ID   NUCB1_HUMAN             Reviewed;         461 AA.
AC   Q02818; B2RD64; Q15838; Q7Z4J7; Q9BUR1;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 4.
DT   27-MAR-2024, entry version 207.
DE   RecName: Full=Nucleobindin-1;
DE   AltName: Full=CALNUC;
DE   Flags: Precursor;
GN   Name=NUCB1; Synonyms=NUC;
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=1520323; DOI=10.1016/s0006-291x(05)81503-7;
RA   Miura K., Titani K., Kurosawa Y., Kanai Y.;
RT   "Molecular cloning of nucleobindin, a novel DNA-binding protein that
RT   contains both a signal peptide and a leucine zipper structure.";
RL   Biochem. Biophys. Res. Commun. 187:375-380(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS 13-LEU-PRO-14 DELINS SER AND
RP   GLN-399, AND SEQUENCE REVISION TO 299-300.
RC   TISSUE=Placenta;
RX   PubMed=8661046; DOI=10.1006/geno.1996.0263;
RA   Miura K., Hirai M., Kanai Y., Kurosawa Y.;
RT   "Organization of the human gene for nucleobindin (NUC) and its chromosomal
RT   assignment to 19q13.2-q13.4.";
RL   Genomics 34:181-186(1996).
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Umbilical cord blood;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [7]
RP   CHARACTERIZATION.
RX   PubMed=7589456; DOI=10.1016/0014-5793(95)01031-9;
RA   Mochizuki N., Hibi M., Kanai Y., Insel P.A.;
RT   "Interaction of the protein nucleobindin with G alpha i2, as revealed by
RT   the yeast two-hybrid system.";
RL   FEBS Lett. 373:155-158(1995).
RN   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22905912; DOI=10.1021/pr300539b;
RA   Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA   Mariman E.C., Renes J.;
RT   "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL   J. Proteome Res. 11:4733-4743(2012).
RN   [10]
RP   GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23234360; DOI=10.1021/pr300963h;
RA   Halim A., Ruetschi U., Larson G., Nilsson J.;
RT   "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT   of human cerebrospinal fluid glycoproteins.";
RL   J. Proteome Res. 12:573-584(2013).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-148, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   PHOSPHORYLATION AT SER-86; THR-148 AND SER-369.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
RN   [13]
RP   GBA MOTIF.
RX   PubMed=30194280; DOI=10.1074/jbc.ra118.003580;
RA   Maziarz M., Broselid S., DiGiacomo V., Park J.C., Luebbers A.,
RA   Garcia-Navarrete L., Blanco-Canosa J.B., Baillie G.S., Garcia-Marcos M.;
RT   "A biochemical and genetic discovery pipeline identifies PLCdelta4b as a
RT   nonreceptor activator of heterotrimeric G-proteins.";
RL   J. Biol. Chem. 293:16964-16983(2018).
RN   [14]
RP   STRUCTURE BY NMR OF 228-326, CALCIUM-BINDING, AND DOMAIN.
RX   PubMed=15287731; DOI=10.1021/bi049310a;
RA   de Alba E., Tjandra N.;
RT   "Structural studies on the Ca2+-binding domain of human nucleobindin
RT   (Calnuc).";
RL   Biochemistry 43:10039-10049(2004).
CC   -!- FUNCTION: Major calcium-binding protein of the Golgi which may have a
CC       role in calcium homeostasis (By similarity). Acts as a non-receptor
CC       guanine nucleotide exchange factor which binds to and activates alpha
CC       subunits of guanine nucleotide-binding proteins (G proteins) (By
CC       similarity). {ECO:0000250|UniProtKB:Q0P569,
CC       ECO:0000250|UniProtKB:Q63083}.
CC   -!- SUBUNIT: Interacts (via GBA motif) with guanine nucleotide-binding
CC       protein G(i) alpha subunits GNAI1, GNAI2 and GNAI3 with higher affinity
CC       for GNAI1 and GNAI3 than for GNAI2. Preferentially interacts with
CC       inactive rather than active GNAI3. Interaction with GNAI3 is inhibited
CC       when NUCB1 binds calcium, probably due to a conformational change which
CC       renders the GBA motif inaccessible. {ECO:0000250|UniProtKB:Q63083}.
CC   -!- INTERACTION:
CC       Q02818; P05067: APP; NbExp=3; IntAct=EBI-2622179, EBI-77613;
CC       Q02818; PRO_0000045603 [Q99IB8]; Xeno; NbExp=3; IntAct=EBI-2622179, EBI-6927928;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000250|UniProtKB:Q63083}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q63083}; Lumenal side
CC       {ECO:0000250|UniProtKB:Q63083}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q63083}. Secreted
CC       {ECO:0000250|UniProtKB:Q63083}. Note=A small fraction of the protein
CC       may be cytoplasmic. {ECO:0000250|UniProtKB:Q63083}.
CC   -!- TISSUE SPECIFICITY: Expressed both in fetal and adult heart, lung,
CC       liver, kidney and brain, and in adult skeletal muscle, placenta and
CC       pancreas.
CC   -!- DOMAIN: The EF-hand domains are unfolded in the absence of Ca(2+) and
CC       fold upon Ca(2+) addition. {ECO:0000269|PubMed:15287731}.
CC   -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC       to the alpha subunits of guanine nucleotide-binding proteins (G
CC       proteins). {ECO:0000269|PubMed:30194280}.
CC   -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
CC   -!- MISCELLANEOUS: Discovered as DNA-binding protein in the serum of lupus-
CC       prone mice.
CC   -!- SIMILARITY: Belongs to the nucleobindin family. {ECO:0000305}.
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DR   EMBL; M96824; AAA36383.1; -; mRNA.
DR   EMBL; U31342; AAB60431.1; -; Genomic_DNA.
DR   EMBL; U31336; AAB60431.1; JOINED; Genomic_DNA.
DR   EMBL; U31337; AAB60431.1; JOINED; Genomic_DNA.
DR   EMBL; U31338; AAB60431.1; JOINED; Genomic_DNA.
DR   EMBL; U31340; AAB60431.1; JOINED; Genomic_DNA.
DR   EMBL; U31341; AAB60431.1; JOINED; Genomic_DNA.
DR   EMBL; BT009828; AAP88830.1; -; mRNA.
DR   EMBL; AK315422; BAG37811.1; -; mRNA.
DR   EMBL; CH471177; EAW52411.1; -; Genomic_DNA.
DR   EMBL; BC002356; AAH02356.1; -; mRNA.
DR   CCDS; CCDS12740.1; -.
DR   RefSeq; NP_006175.2; NM_006184.5.
DR   RefSeq; XP_016882334.1; XM_017026845.1.
DR   PDB; 1SNL; NMR; -; A=228-326.
DR   PDBsum; 1SNL; -.
DR   AlphaFoldDB; Q02818; -.
DR   BMRB; Q02818; -.
DR   SMR; Q02818; -.
DR   BioGRID; 110978; 95.
DR   IntAct; Q02818; 35.
DR   MINT; Q02818; -.
DR   STRING; 9606.ENSP00000385923; -.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   GuidetoPHARMACOLOGY; 2871; -.
DR   GlyCosmos; Q02818; 4 sites, 7 glycans.
DR   GlyGen; Q02818; 24 sites, 8 O-linked glycans (19 sites).
DR   iPTMnet; Q02818; -.
DR   MetOSite; Q02818; -.
DR   PhosphoSitePlus; Q02818; -.
DR   SwissPalm; Q02818; -.
DR   BioMuta; NUCB1; -.
DR   DMDM; 90110780; -.
DR   EPD; Q02818; -.
DR   jPOST; Q02818; -.
DR   MassIVE; Q02818; -.
DR   MaxQB; Q02818; -.
DR   PaxDb; 9606-ENSP00000385923; -.
DR   PeptideAtlas; Q02818; -.
DR   ProteomicsDB; 58128; -.
DR   Pumba; Q02818; -.
DR   Antibodypedia; 2173; 352 antibodies from 30 providers.
DR   DNASU; 4924; -.
DR   Ensembl; ENST00000405315.9; ENSP00000385923.3; ENSG00000104805.17.
DR   Ensembl; ENST00000407032.5; ENSP00000385211.1; ENSG00000104805.17.
DR   Ensembl; ENST00000411700.6; ENSP00000410519.2; ENSG00000104805.17.
DR   Ensembl; ENST00000451312.6; ENSP00000397201.2; ENSG00000104805.17.
DR   Ensembl; ENST00000706746.1; ENSP00000516525.1; ENSG00000104805.17.
DR   GeneID; 4924; -.
DR   KEGG; hsa:4924; -.
DR   MANE-Select; ENST00000405315.9; ENSP00000385923.3; NM_006184.6; NP_006175.2.
DR   UCSC; uc002plb.5; human.
DR   AGR; HGNC:8043; -.
DR   CTD; 4924; -.
DR   DisGeNET; 4924; -.
DR   GeneCards; NUCB1; -.
DR   HGNC; HGNC:8043; NUCB1.
DR   HPA; ENSG00000104805; Low tissue specificity.
DR   MIM; 601323; gene.
DR   neXtProt; NX_Q02818; -.
DR   OpenTargets; ENSG00000104805; -.
DR   PharmGKB; PA31825; -.
DR   VEuPathDB; HostDB:ENSG00000104805; -.
DR   eggNOG; KOG3866; Eukaryota.
DR   GeneTree; ENSGT00390000001927; -.
DR   HOGENOM; CLU_031153_1_0_1; -.
DR   InParanoid; Q02818; -.
DR   OMA; VWEDTDK; -.
DR   OrthoDB; 2881246at2759; -.
DR   PhylomeDB; Q02818; -.
DR   TreeFam; TF323218; -.
DR   PathwayCommons; Q02818; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; Q02818; -.
DR   SIGNOR; Q02818; -.
DR   BioGRID-ORCS; 4924; 275 hits in 1151 CRISPR screens.
DR   ChiTaRS; NUCB1; human.
DR   EvolutionaryTrace; Q02818; -.
DR   GeneWiki; NUCB1; -.
DR   GenomeRNAi; 4924; -.
DR   Pharos; Q02818; Tchem.
DR   PRO; PR:Q02818; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q02818; Protein.
DR   Bgee; ENSG00000104805; Expressed in stromal cell of endometrium and 197 other cell types or tissues.
DR   ExpressionAtlas; Q02818; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
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; IPR040250; Nucleobindin.
DR   PANTHER; PTHR19237; NUCLEOBINDIN; 1.
DR   PANTHER; PTHR19237:SF21; NUCLEOBINDIN-1; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   Genevisible; Q02818; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Coiled coil; Cytoplasm; DNA-binding; Glycoprotein;
KW   Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250|UniProtKB:Q0P569"
FT   CHAIN           27..461
FT                   /note="Nucleobindin-1"
FT                   /id="PRO_0000004162"
FT   DOMAIN          240..275
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          292..327
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DNA_BIND        172..218
FT                   /evidence="ECO:0000255"
FT   REGION          42..51
FT                   /note="O-glycosylated at one site"
FT   REGION          193..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..321
FT                   /note="Binds to GNAI2 and GNAI3"
FT                   /evidence="ECO:0000250"
FT   REGION          368..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          150..218
FT                   /evidence="ECO:0000255"
FT   COILED          341..407
FT                   /evidence="ECO:0000255"
FT   MOTIF           303..333
FT                   /note="GBA"
FT                   /evidence="ECO:0000269|PubMed:30194280"
FT   COMPBIAS        193..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15287731"
FT   BINDING         255
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15287731"
FT   BINDING         257
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15287731"
FT   BINDING         264
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15287731"
FT   BINDING         305
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15287731"
FT   BINDING         307
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15287731"
FT   BINDING         309
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15287731"
FT   BINDING         316
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15287731"
FT   MOD_RES         86
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         148
FT                   /note="Phosphothreonine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         369
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   VARIANT         13..14
FT                   /note="LP -> S"
FT                   /evidence="ECO:0000269|PubMed:8661046"
FT                   /id="VAR_012151"
FT   VARIANT         338
FT                   /note="M -> V (in dbSNP:rs35456905)"
FT                   /id="VAR_061087"
FT   VARIANT         399
FT                   /note="R -> Q (in dbSNP:rs200372110)"
FT                   /evidence="ECO:0000269|PubMed:8661046"
FT                   /id="VAR_012152"
FT   CONFLICT        299..300
FT                   /note="HV -> QL (in Ref. 1; AAA36383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="Q -> K (in Ref. 1; AAA36383 and 2; AAB60431)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        390..391
FT                   /note="QQ -> LL (in Ref. 1; AAA36383 and 2; AAB60431)"
FT                   /evidence="ECO:0000305"
FT   HELIX           245..252
FT                   /evidence="ECO:0007829|PDB:1SNL"
FT   STRAND          258..261
FT                   /evidence="ECO:0007829|PDB:1SNL"
FT   HELIX           262..274
FT                   /evidence="ECO:0007829|PDB:1SNL"
FT   HELIX           285..288
FT                   /evidence="ECO:0007829|PDB:1SNL"
FT   HELIX           291..303
FT                   /evidence="ECO:0007829|PDB:1SNL"
FT   STRAND          309..313
FT                   /evidence="ECO:0007829|PDB:1SNL"
FT   HELIX           314..322
FT                   /evidence="ECO:0007829|PDB:1SNL"
SQ   SEQUENCE   461 AA;  53879 MW;  913C4B87C2A644C5 CRC64;
     MPPSGPRGTL LLLPLLLLLL LRAVLAVPLE RGAPNKEETP ATESPDTGLY YHRYLQEVID
     VLETDGHFRE KLQAANAEDI KSGKLSRELD FVSHHVRTKL DELKRQEVSR LRMLLKAKMD
     AEQDPNVQVD HLNLLKQFEH LDPQNQHTFE ARDLELLIQT ATRDLAQYDA AHHEEFKRYE
     MLKEHERRRY LESLGEEQRK EAERKLEEQQ RRHREHPKVN VPGSQAQLKE VWEELDGLDP
     NRFNPKTFFI LHDINSDGVL DEQELEALFT KELEKVYDPK NEEDDMREME EERLRMREHV
     MKNVDTNQDR LVTLEEFLAS TQRKEFGDTG EGWETVEMHP AYTEEELRRF EEELAAREAE
     LNAKAQRLSQ ETEALGRSQG RLEAQKRELQ QAVLHMEQRK QQQQQQQGHK APAAHPEGQL
     KFHPDTDDVP VPAPAGDQKE VDTSEKKLLE RLPEVEVPQH L
//