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Protein S100-P (Migration-inducing gene 9 protein) (MIG9) (Protein S100-E) (S100 calcium-binding protein P)

 S100P_HUMAN             Reviewed;          95 AA.
P25815; Q5J7W2;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
25-OCT-2017, entry version 163.
RecName: Full=Protein S100-P;
AltName: Full=Migration-inducing gene 9 protein;
Short=MIG9;
AltName: Full=Protein S100-E;
AltName: Full=S100 calcium-binding protein P;
Name=S100P; Synonyms=S100E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1633809; DOI=10.1111/j.1432-1033.1992.tb17080.x;
Becker T., Gerke V., Kube E., Weber K.;
"S100P, a novel Ca(2+)-binding protein from human placenta. cDNA
cloning, recombinant protein expression and Ca2+ binding properties.";
Eur. J. Biochem. 207:541-547(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Jin G., Wang S., Chen J.;
"Cloning, expression and characterization of a novel human calcium-
binding S100 gene.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human migration-inducing gene 9 (MIG9).";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-91.
TISSUE=Placenta;
PubMed=1540168; DOI=10.1016/0006-291X(92)91865-N;
Emoto Y., Kobayashi R., Akatsuka H., Hidaka H.;
"Purification and characterization of a new member of the S-100
protein family from human placenta.";
Biochem. Biophys. Res. Commun. 182:1246-1253(1992).
[7]
INTERACTION WITH EZR.
PubMed=12808036; DOI=10.1091/mbc.E02-09-0553;
Koltzscher M., Neumann C., Konig S., Gerke V.;
"Ca2+-dependent binding and activation of dormant ezrin by dimeric
S100P.";
Mol. Biol. Cell 14:2372-2384(2003).
[8]
TISSUE SPECIFICITY.
PubMed=14672411; DOI=10.1023/A:1026311423326;
Jin G., Wang S., Hu X., Jing Z., Chen J., Ying K., Xie Y., Mao Y.;
"Characterization of the tissue-specific expression of the s100P gene
which encodes an EF-hand Ca2+-binding protein.";
Mol. Biol. Rep. 30:243-248(2003).
[9]
SUBUNIT, AND INTERACTION WITH S100A1.
PubMed=15171681; DOI=10.1042/BJ20040142;
Wang G., Zhang S., Fernig D.G., Spiller D., Martin-Fernandez M.,
Zhang H., Ding Y., Rao Z., Rudland P.S., Barraclough R.;
"Heterodimeric interaction and interfaces of S100A1 and S100P.";
Biochem. J. 382:375-383(2004).
[10]
FUNCTION.
PubMed=14617629; DOI=10.1074/jbc.M310124200;
Arumugam T., Simeone D.M., Schmidt A.M., Logsdon C.D.;
"S100P stimulates cell proliferation and survival via receptor for
activated glycation end products (RAGE).";
J. Biol. Chem. 279:5059-5065(2004).
[11]
INTERACTION WITH S100PBP, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=15632002; DOI=10.1016/S0002-9440(10)62234-1;
Dowen S.E., Crnogorac-Jurcevic T., Gangeswaran R., Hansen M.,
Eloranta J.J., Bhakta V., Brentnall T.A., Luettges J., Kloeppel G.,
Lemoine N.R.;
"Expression of S100P and its novel binding partner S100PBPR in early
pancreatic cancer.";
Am. J. Pathol. 166:81-92(2005).
[12]
FUNCTION, INTERACTION WITH EZR, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF 21-SER--GLY-23; ASN-64; GLN-68 AND GLU-73.
PubMed=19111582; DOI=10.1016/j.bbamcr.2008.11.012;
Austermann J., Nazmi A.R., Heil A., Fritz G., Kolinski M., Filipek S.,
Gerke V.;
"Generation and characterization of a novel, permanently active S100P
mutant.";
Biochim. Biophys. Acta 1793:1078-1085(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
FUNCTION, INTERACTION WITH PPP5C, AND MUTAGENESIS OF 21-SER--GLY-23;
ASN-64; GLN-68 AND GLU-73.
PubMed=22399290; DOI=10.1074/jbc.M111.329771;
Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H.,
Tokuda M., Kobayashi R.;
"S100 proteins modulate protein phosphatase 5 function: a link between
CA2+ signal transduction and protein dephosphorylation.";
J. Biol. Chem. 287:13787-13798(2012).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=12507480; DOI=10.1016/S0022-2836(02)01278-0;
Zhang H., Wang G., Ding Y., Wang Z., Barraclough R., Rudland P.S.,
Fernig D.G., Rao Z.;
"The crystal structure at 2A resolution of the Ca2+ -binding protein
S100P.";
J. Mol. Biol. 325:785-794(2003).
[16]
STRUCTURE BY NMR.
PubMed=15213440; DOI=10.1023/B:JNMR.0000032617.88899.4b;
Lee Y.C., Volk D.E., Thiviyanathan V., Kleerekoper Q., Gribenko A.V.,
Zhang S., Gorenstein D.G., Makhatadze G.I., Luxon B.A.;
"NMR structure of the Apo-S100P protein.";
J. Biomol. NMR 29:399-402(2004).
-!- FUNCTION: May function as calcium sensor and contribute to
cellular calcium signaling. In a calcium-dependent manner,
functions by interacting with other proteins, such as EZR and
PPP5C, and indirectly plays a role in physiological processes like
the formation of microvilli in epithelial cells. May stimulate
cell proliferation in an autocrine manner via activation of the
receptor for activated glycation end products (RAGE).
{ECO:0000269|PubMed:14617629, ECO:0000269|PubMed:19111582,
ECO:0000269|PubMed:22399290}.
-!- SUBUNIT: Homodimer and heterodimer with S100A1. Interacts with
S100PBP and S100Z. Interacts with CACYBP in a calcium-dependent
manner. Dimeric form binds to and activates EZR/Ezrin by unmasking
its F-actin binding sites. Interacts with PPP5C (via TPR repeats);
the interaction is calcium-dependent and modulates PPP5C activity.
{ECO:0000269|PubMed:12808036, ECO:0000269|PubMed:15171681,
ECO:0000269|PubMed:15632002, ECO:0000269|PubMed:19111582,
ECO:0000269|PubMed:22399290}.
-!- INTERACTION:
Q15109:AGER; NbExp=2; IntAct=EBI-743700, EBI-1646426;
Q9CXW3:Cacybp (xeno); NbExp=2; IntAct=EBI-743700, EBI-767146;
P20809:IL11; NbExp=2; IntAct=EBI-743700, EBI-751694;
P23297:S100A1; NbExp=12; IntAct=EBI-743700, EBI-743686;
Q5T7Y6:S100A1; NbExp=4; IntAct=EBI-743700, EBI-11746600;
P04271:S100B; NbExp=6; IntAct=EBI-743700, EBI-458391;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-743700, EBI-750109;
Q9UBB9:TFIP11; NbExp=3; IntAct=EBI-743700, EBI-1105213;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection,
microvillus membrane. Note=Colocalizes with S100PBP in the
nucleus. Colocolizes with EZR in the microvilli in a calcium-
dependent manner.
-!- TISSUE SPECIFICITY: Detected in all of the tissues except brain,
testis and small intestine, expression level is higher in
placenta, heart, lung, skeletal muscle, spleen and leukocyte. Up-
regulated in various pancreatic ductal adenocarcinomas and
pancreatic intraepithelial neoplasias.
{ECO:0000269|PubMed:14672411, ECO:0000269|PubMed:15632002}.
-!- MISCELLANEOUS: This protein binds two calcium ions.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAS00487.1; Type=Miscellaneous discrepancy; Note=Sequencing error in Met-1 codon.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/S100PID42196ch4p16.html";
-----------------------------------------------------------------------
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EMBL; X65614; CAA46566.1; -; mRNA.
EMBL; AF539739; AAO41114.1; -; mRNA.
EMBL; BT007289; AAP35953.1; -; mRNA.
EMBL; AY423724; AAS00487.1; ALT_SEQ; mRNA.
EMBL; BC006819; AAH06819.1; -; mRNA.
CCDS; CCDS3391.1; -.
PIR; S24146; S24146.
RefSeq; NP_005971.1; NM_005980.2.
UniGene; Hs.2962; -.
PDB; 1J55; X-ray; 2.00 A; A=1-95.
PDB; 1OZO; NMR; -; A/B=1-95.
PDB; 2MJW; NMR; -; B/D=1-94.
PDBsum; 1J55; -.
PDBsum; 1OZO; -.
PDBsum; 2MJW; -.
ProteinModelPortal; P25815; -.
SMR; P25815; -.
BioGrid; 112194; 23.
IntAct; P25815; 15.
MINT; MINT-239013; -.
STRING; 9606.ENSP00000296370; -.
DrugBank; DB01003; Cromoglicic acid.
iPTMnet; P25815; -.
PhosphoSitePlus; P25815; -.
BioMuta; S100P; -.
DMDM; 134142; -.
EPD; P25815; -.
MaxQB; P25815; -.
PaxDb; P25815; -.
PeptideAtlas; P25815; -.
PRIDE; P25815; -.
TopDownProteomics; P25815; -.
DNASU; 6286; -.
Ensembl; ENST00000296370; ENSP00000296370; ENSG00000163993.
GeneID; 6286; -.
KEGG; hsa:6286; -.
UCSC; uc003gjl.4; human.
CTD; 6286; -.
DisGeNET; 6286; -.
EuPathDB; HostDB:ENSG00000163993.6; -.
GeneCards; S100P; -.
HGNC; HGNC:10504; S100P.
HPA; HPA019502; -.
MIM; 600614; gene.
neXtProt; NX_P25815; -.
OpenTargets; ENSG00000163993; -.
PharmGKB; PA34913; -.
eggNOG; ENOG410J11V; Eukaryota.
eggNOG; ENOG410YX5D; LUCA.
GeneTree; ENSGT00760000119034; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P25815; -.
OMA; CHKYFEQ; -.
OrthoDB; EOG091G10QT; -.
PhylomeDB; P25815; -.
TreeFam; TF332727; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; P25815; -.
GeneWiki; S100P; -.
GenomeRNAi; 6286; -.
PRO; PR:P25815; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163993; -.
CleanEx; HS_S100P; -.
Genevisible; P25815; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:HGNC.
GO; GO:0000287; F:magnesium ion binding; TAS:HGNC.
GO; GO:0050786; F:RAGE receptor binding; IEA:InterPro.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0010033; P:response to organic substance; IEP:UniProtKB.
CDD; cd00213; S-100; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR034325; S-100_dom.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
InterPro; IPR028494; S100P.
PANTHER; PTHR11639:SF69; PTHR11639:SF69; 1.
Pfam; PF01023; S_100; 1.
SMART; SM00054; EFh; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Direct protein sequencing; Membrane;
Metal-binding; Nucleus; Reference proteome; Repeat.
CHAIN 1 95 Protein S100-P.
/FTId=PRO_0000144032.
DOMAIN 12 47 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 49 84 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 19 32 1; low affinity.
CA_BIND 62 73 2; high affinity.
MUTAGEN 21 23 Missing: In S100Ppa; permanently active,
interacts with EZR and PPP5C in absence
of calcium; when associated with C-64, K-
68 and S-73.
{ECO:0000269|PubMed:19111582,
ECO:0000269|PubMed:22399290}.
MUTAGEN 64 64 N->C: In S100Ppa; permanently active,
interacts with EZR and PPP5C in absence
of calcium; when associated with 21-S--G-
23, K-68 and S-73.
{ECO:0000269|PubMed:19111582,
ECO:0000269|PubMed:22399290}.
MUTAGEN 68 68 Q->K: In S100Ppa; permanently active,
interacts with EZR and PPP5C in absence
of calcium; when associated with 21-S--G-
23, C-64 and S-73.
{ECO:0000269|PubMed:19111582,
ECO:0000269|PubMed:22399290}.
MUTAGEN 73 73 E->S: In S100Ppa; permanently active,
interacts with EZR and PPP5C in absence
of calcium; when associated with 21-S--G-
23, C-64 and K-68.
{ECO:0000269|PubMed:19111582,
ECO:0000269|PubMed:22399290}.
CONFLICT 12 12 I -> M (in Ref. 4; AAS00487).
{ECO:0000305}.
CONFLICT 32 32 E -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 44 44 F -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
HELIX 3 18 {ECO:0000244|PDB:1J55}.
STRAND 21 23 {ECO:0000244|PDB:1J55}.
STRAND 25 28 {ECO:0000244|PDB:2MJW}.
HELIX 30 40 {ECO:0000244|PDB:1J55}.
HELIX 44 46 {ECO:0000244|PDB:1OZO}.
HELIX 53 61 {ECO:0000244|PDB:1J55}.
STRAND 63 70 {ECO:0000244|PDB:1J55}.
HELIX 71 92 {ECO:0000244|PDB:1J55}.
SEQUENCE 95 AA; 10400 MW; 786E6E3F3EACC6C1 CRC64;
MTELETAMGM IIDVFSRYSG SEGSTQTLTK GELKVLMEKE LPGFLQSGKD KDAVDKLLKD
LDANGDAQVD FSEFIVFVAA ITSACHKYFE KAGLK


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