.A., Lawrence D.A.;
RT "Identification of a novel targeting sequence for regulated secretion in
RT the serine protease inhibitor neuroserpin.";
RL Biochem. J. 402:25-34(2007).
RN [9]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-289.
RX PubMed=26329378; DOI=10.1038/srep13666;
RA Noto R., Randazzo L., Raccosta S., Caccia S., Moriconi C., Miranda E.,
RA Martorana V., Manno M.;
RT "The stability and activity of human neuroserpin are modulated by a salt
RT bridge that stabilises the reactive centre loop.";
RL Sci. Rep. 5:13666-13666(2015).
RN [10] {ECO:0007744|PDB:3F02, ECO:0007744|PDB:3F5N}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 17-362 AND 363-410, FUNCTION, AND
RP REACTIVE BOND.
RX PubMed=19265707; DOI=10.1016/j.jmb.2009.02.056;
RA Ricagno S., Caccia S., Sorrentino G., Antonini G., Bolognesi M.;
RT "Human neuroserpin: structure and time-dependent inhibition.";
RL J. Mol. Biol. 388:109-121(2009).
RN [11] {ECO:0007744|PDB:3FGQ}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 17-400, FUNCTION, MUTAGENESIS OF
RP ASN-161; LEU-162; VAL-163 AND SER-340, SUBUNIT, AND REACTIVE BOND.
RX PubMed=19285087; DOI=10.1016/j.jmb.2009.03.007;
RA Takehara S., Onda M., Zhang J., Nishiyama M., Yang X., Mikami B.,
RA Lomas D.A.;
RT "The 2.1-A crystal structure of native neuroserpin reveals unique
RT structural elements that contribute to conformational instability.";
RL J. Mol. Biol. 388:11-20(2009).
RN [12]
RP VARIANTS FENIB PRO-49 AND ARG-52.
RX PubMed=10517635; DOI=10.1038/43894;
RA Davis R.L., Shrimpton A.E., Holohan P.D., Bradshaw C., Feiglin D.,
RA Collins G.H., Sonderegger P., Kinter J., Becker L.M., Lacbawan F.,
RA Krasnewich D., Muenke M., Lawrence D.A., Yerby M.S., Shaw C.M., Gooptu B.,
RA Elliott P.R., Finch J.T., Carrell R.W., Lomas D.A.;
RT "Familial dementia caused by polymerization of mutant neuroserpin.";
RL Nature 401:376-379(1999).
RN [13]
RP CHARACTERIZATION OF VARIANT FENIB PRO-49, AND FUNCTION.
RX PubMed=11880376; DOI=10.1074/jbc.m200680200;
RA Belorgey D., Crowther D.C., Mahadeva R., Lomas D.A.;
RT "Mutant Neuroserpin (S49P) that causes familial encephalopathy with
RT neuroserpin inclusion bodies is a poor proteinase inhibitor and readily
RT forms polymers in vitro.";
RL J. Biol. Chem. 277:17367-17373(2002).
CC -!- FUNCTION: Serine protease inhibitor that inhibits plasminogen
CC activators and plasmin but not thrombin (PubMed:9442076,
CC PubMed:26329378, PubMed:19265707, PubMed:19285087, PubMed:11880376).
CC May be involved in the formation or reorganization of synaptic
CC connections as well as for synaptic plasticity in the adult nervous
CC system. May protect neurons from cell damage by tissue-type plasminogen
CC activator (Probable). {ECO:0000269|PubMed:11880376,
CC ECO:0000269|PubMed:19265707, ECO:0000269|PubMed:19285087,
CC ECO:0000269|PubMed:26329378, ECO:0000269|PubMed:9442076, ECO:0000305}.
CC -!- SUBUNIT: Monomer. Has a tendency to form large polymers already at 41
CC and 45 degrees Celsius (in vitro). {ECO:0000269|PubMed:19285087,
CC ECO:0000269|PubMed:26329378}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17040209}.
CC Cytoplasmic vesicle, secretory vesicle lumen
CC {ECO:0000305|PubMed:17040209}. Perikaryon
CC {ECO:0000269|PubMed:17040209}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex and hippocampus pyramidal
CC neurons (at protein level) (PubMed:17040209). Predominantly expressed
CC in the brain (PubMed:9070919). {ECO:0000269|PubMed:17040209,
CC ECO:0000269|PubMed:9070919}.
CC -!- DISEASE: Encephalopathy, familial, with neuroserpin inclusion bodies
CC (FENIB) [MIM:604218]: A neurodegenerative disease clinically
CC characterized by dementia. Additional features include intellectual
CC decline, psychic seizures, progressive myoclonic epilepsy, and cerebral
CC atrophy. Histologically, it is characterized by the presence of
CC eosinophilic inclusion bodies (called Collins bodies) throughout the
CC deeper layers of the cerebral cortex, leading to neuronal death.
CC {ECO:0000269|PubMed:10517635, ECO:0000269|PubMed:11880376}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; Z81326; CAB03626.1; -; mRNA.
DR EMBL; AF248246; AAG01089.1; -; Genomic_DNA.
DR EMBL; AF248244; AAG01089.1; JOINED; Genomic_DNA.
DR EMBL; AF248245; AAG01089.1; JOINED; Genomic_DNA.
DR EMBL; AK290082; BAF82771.1; -; mRNA.
DR EMBL; CR627434; CAH10520.1; -; mRNA.
DR EMBL; CH471052; EAW78571.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78572.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78573.1; -; Genomic_DNA.
DR EMBL; BC018043; AAH18043.1; -; mRNA.
DR CCDS; CCDS3203.1; -.
DR RefSeq; NP_001116224.1; NM_001122752.1.
DR RefSeq; NP_005016.1; NM_005025.4.
DR RefSeq; XP_016862107.1; XM_017006618.1.
DR PDB; 3F02; X-ray; 1.80 A; A/B=17-362, C/D=363-410.
DR PDB; 3F5N; X-ray; 3.15 A; A/B/C/D/E=17-410.
DR PDB; 3FGQ; X-ray; 2.09 A; A/B=17-400.
DR PDBsum; 3F02; -.
DR PDBsum; 3F5N; -.
DR PDBsum; 3FGQ; -.
DR AlphaFoldDB; Q99574; -.
DR SMR; Q99574; -.
DR BioGRID; 111292; 8.
DR IntAct; Q99574; 3.
DR MINT; Q99574; -.
DR STRING; 9606.ENSP00000295777; -.
DR MEROPS; I04.025; -.
DR GlyConnect; 1559; 2 N-Linked glycans (1 site).
DR GlyGen; Q99574; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q99574; -.
DR PhosphoSitePlus; Q99574; -.
DR BioMuta; SERPINI1; -.
DR DMDM; 3183087; -.
DR EPD; Q99574; -.
DR jPOST; Q99574; -.
DR MassIVE; Q99574; -.
DR MaxQB; Q99574; -.
DR PaxDb; Q99574; -.
DR PeptideAtlas; Q99574; -.
DR PRIDE; Q99574; -.
DR ProteomicsDB; 78333; -.
DR Antibodypedia; 987; 478 antibodies from 39 providers.
DR DNASU; 5274; -.
DR Ensembl; ENST00000295777.9; ENSP00000295777.5; ENSG00000163536.13.
DR Ensembl; ENST00000446050.7; ENSP00000397373.2; ENSG00000163536.13.
DR GeneID; 5274; -.
DR KEGG; hsa:5274; -.
DR MANE-Select; ENST00000446050.7; ENSP00000397373.2; NM_001122752.2; NP_001116224.1.
DR UCSC; uc003ffa.5; human.
DR CTD; 5274; -.
DR DisGeNET; 5274; -.
DR GeneCards; SERPINI1; -.
DR HGNC; HGNC:8943; SERPINI1.
DR HPA; ENSG00000163536; Tissue enhanced (brain, choroid plexus).
DR MalaCards; SERPINI1; -.
DR MIM; 602445; gene.
DR MIM; 604218; phenotype.
DR neXtProt; NX_Q99574; -.
DR OpenTargets; ENSG00000163536; -.
DR Orphanet; 530303; Progressive dementia with neuroserpin inclusion bodies.
DR PharmGKB; PA35511; -.
DR VEuPathDB; HostDB:ENSG00000163536; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158168; -.
DR HOGENOM; CLU_023330_0_4_1; -.
DR InParanoid; Q99574; -.
DR OMA; KDVWRGL; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q99574; -.
DR TreeFam; TF352620; -.
DR PathwayCommons; Q99574; -.
DR SignaLink; Q99574; -.
DR BioGRID-ORCS; 5274; 14 hits in 1076 CRISPR screens.
DR EvolutionaryTrace; Q99574; -.
DR GeneWiki; SERPINI1; -.
DR GenomeRNAi; 5274; -.
DR Pharos; Q99574; Tbio.
DR PRO; PR:Q99574; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q99574; protein.
DR Bgee; ENSG00000163536; Expressed in frontal pole and 198 other tissues.
DR ExpressionAtlas; Q99574; baseline and differential.
DR Genevisible; Q99574; HS.
DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0034774; C:secretory granule lumen; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007422; P:peripheral nervous system development; TAS:ProtInc.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:ARUK-UCL.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Disease variant; Glycoprotein;
KW Neurodegeneration; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..410
FT /note="Neuroserpin"
FT /id="PRO_0000032521"
FT SITE 362..363
FT /note="Reactive bond"
FT /evidence="ECO:0000269|PubMed:19265707,
FT ECO:0000305|PubMed:19285087"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 49
FT /note="S -> P (in FENIB; Syracuse; decreased protein
FT stability; decreased proteinase inhibitor activity;
FT increased tendency to form polymers; dbSNP:rs121909051)"
FT /evidence="ECO:0000269|PubMed:10517635,
FT ECO:0000269|PubMed:11880376"
FT /id="VAR_008520"
FT VARIANT 52
FT /note="S -> R (in FENIB; Portland)"
FT /evidence="ECO:0000269|PubMed:10517635"
FT /id="VAR_008521"
FT MUTAGEN 161
FT /note="N->G: Increases protein stability and abolishes
FT tendency to form polymers. No effect on inhibitory
FT activity."
FT /evidence="ECO:0000269|PubMed:19285087"
FT MUTAGEN 162
FT /note="L->K: Increases protein stability and abolishes
FT tendency to form polymers. No effect on inhibitory
FT activity."
FT /evidence="ECO:0000269|PubMed:19285087"
FT MUTAGEN 163
FT /note="V->I: Increases protein stability and decreases
FT tendency to form polymers. No effect on inhibitory
FT activity."
FT /evidence="ECO:0000269|PubMed:19285087"
FT MUTAGEN 289
FT /note="E->A: Slightly decreases inhibitory activity. No
FT effect on thermal stability."
FT /evidence="ECO:0000269|PubMed:26329378"
FT MUTAGEN 340
FT /note="S->A: Increases protein stability and decreases
FT tendency to form polymers. No effect on inhibitory
FT activity."
FT /evidence="ECO:0000269|PubMed:19285087"
FT CONFLICT 70
FT /note="K -> E (in Ref. 6; AAH18043)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="S -> Y (in Ref. 6; AAH18043)"
FT /evidence="ECO:0000305"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:3F02"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3FGQ"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:3F02"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 176..192
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 211..229
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:3F02"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:3F02"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 331..344
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 346..361
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:3F02"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:3F02"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:3F02"
SQ SEQUENCE 410 AA; 46427 MW; D966E9036BB21943 CRC64;
MAFLGLFSLL VLQSMATGAT FPEEAIADLS VNMYNRLRAT GEDENILFSP LSIALAMGMM
ELGAQGSTQK EIRHSMGYDS LKNGEEFSFL KEFSNMVTAK ESQYVMKIAN SLFVQNGFHV
NEEFLQMMKK YFNAAVNHVD FSQNVAVANY INKWVENNTN NLVKDLVSPR DFDAATYLAL
INAVYFKGNW KSQFRPENTR TFSFTKDDES EVQIPMMYQQ GEFYYGEFSD GSNEAGGIYQ
VLEIPYEGDE ISMMLVLSRQ EVPLATLEPL VKAQLVEEWA NSVKKQKVEV YLPRFTVEQE
IDLKDVLKAL GITEIFIKDA NLTGLSDNKE IFLSKAIHKS FLEVNEEGSE AAAVSGMIAI
SRMAVLYPQV IVDHPFFFLI RNRRTGTILF MGRVMHPETM NTSGHDFEEL
