S100P_HUMAN
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 03-AUG-2022, entry version 189.
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 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 [16]
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 -!- 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="http://atlasgeneticsoncology.org/Genes/S100PID42196ch4p16.html";
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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; 264.
DR IntAct; P25815; 33.
DR MINT; P25815; -.
DR STRING; 9606.ENSP00000296370; -.
DR DrugBank; DB01003; Cromoglicic acid.
DR DrugCentral; P25815; -.
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; P25815; -.
DR PeptideAtlas; P25815; -.
DR PRIDE; P25815; -.
DR ProteomicsDB; 54298; -.
DR TopDownProteomics; P25815; -.
DR Antibodypedia; 4560; 383 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 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; 1558629at2759; -.
DR PhylomeDB; P25815; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; P25815; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P25815; -.
DR BioGRID-ORCS; 6286; 16 hits in 1081 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 147 other tissues.
DR Genevisible; P25815; HS.
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 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 Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
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:2MJW"
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
