ID   S100P_HUMAN             Reviewed;          95 AA.
AC   P25815; Q5J7W2;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Protein S100-P;
DE   AltName: Full=Migration-inducing gene 9 protein;
DE            Short=MIG9;
DE   AltName: Full=Protein S100-E;
DE   AltName: Full=S100 calcium-binding protein P;
GN   Name=S100P; Synonyms=S100E;
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].
RC   TISSUE=Placenta;
RX   PubMed=1633809; DOI=10.1111/j.1432-1033.1992.tb17080.x;
RA   Becker T., Gerke V., Kube E., Weber K.;
RT   "S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning,
RT   recombinant protein expression and Ca2+ binding properties.";
RL   Eur. J. Biochem. 207:541-547(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jin G., Wang S., Chen J.;
RT   "Cloning, expression and characterization of a novel human calcium-binding
RT   S100 gene.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim J.W.;
RT   "Identification of a human migration-inducing gene 9 (MIG9).";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [6]
RP   PROTEIN SEQUENCE OF 1-91.
RC   TISSUE=Placenta;
RX   PubMed=1540168; DOI=10.1016/0006-291x(92)91865-n;
RA   Emoto Y., Kobayashi R., Akatsuka H., Hidaka H.;
RT   "Purification and characterization of a new member of the S-100 protein
RT   family from human placenta.";
RL   Biochem. Biophys. Res. Commun. 182:1246-1253(1992).
RN   [7]
RP   INTERACTION WITH EZR.
RX   PubMed=12808036; DOI=10.1091/mbc.e02-09-0553;
RA   Koltzscher M., Neumann C., Konig S., Gerke V.;
RT   "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P.";
RL   Mol. Biol. Cell 14:2372-2384(2003).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=14672411; DOI=10.1023/a:1026311423326;
RA   Jin G., Wang S., Hu X., Jing Z., Chen J., Ying K., Xie Y., Mao Y.;
RT   "Characterization of the tissue-specific expression of the s100P gene which
RT   encodes an EF-hand Ca2+-binding protein.";
RL   Mol. Biol. Rep. 30:243-248(2003).
RN   [9]
RP   SUBUNIT, AND INTERACTION WITH S100A1.
RX   PubMed=15171681; DOI=10.1042/bj20040142;
RA   Wang G., Zhang S., Fernig D.G., Spiller D., Martin-Fernandez M., Zhang H.,
RA   Ding Y., Rao Z., Rudland P.S., Barraclough R.;
RT   "Heterodimeric interaction and interfaces of S100A1 and S100P.";
RL   Biochem. J. 382:375-383(2004).
RN   [10]
RP   FUNCTION.
RX   PubMed=14617629; DOI=10.1074/jbc.m310124200;
RA   Arumugam T., Simeone D.M., Schmidt A.M., Logsdon C.D.;
RT   "S100P stimulates cell proliferation and survival via receptor for
RT   activated glycation end products (RAGE).";
RL   J. Biol. Chem. 279:5059-5065(2004).
RN   [11]
RP   INTERACTION WITH S100PBP, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15632002; DOI=10.1016/s0002-9440(10)62234-1;
RA   Dowen S.E., Crnogorac-Jurcevic T., Gangeswaran R., Hansen M.,
RA   Eloranta J.J., Bhakta V., Brentnall T.A., Luettges J., Kloeppel G.,
RA   Lemoine N.R.;
RT   "Expression of S100P and its novel binding partner S100PBPR in early
RT   pancreatic cancer.";
RL   Am. J. Pathol. 166:81-92(2005).
RN   [12]
RP   FUNCTION, INTERACTION WITH EZR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   21-SER--GLY-23; ASN-64; GLN-68 AND GLU-73.
RX   PubMed=19111582; DOI=10.1016/j.bbamcr.2008.11.012;
RA   Austermann J., Nazmi A.R., Heil A., Fritz G., Kolinski M., Filipek S.,
RA   Gerke V.;
RT   "Generation and characterization of a novel, permanently active S100P
RT   mutant.";
RL   Biochim. Biophys. Acta 1793:1078-1085(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   FUNCTION, INTERACTION WITH PPP5C, AND MUTAGENESIS OF 21-SER--GLY-23;
RP   ASN-64; GLN-68 AND GLU-73.
RX   PubMed=22399290; DOI=10.1074/jbc.m111.329771;
RA   Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H., Tokuda M.,
RA   Kobayashi R.;
RT   "S100 proteins modulate protein phosphatase 5 function: a link between CA2+
RT   signal transduction and protein dephosphorylation.";
RL   J. Biol. Chem. 287:13787-13798(2012).
RN   [15]
RP   INTERACTION WITH P.FALCIPARUM MSP1 (MICROBIAL INFECTION).
RX   PubMed=22431641; DOI=10.1073/pnas.1202689109;
RA   Waisberg M., Cerqueira G.C., Yager S.B., Francischetti I.M., Lu J.,
RA   Gera N., Srinivasan P., Miura K., Rada B., Lukszo J., Barbian K.D.,
RA   Leto T.L., Porcella S.F., Narum D.L., El-Sayed N., Miller L.H.,
RA   Pierce S.K.;
RT   "Plasmodium falciparum merozoite surface protein 1 blocks the
RT   proinflammatory protein S100P.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5429-5434(2012).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=12507480; DOI=10.1016/s0022-2836(02)01278-0;
RA   Zhang H., Wang G., Ding Y., Wang Z., Barraclough R., Rudland P.S.,
RA   Fernig D.G., Rao Z.;
RT   "The crystal structure at 2A resolution of the Ca2+ -binding protein
RT   S100P.";
RL   J. Mol. Biol. 325:785-794(2003).
RN   [17]
RP   STRUCTURE BY NMR.
RX   PubMed=15213440; DOI=10.1023/b:jnmr.0000032617.88899.4b;
RA   Lee Y.C., Volk D.E., Thiviyanathan V., Kleerekoper Q., Gribenko A.V.,
RA   Zhang S., Gorenstein D.G., Makhatadze G.I., Luxon B.A.;
RT   "NMR structure of the Apo-S100P protein.";
RL   J. Biomol. NMR 29:399-402(2004).
CC   -!- FUNCTION: May function as calcium sensor and contribute to cellular
CC       calcium signaling. In a calcium-dependent manner, functions by
CC       interacting with other proteins, such as EZR and PPP5C, and indirectly
CC       plays a role in physiological processes like the formation of
CC       microvilli in epithelial cells. May stimulate cell proliferation in an
CC       autocrine manner via activation of the receptor for activated glycation
CC       end products (RAGE). {ECO:0000269|PubMed:14617629,
CC       ECO:0000269|PubMed:19111582, ECO:0000269|PubMed:22399290}.
CC   -!- SUBUNIT: Homodimer and heterodimer with S100A1. Interacts with S100PBP
CC       and S100Z. Interacts with CACYBP in a calcium-dependent manner. Dimeric
CC       form binds to and activates EZR/Ezrin by unmasking its F-actin binding
CC       sites. Interacts with PPP5C (via TPR repeats); the interaction is
CC       calcium-dependent and modulates PPP5C activity.
CC       {ECO:0000269|PubMed:12808036, ECO:0000269|PubMed:15171681,
CC       ECO:0000269|PubMed:15632002, ECO:0000269|PubMed:19111582,
CC       ECO:0000269|PubMed:22399290}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with P.falciparum (strains 3D7
CC       and FVO) MSP1 subunit p33; the interaction blocks S100P inflammatory
CC       and chemotactic activities. {ECO:0000269|PubMed:22431641}.
CC   -!- INTERACTION:
CC       P25815; Q15109: AGER; NbExp=2; IntAct=EBI-743700, EBI-1646426;
CC       P25815; Q7LC44: ARC; NbExp=3; IntAct=EBI-743700, EBI-750550;
CC       P25815; P52907: CAPZA1; NbExp=2; IntAct=EBI-743700, EBI-355586;
CC       P25815; P42858: HTT; NbExp=9; IntAct=EBI-743700, EBI-466029;
CC       P25815; P20809: IL11; NbExp=2; IntAct=EBI-743700, EBI-751694;
CC       P25815; P35579: MYH9; NbExp=3; IntAct=EBI-743700, EBI-350338;
CC       P25815; P07196: NEFL; NbExp=3; IntAct=EBI-743700, EBI-475646;
CC       P25815; P23297: S100A1; NbExp=11; IntAct=EBI-743700, EBI-743686;
CC       P25815; Q5T7Y6: S100A1; NbExp=4; IntAct=EBI-743700, EBI-11746600;
CC       P25815; P04271: S100B; NbExp=7; IntAct=EBI-743700, EBI-458391;
CC       P25815; Q8WXG8: S100Z; NbExp=3; IntAct=EBI-743700, EBI-12198403;
CC       P25815; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-743700, EBI-750109;
CC       P25815; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-743700, EBI-1105213;
CC       P25815; Q15582: TGFBI; NbExp=3; IntAct=EBI-743700, EBI-10236573;
CC       P25815; P04637: TP53; NbExp=2; IntAct=EBI-743700, EBI-366083;
CC       P25815; P11441: UBL4A; NbExp=3; IntAct=EBI-743700, EBI-356983;
CC       P25815; O76024: WFS1; NbExp=3; IntAct=EBI-743700, EBI-720609;
CC       P25815; Q9CXW3: Cacybp; Xeno; NbExp=2; IntAct=EBI-743700, EBI-767146;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, microvillus
CC       membrane. Note=Colocalizes with S100PBP in the nucleus. Colocolizes
CC       with EZR in the microvilli in a calcium-dependent manner.
CC   -!- TISSUE SPECIFICITY: Detected in all of the tissues except brain, testis
CC       and small intestine, expression level is higher in placenta, heart,
CC       lung, skeletal muscle, spleen and leukocyte. Up-regulated in various
CC       pancreatic ductal adenocarcinomas and pancreatic intraepithelial
CC       neoplasias. {ECO:0000269|PubMed:14672411, ECO:0000269|PubMed:15632002}.
CC   -!- MISCELLANEOUS: This protein binds two calcium ions.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS00487.1; Type=Miscellaneous discrepancy; Note=Sequencing error in Met-1 codon.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42196/S100P";
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; X65614; CAA46566.1; -; mRNA.
DR   EMBL; AF539739; AAO41114.1; -; mRNA.
DR   EMBL; BT007289; AAP35953.1; -; mRNA.
DR   EMBL; AY423724; AAS00487.1; ALT_SEQ; mRNA.
DR   EMBL; BC006819; AAH06819.1; -; mRNA.
DR   CCDS; CCDS3391.1; -.
DR   PIR; S24146; S24146.
DR   RefSeq; NP_005971.1; NM_005980.2.
DR   PDB; 1J55; X-ray; 2.00 A; A=1-95.
DR   PDB; 1OZO; NMR; -; A/B=1-95.
DR   PDB; 2MJW; NMR; -; B/D=1-94.
DR   PDB; 7NMI; X-ray; 2.10 A; B=1-95.
DR   PDBsum; 1J55; -.
DR   PDBsum; 1OZO; -.
DR   PDBsum; 2MJW; -.
DR   PDBsum; 7NMI; -.
DR   AlphaFoldDB; P25815; -.
DR   BMRB; P25815; -.
DR   SMR; P25815; -.
DR   BioGRID; 112194; 300.
DR   IntAct; P25815; 33.
DR   MINT; P25815; -.
DR   STRING; 9606.ENSP00000296370; -.
DR   DrugBank; DB01003; Cromoglicic acid.
DR   DrugCentral; P25815; -.
DR   GlyGen; P25815; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P25815; -.
DR   PhosphoSitePlus; P25815; -.
DR   BioMuta; S100P; -.
DR   DMDM; 134142; -.
DR   EPD; P25815; -.
DR   jPOST; P25815; -.
DR   MassIVE; P25815; -.
DR   MaxQB; P25815; -.
DR   PaxDb; 9606-ENSP00000296370; -.
DR   PeptideAtlas; P25815; -.
DR   ProteomicsDB; 54298; -.
DR   Pumba; P25815; -.
DR   TopDownProteomics; P25815; -.
DR   Antibodypedia; 4560; 507 antibodies from 32 providers.
DR   DNASU; 6286; -.
DR   Ensembl; ENST00000296370.4; ENSP00000296370.3; ENSG00000163993.7.
DR   GeneID; 6286; -.
DR   KEGG; hsa:6286; -.
DR   MANE-Select; ENST00000296370.4; ENSP00000296370.3; NM_005980.3; NP_005971.1.
DR   UCSC; uc003gjl.4; human.
DR   AGR; HGNC:10504; -.
DR   CTD; 6286; -.
DR   DisGeNET; 6286; -.
DR   GeneCards; S100P; -.
DR   HGNC; HGNC:10504; S100P.
DR   HPA; ENSG00000163993; Tissue enhanced (bone marrow, stomach, urinary bladder).
DR   MIM; 600614; gene.
DR   neXtProt; NX_P25815; -.
DR   OpenTargets; ENSG00000163993; -.
DR   PharmGKB; PA34913; -.
DR   VEuPathDB; HostDB:ENSG00000163993; -.
DR   eggNOG; ENOG502S6E1; Eukaryota.
DR   GeneTree; ENSGT00940000162871; -.
DR   HOGENOM; CLU_138624_6_1_1; -.
DR   InParanoid; P25815; -.
DR   OMA; FNEFIIF; -.
DR   OrthoDB; 3777956at2759; -.
DR   PhylomeDB; P25815; -.
DR   TreeFam; TF332727; -.
DR   PathwayCommons; P25815; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; P25815; -.
DR   SIGNOR; P25815; -.
DR   BioGRID-ORCS; 6286; 17 hits in 1160 CRISPR screens.
DR   ChiTaRS; S100P; human.
DR   EvolutionaryTrace; P25815; -.
DR   GeneWiki; S100P; -.
DR   GenomeRNAi; 6286; -.
DR   Pharos; P25815; Tbio.
DR   PRO; PR:P25815; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P25815; Protein.
DR   Bgee; ENSG00000163993; Expressed in nasal cavity epithelium and 149 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:HGNC-UCL.
DR   GO; GO:0000287; F:magnesium ion binding; TAS:HGNC-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
DR   GO; GO:0010033; P:response to organic substance; IEP:UniProtKB.
DR   CDD; cd00213; S-100; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR034325; S-100_dom.
DR   InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   PANTHER; PTHR11639:SF134; PROTEIN S100-A1-RELATED; 1.
DR   PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM00054; EFh; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
DR   Genevisible; P25815; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell membrane; Cell projection; Cytoplasm;
KW   Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..95
FT                   /note="Protein S100-P"
FT                   /id="PRO_0000144032"
FT   DOMAIN          12..47
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          49..84
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         25
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         21..23
FT                   /note="Missing: In S100Ppa; permanently active, interacts
FT                   with EZR and PPP5C in absence of calcium; when associated
FT                   with C-64, K-68 and S-73."
FT                   /evidence="ECO:0000269|PubMed:19111582,
FT                   ECO:0000269|PubMed:22399290"
FT   MUTAGEN         64
FT                   /note="N->C: In S100Ppa; permanently active, interacts with
FT                   EZR and PPP5C in absence of calcium; when associated with
FT                   21-S--G-23, K-68 and S-73."
FT                   /evidence="ECO:0000269|PubMed:19111582,
FT                   ECO:0000269|PubMed:22399290"
FT   MUTAGEN         68
FT                   /note="Q->K: In S100Ppa; permanently active, interacts with
FT                   EZR and PPP5C in absence of calcium; when associated with
FT                   21-S--G-23, C-64 and S-73."
FT                   /evidence="ECO:0000269|PubMed:19111582,
FT                   ECO:0000269|PubMed:22399290"
FT   MUTAGEN         73
FT                   /note="E->S: In S100Ppa; permanently active, interacts with
FT                   EZR and PPP5C in absence of calcium; when associated with
FT                   21-S--G-23, C-64 and K-68."
FT                   /evidence="ECO:0000269|PubMed:19111582,
FT                   ECO:0000269|PubMed:22399290"
FT   CONFLICT        12
FT                   /note="I -> M (in Ref. 4; AAS00487)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="E -> T (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="F -> E (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..18
FT                   /evidence="ECO:0007829|PDB:1J55"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:1J55"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:7NMI"
FT   HELIX           30..40
FT                   /evidence="ECO:0007829|PDB:1J55"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:1OZO"
FT   HELIX           53..61
FT                   /evidence="ECO:0007829|PDB:1J55"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:1J55"
FT   HELIX           71..92
FT                   /evidence="ECO:0007829|PDB:1J55"
SQ   SEQUENCE   95 AA;  10400 MW;  786E6E3F3EACC6C1 CRC64;
     MTELETAMGM IIDVFSRYSG SEGSTQTLTK GELKVLMEKE LPGFLQSGKD KDAVDKLLKD
     LDANGDAQVD FSEFIVFVAA ITSACHKYFE KAGLK
//