S100G_HUMAN
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 03-AUG-2022, entry version 173.
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; P29377; -.
DR PeptideAtlas; P29377; -.
DR PRIDE; P29377; -.
DR ProteomicsDB; 54565; -.
DR Antibodypedia; 4324; 77 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 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; 1558629at2759; -.
DR PhylomeDB; P29377; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; P29377; -.
DR SignaLink; P29377; -.
DR SIGNOR; P29377; -.
DR BioGRID-ORCS; 795; 45 hits in 634 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 tissues.
DR Genevisible; P29377; HS.
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 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 InterPro; IPR028489; S100G.
DR PANTHER; PTHR11639:SF73; PTHR11639:SF73; 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; 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 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
