S100Z_HUMAN
ID S100Z_HUMAN Reviewed; 99 AA.
AC Q8WXG8;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein S100-Z {ECO:0000305};
DE AltName: Full=S100 calcium-binding protein Z {ECO:0000312|HGNC:HGNC:30367};
GN Name=S100Z {ECO:0000312|HGNC:HGNC:30367};
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], PROTEIN SEQUENCE OF 2-21, SUBUNIT,
RP CALCIUM-BINDING, TISSUE SPECIFICITY, INTERACTION WITH S100P, AND VARIANT
RP ALA-23.
RC TISSUE=Prostate;
RX PubMed=11747429; DOI=10.1021/bi0114731;
RA Gribenko A.V., Hopper J.E., Makhatadze G.I.;
RT "Molecular characterization and tissue distribution of a novel member of
RT the S100 family of EF-hand proteins.";
RL Biochemistry 40:15538-15548(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-23.
RC TISSUE=Testis;
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] {ECO:0007744|PDB:5HYD}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), AND SUBUNIT.
RX PubMed=28074300; DOI=10.1007/s00775-017-1437-4;
RA Calderone V., Fragai M., Gallo G., Luchinat C.;
RT "Solving the crystal structure of human calcium-free S100Z: the siege and
RT conquer of one of the last S100 family strongholds.";
RL J. Biol. Inorg. Chem. 22:519-526(2017).
CC -!- SUBUNIT: Homodimer (PubMed:28074300). Interacts with S100P
CC (PubMed:11747429). {ECO:0000269|PubMed:11747429,
CC ECO:0000269|PubMed:28074300}.
CC -!- INTERACTION:
CC Q8WXG8; Q00994: BEX3; NbExp=5; IntAct=EBI-12198403, EBI-741753;
CC Q8WXG8; O43482: OIP5; NbExp=3; IntAct=EBI-12198403, EBI-536879;
CC Q8WXG8; P50749: RASSF2; NbExp=3; IntAct=EBI-12198403, EBI-960081;
CC Q8WXG8; Q5RL73: RBM48; NbExp=3; IntAct=EBI-12198403, EBI-473821;
CC Q8WXG8; P23297: S100A1; NbExp=7; IntAct=EBI-12198403, EBI-743686;
CC Q8WXG8; P60903: S100A10; NbExp=6; IntAct=EBI-12198403, EBI-717048;
CC Q8WXG8; P33764: S100A3; NbExp=3; IntAct=EBI-12198403, EBI-1044747;
CC Q8WXG8; P04271: S100B; NbExp=3; IntAct=EBI-12198403, EBI-458391;
CC Q8WXG8; P25815: S100P; NbExp=3; IntAct=EBI-12198403, EBI-743700;
CC Q8WXG8; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-12198403, EBI-12004298;
CC -!- TISSUE SPECIFICITY: Highest level of expression in spleen and
CC leukocytes. {ECO:0000269|PubMed:11747429}.
CC -!- MISCELLANEOUS: This protein binds two calcium ions.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; AF437876; AAL30893.1; -; mRNA.
DR EMBL; AC114962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022320; AAH22320.1; -; mRNA.
DR CCDS; CCDS43333.1; -.
DR RefSeq; NP_570128.2; NM_130772.3.
DR RefSeq; XP_011541541.1; XM_011543239.2.
DR RefSeq; XP_011541542.1; XM_011543240.2.
DR RefSeq; XP_011541543.1; XM_011543241.2.
DR RefSeq; XP_011541546.1; XM_011543244.2.
DR RefSeq; XP_011541547.1; XM_011543245.2.
DR RefSeq; XP_016864660.1; XM_017009171.1.
DR RefSeq; XP_016864661.1; XM_017009172.1.
DR RefSeq; XP_016864662.1; XM_017009173.1.
DR PDB; 5HYD; X-ray; 2.30 A; A/B/C/D=2-97.
DR PDBsum; 5HYD; -.
DR AlphaFoldDB; Q8WXG8; -.
DR SMR; Q8WXG8; -.
DR BioGRID; 128065; 10.
DR IntAct; Q8WXG8; 11.
DR STRING; 9606.ENSP00000320430; -.
DR BioMuta; S100Z; -.
DR DMDM; 296453019; -.
DR MassIVE; Q8WXG8; -.
DR PaxDb; Q8WXG8; -.
DR PRIDE; Q8WXG8; -.
DR Antibodypedia; 54566; 131 antibodies from 22 providers.
DR DNASU; 170591; -.
DR Ensembl; ENST00000317593.9; ENSP00000320430.4; ENSG00000171643.14.
DR Ensembl; ENST00000513010.5; ENSP00000426768.1; ENSG00000171643.14.
DR Ensembl; ENST00000613039.1; ENSP00000483535.1; ENSG00000171643.14.
DR GeneID; 170591; -.
DR KEGG; hsa:170591; -.
DR MANE-Select; ENST00000317593.9; ENSP00000320430.4; NM_130772.4; NP_570128.2.
DR UCSC; uc003kep.1; human.
DR CTD; 170591; -.
DR DisGeNET; 170591; -.
DR GeneCards; S100Z; -.
DR HGNC; HGNC:30367; S100Z.
DR HPA; ENSG00000171643; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 610103; gene.
DR neXtProt; NX_Q8WXG8; -.
DR OpenTargets; ENSG00000171643; -.
DR PharmGKB; PA134902118; -.
DR VEuPathDB; HostDB:ENSG00000171643; -.
DR eggNOG; ENOG502S17E; Eukaryota.
DR GeneTree; ENSGT00940000161125; -.
DR HOGENOM; CLU_138624_2_1_1; -.
DR InParanoid; Q8WXG8; -.
DR OMA; MSQKDPM; -.
DR OrthoDB; 1495576at2759; -.
DR PhylomeDB; Q8WXG8; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; Q8WXG8; -.
DR SignaLink; Q8WXG8; -.
DR BioGRID-ORCS; 170591; 13 hits in 1070 CRISPR screens.
DR ChiTaRS; S100Z; human.
DR GenomeRNAi; 170591; -.
DR Pharos; Q8WXG8; Tbio.
DR PRO; PR:Q8WXG8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8WXG8; protein.
DR Bgee; ENSG00000171643; Expressed in monocyte and 85 other tissues.
DR Genevisible; Q8WXG8; HS.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028490; S100Z.
DR PANTHER; PTHR11639:SF72; PTHR11639:SF72; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Metal-binding;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11747429"
FT CHAIN 2..99
FT /note="Protein S100-Z"
FT /id="PRO_0000144033"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
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 33
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 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VARIANT 23
FT /note="E -> A (in dbSNP:rs1320308)"
FT /evidence="ECO:0000269|PubMed:11747429,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060484"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:5HYD"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5HYD"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:5HYD"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:5HYD"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:5HYD"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:5HYD"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5HYD"
FT HELIX 72..96
FT /evidence="ECO:0007829|PDB:5HYD"
SQ SEQUENCE 99 AA; 11620 MW; 2D019EE19C68E994 CRC64;
MPTQLEMAMD TMIRIFHRYS GKERKRFKLS KGELKLLLQR ELTEFLSCQK ETQLVDKIVQ
DLDANKDNEV DFNEFVVMVA ALTVACNDYF VEQLKKKGK
