ID RCN1_MOUSE Reviewed; 325 AA. AC Q05186; Q3TVU3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 24-JAN-2024, entry version 186. DE RecName: Full=Reticulocalbin-1; DE Flags: Precursor; GN Name=Rcn1; Synonyms=Rca1, Rcn; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8416973; DOI=10.1016/s0021-9258(18)54208-3; RA Ozawa M., Muramatsu T.; RT "Reticulocalbin, a novel endoplasmic reticulum resident Ca(2+)-binding RT protein with multiple EF-hand motifs and a carboxyl-terminal HDEL RT sequence."; RL J. Biol. Chem. 268:699-705(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; TISSUE=Liver; RX PubMed=8537305; DOI=10.1093/oxfordjournals.jbchem.a124871; RA Ozawa M.; RT "Structure of the gene encoding mouse reticulocalbin, a novel endoplasmic RT reticulum-resident Ca(2+)-binding protein with multiple EF-hand motifs."; RL J. Biochem. 118:154-160(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP PROTEIN SEQUENCE OF 24-39. RC TISSUE=Fibroblast; RX PubMed=7523108; DOI=10.1002/elps.11501501101; RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.; RT "Separation and sequencing of familiar and novel murine proteins using RT preparative two-dimensional gel electrophoresis."; RL Electrophoresis 15:735-745(1994). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and RC Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: May regulate calcium-dependent activities in the endoplasmic CC reticulum lumen or post-ER compartment. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by CC POMGNT1. {ECO:0000250|UniProtKB:Q15293}. CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites; CC potential sites II and VI have lost affinity for calcium. CC -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D13003; BAA02366.1; -; mRNA. DR EMBL; D43956; BAA07896.1; -; Genomic_DNA. DR EMBL; BC049108; AAH49108.1; -; mRNA. DR EMBL; AK017494; BAB30773.1; -; mRNA. DR EMBL; AK133971; BAE21962.1; -; mRNA. DR EMBL; AK159973; BAE35525.1; -; mRNA. DR CCDS; CCDS16498.1; -. DR PIR; A45337; A45337. DR RefSeq; NP_033063.1; NM_009037.2. DR AlphaFoldDB; Q05186; -. DR BioGRID; 202839; 8. DR STRING; 10090.ENSMUSP00000006128; -. DR GlyConnect; 2679; 12 N-Linked glycans (1 site). DR GlyCosmos; Q05186; 1 site, 11 glycans. DR GlyGen; Q05186; 1 site, 12 N-linked glycans (1 site). DR iPTMnet; Q05186; -. DR PhosphoSitePlus; Q05186; -. DR REPRODUCTION-2DPAGE; IPI00137831; -. DR EPD; Q05186; -. DR jPOST; Q05186; -. DR MaxQB; Q05186; -. DR PaxDb; 10090-ENSMUSP00000006128; -. DR PeptideAtlas; Q05186; -. DR ProteomicsDB; 255056; -. DR Pumba; Q05186; -. DR Antibodypedia; 25609; 152 antibodies from 23 providers. DR DNASU; 19672; -. DR Ensembl; ENSMUST00000006128.7; ENSMUSP00000006128.7; ENSMUSG00000005973.7. DR GeneID; 19672; -. DR KEGG; mmu:19672; -. DR UCSC; uc008lks.1; mouse. DR AGR; MGI:104559; -. DR CTD; 5954; -. DR MGI; MGI:104559; Rcn1. DR VEuPathDB; HostDB:ENSMUSG00000005973; -. DR eggNOG; KOG4223; Eukaryota. DR GeneTree; ENSGT01010000222360; -. DR HOGENOM; CLU_044718_0_1_1; -. DR InParanoid; Q05186; -. DR OMA; DRPGFQY; -. DR OrthoDB; 4490703at2759; -. DR PhylomeDB; Q05186; -. DR TreeFam; TF314849; -. DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation. DR BioGRID-ORCS; 19672; 4 hits in 78 CRISPR screens. DR ChiTaRS; Rcn1; mouse. DR PRO; PR:Q05186; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q05186; Protein. DR Bgee; ENSMUSG00000005973; Expressed in seminal vesicle and 262 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0043010; P:camera-type eye development; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. 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; 3. DR PROSITE; PS50222; EF_HAND_2; 6. DR PROSITE; PS00014; ER_TARGET; 1. DR Genevisible; Q05186; MM. PE 1: Evidence at protein level; KW Calcium; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:7523108" FT CHAIN 24..325 FT /note="Reticulocalbin-1" FT /id="PRO_0000004146" FT DOMAIN 73..108 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 109..144 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 160..195 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 197..232 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 238..273 FT /note="EF-hand 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 274..309 FT /note="EF-hand 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOTIF 322..325 FT /note="Prevents secretion from ER" FT BINDING 86 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 88 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 97 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 122 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 124 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 126 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 128 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 133 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 173 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 175 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 177 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 179 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 184 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 212 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 214 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 251 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 253 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 255 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" 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 262 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 287 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000305" FT BINDING 289 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000305" FT BINDING 291 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000305" FT BINDING 293 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000305" FT BINDING 298 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000305" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15293" FT MOD_RES 74 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15293" FT CARBOHYD 47 FT /note="N-linked (GlcNAc...) asparagine; partial" FT CONFLICT 24 FT /note="K -> G (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 34 FT /note="R -> I (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 37..39 FT /note="SEL -> DEE (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 325 AA; 38113 MW; 0470B10B5A8BC76D CRC64; MARGGRLGLA LGLLLALVLA LRAKPTVRKE RVVRPDSELG ERPPEDNQSF QYDHEAFLGK EDSKTFDQLS PDESKERLGK IVDRIDSDGD GLVTTEELKL WIKRVQKRYI YDNVAKVWKD YDRDKDEKIS WEEYKQATYG YYLGNPAEFH DSSDHHTFKK MLPRDERRFK ASDLDGDLTA TREEFTAFLH PEEFEHMKEI VVLETLEDID KNGDGFVDQD EYIADMFSHE DNGPEPDWVL SEREQFNDFR DLNKDGKLDK DEIRHWILPQ DYDHAQAEAR HLVYESDKNK DEMLTKEEIL DNWNMFVGSQ ATNYGEDLTK NHDEL //