ID   S100G_HUMAN             Reviewed;          79 AA.
AC   P29377; Q5JS49;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=Protein S100-G;
DE   AltName: Full=Calbindin-D9k;
DE   AltName: Full=S100 calcium-binding protein G;
DE   AltName: Full=Vitamin D-dependent calcium-binding protein, intestinal;
DE            Short=CABP;
GN   Name=S100G; Synonyms=CABP9K, CALB3, S100D;
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].
RX   PubMed=1610358; DOI=10.1016/0006-291x(92)91676-h;
RA   Howard A., Legon S., Spurr N.K., Walters J.R.I.;
RT   "Molecular cloning and chromosomal assignment of human calbindin-D9k.";
RL   Biochem. Biophys. Res. Commun. 185:663-669(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1379540; DOI=10.1016/0014-5793(92)80772-9;
RA   Jeung E.B., Krisinger J., Dann J.L., Leung P.C.K.;
RT   "Molecular cloning of the full-length cDNA encoding the human calbindin-
RT   D9k.";
RL   FEBS Lett. 307:224-228(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8308886; DOI=10.1006/jmbi.1994.1076;
RA   Jeung E.B., Leung P.C.K., Krisinger J.;
RT   "The human calbindin-D9k gene. Complete structure and implications on
RT   steroid hormone regulation.";
RL   J. Mol. Biol. 235:1231-1238(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC   -!- INTERACTION:
CC       P29377; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-22734539, EBI-12028784;
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR   EMBL; X65869; CAA46699.1; -; mRNA.
DR   EMBL; L13220; AAA35638.1; -; mRNA.
DR   EMBL; L13042; AAA35637.1; -; Genomic_DNA.
DR   EMBL; AL445467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC112174; AAI12175.1; -; mRNA.
DR   CCDS; CCDS14176.1; -.
DR   PIR; JN0246; JN0246.
DR   RefSeq; NP_004048.1; NM_004057.2.
DR   RefSeq; XP_016885330.1; XM_017029841.1.
DR   AlphaFoldDB; P29377; -.
DR   BMRB; P29377; -.
DR   SMR; P29377; -.
DR   BioGRID; 107246; 1.
DR   IntAct; P29377; 4.
DR   STRING; 9606.ENSP00000369547; -.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   DrugBank; DB04464; N-Formylmethionine.
DR   iPTMnet; P29377; -.
DR   PhosphoSitePlus; P29377; -.
DR   BioMuta; S100G; -.
DR   DMDM; 115387; -.
DR   MassIVE; P29377; -.
DR   PaxDb; 9606-ENSP00000369547; -.
DR   PeptideAtlas; P29377; -.
DR   ProteomicsDB; 54565; -.
DR   Antibodypedia; 4324; 83 antibodies from 15 providers.
DR   DNASU; 795; -.
DR   Ensembl; ENST00000380200.3; ENSP00000369547.3; ENSG00000169906.5.
DR   GeneID; 795; -.
DR   KEGG; hsa:795; -.
DR   MANE-Select; ENST00000380200.3; ENSP00000369547.3; NM_004057.3; NP_004048.1.
DR   UCSC; uc004cxn.2; human.
DR   AGR; HGNC:1436; -.
DR   CTD; 795; -.
DR   DisGeNET; 795; -.
DR   GeneCards; S100G; -.
DR   HGNC; HGNC:1436; S100G.
DR   HPA; ENSG00000169906; Tissue enriched (intestine).
DR   MIM; 302020; gene.
DR   neXtProt; NX_P29377; -.
DR   OpenTargets; ENSG00000169906; -.
DR   PharmGKB; PA26028; -.
DR   VEuPathDB; HostDB:ENSG00000169906; -.
DR   eggNOG; ENOG502T3Z3; Eukaryota.
DR   GeneTree; ENSGT00530000064238; -.
DR   HOGENOM; CLU_138624_4_0_1; -.
DR   InParanoid; P29377; -.
DR   OMA; QKYAAKE; -.
DR   OrthoDB; 4248222at2759; -.
DR   PhylomeDB; P29377; -.
DR   TreeFam; TF332727; -.
DR   PathwayCommons; P29377; -.
DR   SignaLink; P29377; -.
DR   SIGNOR; P29377; -.
DR   BioGRID-ORCS; 795; 46 hits in 710 CRISPR screens.
DR   ChiTaRS; S100G; human.
DR   GeneWiki; S100G; -.
DR   GenomeRNAi; 795; -.
DR   Pharos; P29377; Tbio.
DR   PRO; PR:P29377; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P29377; Protein.
DR   Bgee; ENSG00000169906; Expressed in jejunal mucosa and 41 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
DR   CDD; cd00213; S-100; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
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:SF73; PROTEIN S100-G; 1.
DR   PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1.
DR   Pfam; PF00036; EF-hand_1; 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; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
DR   Genevisible; P29377; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Metal-binding; Phosphoprotein; Reference proteome;
KW   Repeat; Vitamin D.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02633"
FT   CHAIN           2..79
FT                   /note="Protein S100-G"
FT                   /id="PRO_0000144027"
FT   DOMAIN          13..48
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          45..79
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         26
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         31
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         58
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         60
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         62
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         64
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   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02633"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02634"
FT   CONFLICT        79
FT                   /note="Q -> S (in Ref. 3; AAA35637)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   79 AA;  9016 MW;  30416A681485B690 CRC64;
     MSTKKSPEEL KRIFEKYAAK EGDPDQLSKD ELKLLIQAEF PSLLKGPNTL DDLFQELDKN
     GDGEVSFEEF QVLVKKISQ
//