NUCB2_HUMAN
ID NUCB2_HUMAN Reviewed; 420 AA.
AC P80303; A8K642; D3DQX5; Q8NFT5; V9HW75;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Nucleobindin-2 {ECO:0000305};
DE AltName: Full=DNA-binding protein NEFA;
DE AltName: Full=Epididymis secretory protein Li 109 {ECO:0000303|Ref.6};
DE AltName: Full=Gastric cancer antigen Zg4;
DE AltName: Full=Prepronesfatin;
DE Contains:
DE RecName: Full=Nesfatin-1;
DE Flags: Precursor;
GN Name=NUCB2 {ECO:0000312|HGNC:HGNC:8044}; Synonyms=NEFA;
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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Blood;
RX PubMed=7811391; DOI=10.1515/bchm3.1994.375.8.497;
RA Barnikol-Watanabe S., Gross N.A., Goetz H., Henkel T., Karabinos A.,
RA Kratzin H., Barnikol H.U., Hilschmann N.;
RT "Human protein NEFA, a novel DNA binding/EF-hand/leucine zipper protein.
RT Molecular cloning and sequence analysis of the cDNA, isolation and
RT characterization of the protein.";
RL Biol. Chem. Hoppe-Seyler 375:497-512(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9639681; DOI=10.1016/s0925-4439(98)00025-8;
RA Deangelis M.M., Doucet J.P., Drury S., Sherry S.T., Robichaux M.B., Den Z.,
RA Pelias M.Z., Ditta G.M., Keats B.J., Deininger P.L., Batzer M.A.;
RT "Assembly of a high-resolution map of the Acadian Usher syndrome region and
RT localization of the nuclear EF-hand acidic gene.";
RL Biochim. Biophys. Acta 1407:84-91(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP GLN-402 DEL.
RX PubMed=12087473; DOI=10.1038/sj.bjc.6600321;
RA Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.;
RT "Serological identification and expression analysis of gastric cancer-
RT associated genes.";
RL Br. J. Cancer 86:1824-1830(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20427483; DOI=10.1210/en.2009-1169;
RA Yamada M., Horiguchi K., Umezawa R., Hashimoto K., Satoh T., Ozawa A.,
RA Shibusawa N., Monden T., Okada S., Shimizu H., Mori M.;
RT "Troglitazone, a ligand of peroxisome proliferator-activated receptor-
RT gamma, stabilizes NUCB2 (Nesfatin) mRNA by activating the ERK1/2 pathway:
RT isolation and characterization of the human NUCB2 gene.";
RL Endocrinology 151:2494-2503(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-402
RP DEL.
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Li J., Wang H., Liu J., Liu F.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11749975; DOI=10.1016/s0014-5793(01)03187-8;
RA Nesselhut J., Jurgan U., Onken E., Gotz H., Barnikol H.U., Hirschfeld G.,
RA Barnikol-Watanabe S., Hilschmann N.;
RT "Golgi retention of human protein NEFA is mediated by its N-terminal
RT Leu/Ile-rich region.";
RL FEBS Lett. 509:469-475(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP IDENTIFICATION BY 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 [14]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-24, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
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).
CC -!- FUNCTION: Calcium-binding protein which may have a role in calcium
CC homeostasis (By similarity). Acts as a non-receptor guanine nucleotide
CC exchange factor which binds to and activates guanine nucleotide-binding
CC protein (G-protein) alpha subunit GNAI3 (By similarity).
CC {ECO:0000250|UniProtKB:P81117, ECO:0000250|UniProtKB:Q9JI85}.
CC -!- FUNCTION: [Nesfatin-1]: Anorexigenic peptide, seems to play an
CC important role in hypothalamic pathways regulating food intake and
CC energy homeostasis, acting in a leptin-independent manner. May also
CC exert hypertensive roles and modulate blood pressure through directly
CC acting on peripheral arterial resistance.
CC {ECO:0000250|UniProtKB:Q9JI85}.
CC -!- SUBUNIT: Interacts (via GBA motif) with guanine nucleotide-binding
CC protein G(i) alpha subunit GNAI3 (By similarity). Preferentially
CC interacts with inactive rather than active GNAI3 (By similarity).
CC Interaction with GNAI3 is inhibited when NUCB2 binds calcium, probably
CC due to a conformational change which renders the GBA motif inaccessible
CC (By similarity). Binds to the postmitotic growth suppressor NDN;
CC coexpression abolishes NUCB2 secretion (By similarity).
CC {ECO:0000250|UniProtKB:P81117, ECO:0000250|UniProtKB:Q9JI85}.
CC -!- INTERACTION:
CC P80303; P24522: GADD45A; NbExp=2; IntAct=EBI-2296670, EBI-448167;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11749975}.
CC Membrane {ECO:0000269|PubMed:11749975}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11749975}. Cytoplasm {ECO:0000269|PubMed:11749975}.
CC Secreted {ECO:0000269|PubMed:11749975}. Endoplasmic reticulum
CC {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Golgi retention is
CC mediated by its N-terminal region.
CC -!- SUBCELLULAR LOCATION: [Nesfatin-1]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P80303-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P80303-2; Sequence=VSP_036450;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in spleen, testis and
CC normal stomach. {ECO:0000269|PubMed:12087473}.
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 -!- POLYMORPHISM: Deletion of Gln-402 is frequent.
CC {ECO:0000305|PubMed:12087473}.
CC -!- MISCELLANEOUS: NEFA stands for N=DNA-binding; EF=EF-hand; A=Acidic
CC region.
CC -!- SIMILARITY: Belongs to the nucleobindin family. {ECO:0000305}.
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DR EMBL; X76732; CAA54148.1; -; mRNA.
DR EMBL; AF052642; AAC06300.1; -; mRNA.
DR EMBL; AF052643; AAC06301.1; -; mRNA.
DR EMBL; AF052644; AAC06302.1; -; mRNA.
DR EMBL; AF450266; AAM73810.1; -; mRNA.
DR EMBL; AB478625; BAJ09615.1; -; Genomic_DNA.
DR EMBL; AK291507; BAF84196.1; -; mRNA.
DR EMBL; FJ224327; ACI46019.1; -; mRNA.
DR EMBL; AC107956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF455328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68439.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68440.1; -; Genomic_DNA.
DR CCDS; CCDS41623.1; -. [P80303-1]
DR PIR; S55272; S55272.
DR RefSeq; NP_005004.1; NM_005013.2. [P80303-1]
DR RefSeq; XP_016873295.1; XM_017017806.1.
DR RefSeq; XP_016873296.1; XM_017017807.1.
DR RefSeq; XP_016873297.1; XM_017017808.1.
DR RefSeq; XP_016873298.1; XM_017017809.1.
DR RefSeq; XP_016873299.1; XM_017017810.1.
DR RefSeq; XP_016873300.1; XM_017017811.1.
DR RefSeq; XP_016873301.1; XM_017017812.1. [P80303-1]
DR RefSeq; XP_016873302.1; XM_017017813.1. [P80303-1]
DR RefSeq; XP_016873303.1; XM_017017814.1. [P80303-1]
DR RefSeq; XP_016873304.1; XM_017017815.1. [P80303-1]
DR RefSeq; XP_016873305.1; XM_017017816.1.
DR RefSeq; XP_016873306.1; XM_017017817.1. [P80303-1]
DR RefSeq; XP_016873307.1; XM_017017818.1. [P80303-1]
DR RefSeq; XP_016873308.1; XM_017017819.1.
DR AlphaFoldDB; P80303; -.
DR SMR; P80303; -.
DR BioGRID; 110979; 76.
DR IntAct; P80303; 22.
DR MINT; P80303; -.
DR STRING; 9606.ENSP00000436455; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR GlyGen; P80303; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P80303; -.
DR MetOSite; P80303; -.
DR PhosphoSitePlus; P80303; -.
DR BioMuta; NUCB2; -.
DR DMDM; 224471846; -.
DR EPD; P80303; -.
DR jPOST; P80303; -.
DR MassIVE; P80303; -.
DR PaxDb; P80303; -.
DR PeptideAtlas; P80303; -.
DR PRIDE; P80303; -.
DR ProteomicsDB; 57677; -. [P80303-1]
DR ProteomicsDB; 57678; -. [P80303-2]
DR Antibodypedia; 1610; 314 antibodies from 29 providers.
DR DNASU; 4925; -.
DR Ensembl; ENST00000323688.10; ENSP00000320168.6; ENSG00000070081.18. [P80303-2]
DR Ensembl; ENST00000529010.6; ENSP00000436455.1; ENSG00000070081.18. [P80303-1]
DR GeneID; 4925; -.
DR KEGG; hsa:4925; -.
DR MANE-Select; ENST00000529010.6; ENSP00000436455.1; NM_005013.4; NP_005004.1.
DR UCSC; uc001mmw.4; human.
DR CTD; 4925; -.
DR DisGeNET; 4925; -.
DR GeneCards; NUCB2; -.
DR HGNC; HGNC:8044; NUCB2.
DR HPA; ENSG00000070081; Tissue enhanced (pancreas, salivary gland).
DR MIM; 608020; gene.
DR neXtProt; NX_P80303; -.
DR OpenTargets; ENSG00000070081; -.
DR PharmGKB; PA31826; -.
DR VEuPathDB; HostDB:ENSG00000070081; -.
DR eggNOG; KOG3866; Eukaryota.
DR GeneTree; ENSGT00390000001927; -.
DR InParanoid; P80303; -.
DR OMA; KMCWSRA; -.
DR OrthoDB; 1339224at2759; -.
DR PhylomeDB; P80303; -.
DR TreeFam; TF323218; -.
DR PathwayCommons; P80303; -.
DR SignaLink; P80303; -.
DR BioGRID-ORCS; 4925; 29 hits in 1085 CRISPR screens.
DR ChiTaRS; NUCB2; human.
DR GeneWiki; NUCB2; -.
DR GenomeRNAi; 4925; -.
DR Pharos; P80303; Tbio.
DR PRO; PR:P80303; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P80303; protein.
DR Bgee; ENSG00000070081; Expressed in parotid gland and 206 other tissues.
DR ExpressionAtlas; P80303; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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; IDA:HPA.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
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:0032099; P:negative regulation of appetite; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028813; NUCB2.
DR InterPro; IPR040250; Nucleobindin.
DR PANTHER; PTHR19237; PTHR19237; 1.
DR PANTHER; PTHR19237:SF22; PTHR19237:SF22; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cleavage on pair of basic residues;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Endoplasmic reticulum;
KW Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 25..420
FT /note="Nucleobindin-2"
FT /id="PRO_0000004165"
FT CHAIN 25..106
FT /note="Nesfatin-1"
FT /id="PRO_0000419819"
FT DOMAIN 241..276
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 293..328
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DNA_BIND 171..223
FT /evidence="ECO:0000250"
FT REGION 195..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..420
FT /note="Binds to necdin"
FT /evidence="ECO:0000250"
FT REGION 398..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 304..334
FT /note="GBA"
FT /evidence="ECO:0000269|PubMed:30194280"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 419..420
FT /note="HI -> RV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036450"
FT VARIANT 338
FT /note="Q -> E (in dbSNP:rs757081)"
FT /id="VAR_024399"
FT VARIANT 402
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:12087473,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_020923"
FT CONFLICT 150
FT /note="F -> L (in Ref. 5; BAF84196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 50223 MW; ABA74587B72C33FE CRC64;
MRWRTILLQY CFLLITCLLT ALEAVPIDID KTKVQNIHPV ESAKIEPPDT GLYYDEYLKQ
VIDVLETDKH FREKLQKADI EEIKSGRLSK ELDLVSHHVR TKLDELKRQE VGRLRMLIKA
KLDSLQDIGM DHQALLKQFD HLNHLNPDKF ESTDLDMLIK AATSDLEHYD KTRHEEFKKY
EMMKEHERRE YLKTLNEEKR KEEESKFEEM KKKHENHPKV NHPGSKDQLK EVWEETDGLD
PNDFDPKTFF KLHDVNSDGF LDEQELEALF TKELEKVYDP KNEEDDMVEM EEERLRMREH
VMNEVDTNKD RLVTLEEFLK ATEKKEFLEP DSWETLDQQQ FFTEEELKEY ENIIALQENE
LKKKADELQK QKEELQRQHD QLEAQKLEYH QVIQQMEQKK LQQGIPPSGP AGELKFEPHI
