ID   RCN1_HUMAN              Reviewed;         331 AA.
AC   Q15293; B7Z1M1; D3DR00;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 203.
DE   RecName: Full=Reticulocalbin-1;
DE   Flags: Precursor;
GN   Name=RCN1; Synonyms=RCN;
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).
RX   PubMed=8586628; DOI=10.1093/oxfordjournals.jbchem.a124815;
RA   Ozawa M.;
RT   "Cloning of a human homologue of mouse reticulocalbin reveals conservation
RT   of structural domains in the novel endoplasmic reticulum resident Ca(2+)-
RT   binding protein with multiple EF-hand motifs.";
RL   J. Biochem. 117:1113-1119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Cerebellum;
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   [3]
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   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Ovary;
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   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76, 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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-76 AND SER-80, AND
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   [10]
RP   PHOSPHORYLATION AT SER-80.
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   [11]
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   [12]
RP   GLYCOSYLATION.
RX   PubMed=28512129; DOI=10.1074/jbc.m117.794487;
RA   Larsen I.S.B., Narimatsu Y., Joshi H.J., Yang Z., Harrison O.J., Brasch J.,
RA   Shapiro L., Honig B., Vakhrushev S.Y., Clausen H., Halim A.;
RT   "Mammalian O-mannosylation of cadherins and plexins is independent of
RT   protein O-mannosyltransferases 1 and 2.";
RL   J. Biol. Chem. 292:11586-11598(2017).
RN   [13]
RP   VARIANT [LARGE SCALE ANALYSIS] LEU-117.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May regulate calcium-dependent activities in the endoplasmic
CC       reticulum lumen or post-ER compartment.
CC   -!- INTERACTION:
CC       Q15293; Q12797-6: ASPH; NbExp=3; IntAct=EBI-948278, EBI-12092171;
CC       Q15293; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-948278, EBI-1166928;
CC       Q15293; P54253: ATXN1; NbExp=9; IntAct=EBI-948278, EBI-930964;
CC       Q15293; P46379-2: BAG6; NbExp=3; IntAct=EBI-948278, EBI-10988864;
CC       Q15293; O15182: CETN3; NbExp=5; IntAct=EBI-948278, EBI-712959;
CC       Q15293; Q8TEB1: DCAF11; NbExp=5; IntAct=EBI-948278, EBI-2213388;
CC       Q15293; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-948278, EBI-12593112;
CC       Q15293; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-948278, EBI-743105;
CC       Q15293; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-948278, EBI-744099;
CC       Q15293; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-948278, EBI-1752811;
CC       Q15293; O95257: GADD45G; NbExp=3; IntAct=EBI-948278, EBI-448202;
CC       Q15293; O43681: GET3; NbExp=5; IntAct=EBI-948278, EBI-2515857;
CC       Q15293; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-948278, EBI-740290;
CC       Q15293; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-948278, EBI-14103818;
CC       Q15293; P42858: HTT; NbExp=3; IntAct=EBI-948278, EBI-466029;
CC       Q15293; O14901: KLF11; NbExp=3; IntAct=EBI-948278, EBI-948266;
CC       Q15293; P25800: LMO1; NbExp=3; IntAct=EBI-948278, EBI-8639312;
CC       Q15293; P25791-3: LMO2; NbExp=3; IntAct=EBI-948278, EBI-11959475;
CC       Q15293; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-948278, EBI-11742507;
CC       Q15293; P61968: LMO4; NbExp=3; IntAct=EBI-948278, EBI-2798728;
CC       Q15293; O43765: SGTA; NbExp=3; IntAct=EBI-948278, EBI-347996;
CC       Q15293; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-948278, EBI-744081;
CC       Q15293; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-948278, EBI-5235340;
CC       Q15293; P51687: SUOX; NbExp=3; IntAct=EBI-948278, EBI-3921347;
CC       Q15293; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-948278, EBI-11741890;
CC       Q15293; PRO_0000449619 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-948278, EBI-25475847;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q15293-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15293-2; Sequence=VSP_055511;
CC   -!- PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by
CC       POMGNT1. {ECO:0000269|PubMed:28512129}.
CC   -!- MISCELLANEOUS: This protein has four functional calcium-binding sites;
CC       potential sites II and VI have lost affinity for calcium.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}.
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DR   EMBL; D42073; BAA07670.1; -; mRNA.
DR   EMBL; AK293652; BAH11557.1; -; mRNA.
DR   EMBL; AL035078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL049635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL078612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL138970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z95332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471064; EAW68227.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68228.1; -; Genomic_DNA.
DR   EMBL; BC010120; AAH10120.1; -; mRNA.
DR   CCDS; CCDS7876.1; -. [Q15293-1]
DR   PIR; JC4173; JC4173.
DR   RefSeq; NP_002892.1; NM_002901.2. [Q15293-1]
DR   AlphaFoldDB; Q15293; -.
DR   BioGRID; 111887; 275.
DR   ELM; Q15293; -.
DR   IntAct; Q15293; 125.
DR   MINT; Q15293; -.
DR   STRING; 9606.ENSP00000054950; -.
DR   GlyConnect; 1712; 21 N-Linked glycans (1 site).
DR   GlyCosmos; Q15293; 2 sites, 22 glycans.
DR   GlyGen; Q15293; 5 sites, 28 N-linked glycans (1 site), 2 O-linked glycans (4 sites).
DR   iPTMnet; Q15293; -.
DR   MetOSite; Q15293; -.
DR   PhosphoSitePlus; Q15293; -.
DR   BioMuta; RCN1; -.
DR   DMDM; 2493462; -.
DR   CPTAC; CPTAC-266; -.
DR   CPTAC; CPTAC-267; -.
DR   EPD; Q15293; -.
DR   jPOST; Q15293; -.
DR   MassIVE; Q15293; -.
DR   MaxQB; Q15293; -.
DR   PaxDb; 9606-ENSP00000054950; -.
DR   PeptideAtlas; Q15293; -.
DR   ProteomicsDB; 60519; -. [Q15293-1]
DR   ProteomicsDB; 6347; -.
DR   Pumba; Q15293; -.
DR   TopDownProteomics; Q15293-1; -. [Q15293-1]
DR   Antibodypedia; 25609; 152 antibodies from 23 providers.
DR   DNASU; 5954; -.
DR   Ensembl; ENST00000054950.4; ENSP00000054950.4; ENSG00000049449.10. [Q15293-1]
DR   GeneID; 5954; -.
DR   KEGG; hsa:5954; -.
DR   MANE-Select; ENST00000054950.4; ENSP00000054950.4; NM_002901.4; NP_002892.1.
DR   UCSC; uc058acp.1; human. [Q15293-1]
DR   AGR; HGNC:9934; -.
DR   CTD; 5954; -.
DR   DisGeNET; 5954; -.
DR   GeneCards; RCN1; -.
DR   HGNC; HGNC:9934; RCN1.
DR   HPA; ENSG00000049449; Tissue enriched (epididymis).
DR   MIM; 602735; gene.
DR   neXtProt; NX_Q15293; -.
DR   OpenTargets; ENSG00000049449; -.
DR   PharmGKB; PA34303; -.
DR   VEuPathDB; HostDB:ENSG00000049449; -.
DR   eggNOG; KOG4223; Eukaryota.
DR   GeneTree; ENSGT01010000222360; -.
DR   HOGENOM; CLU_044718_0_1_1; -.
DR   InParanoid; Q15293; -.
DR   OMA; DRPGFQY; -.
DR   OrthoDB; 4490703at2759; -.
DR   PhylomeDB; Q15293; -.
DR   TreeFam; TF314849; -.
DR   PathwayCommons; Q15293; -.
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; Q15293; -.
DR   BioGRID-ORCS; 5954; 35 hits in 1149 CRISPR screens.
DR   ChiTaRS; RCN1; human.
DR   GeneWiki; RCN1; -.
DR   GenomeRNAi; 5954; -.
DR   Pharos; Q15293; Tbio.
DR   PRO; PR:Q15293; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q15293; Protein.
DR   Bgee; ENSG00000049449; Expressed in corpus epididymis and 204 other cell types or tissues.
DR   ExpressionAtlas; Q15293; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   CDD; cd16229; EFh_CREC_RCN1; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 3.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR027241; Rcn1.
DR   PANTHER; PTHR10827; RETICULOCALBIN; 1.
DR   PANTHER; PTHR10827:SF17; RETICULOCALBIN-1; 1.
DR   Pfam; PF13202; EF-hand_5; 2.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 6.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; Q15293; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Endoplasmic reticulum; Glycoprotein;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..331
FT                   /note="Reticulocalbin-1"
FT                   /id="PRO_0000004145"
FT   DOMAIN          79..114
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          115..150
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          166..201
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          203..238
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          244..279
FT                   /note="EF-hand 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          280..315
FT                   /note="EF-hand 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOTIF           328..331
FT                   /note="Prevents secretion from ER"
FT   BINDING         92
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         128
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         179
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         185
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         190
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         220
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         257
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         259
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         261
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         263
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         268
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         293
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000305"
FT   BINDING         295
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000305"
FT   BINDING         297
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000305"
FT   BINDING         299
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000305"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         76
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         80
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039,
FT                   ECO:0007744|PubMed:24275569"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   VAR_SEQ         1..85
FT                   /note="MARGGRGRRLGLALGLLLALVLAPRVLRAKPTVRKERVVRPDSELGERPPED
FT                   NQSFQYDHEAFLGKEDSKTFDQLTPDESKERLG -> MTGGEGPLPTAKQATCSPPSSR
FT                   ERNPRRRGSRPR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055511"
FT   VARIANT         73
FT                   /note="D -> Y (in dbSNP:rs1804281)"
FT                   /id="VAR_011965"
FT   VARIANT         117
FT                   /note="F -> L (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035460"
SQ   SEQUENCE   331 AA;  38890 MW;  608AAD536963F789 CRC64;
     MARGGRGRRL GLALGLLLAL VLAPRVLRAK PTVRKERVVR PDSELGERPP EDNQSFQYDH
     EAFLGKEDSK TFDQLTPDES KERLGKIVDR IDNDGDGFVT TEELKTWIKR VQKRYIFDNV
     AKVWKDYDRD KDDKISWEEY KQATYGYYLG NPAEFHDSSD HHTFKKMLPR DERRFKAADL
     NGDLTATREE FTAFLHPEEF EHMKEIVVLE TLEDIDKNGD GFVDQDEYIA DMFSHEENGP
     EPDWVLSERE QFNEFRDLNK DGKLDKDEIR HWILPQDYDH AQAEARHLVY ESDKNKDEKL
     TKEEILENWN MFVGSQATNY GEDLTKNHDE L
//