ID   CREG1_MOUSE             Reviewed;         220 AA.
AC   O88668; Q3UNP8; Q8C3I1;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Protein CREG1;
DE   AltName: Full=Cellular repressor of E1A-stimulated genes 1;
DE   Flags: Precursor;
GN   Name=Creg1; Synonyms=Creg;
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=9710587; DOI=10.1128/mcb.18.9.5032;
RA   Veal E., Eisenstein M., Tseng Z.H., Gill G.;
RT   "A cellular repressor of E1A-stimulated genes that inhibits activation by
RT   E2F.";
RL   Mol. Cell. Biol. 18:5032-5041(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Kidney, Liver, and Placenta;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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   TISSUE SPECIFICITY, INDUCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=10815803; DOI=10.1038/sj.onc.1203529;
RA   Veal E., Groisman R., Eisenstein M., Gill G.;
RT   "The secreted glycoprotein CREG enhances differentiation of NTERA-2 human
RT   embryonal carcinoma cells.";
RL   Oncogene 19:2120-2128(2000).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Spleen, and 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 contribute to the transcriptional control of cell growth
CC       and differentiation. Antagonizes transcriptional activation and
CC       cellular transformation by the adenovirus E1A protein. The
CC       transcriptional control activity of cell growth requires interaction
CC       with IGF2R (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with IGF2R; the interaction is dependent
CC       on glycosylation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10815803}.
CC   -!- DEVELOPMENTAL STAGE: Found at low level from 7 dpc and increased during
CC       embryonic development. {ECO:0000269|PubMed:10815803}.
CC   -!- INDUCTION: Induced during differentiation.
CC       {ECO:0000269|PubMed:10815803}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CREG family. {ECO:0000305}.
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DR   EMBL; AF084524; AAC34862.1; -; mRNA.
DR   EMBL; AK005388; BAB23994.1; -; mRNA.
DR   EMBL; AK010947; BAB27285.1; -; mRNA.
DR   EMBL; AK085844; BAC39549.1; -; mRNA.
DR   EMBL; AK144101; BAE25699.1; -; mRNA.
DR   EMBL; BC027426; AAH27426.1; -; mRNA.
DR   CCDS; CCDS35759.1; -.
DR   RefSeq; NP_035934.1; NM_011804.2.
DR   RefSeq; XP_006496993.1; XM_006496930.1.
DR   AlphaFoldDB; O88668; -.
DR   SMR; O88668; -.
DR   BioGRID; 241197; 3.
DR   STRING; 10090.ENSMUSP00000107060; -.
DR   GlyConnect; 2620; 5 N-Linked glycans (1 site).
DR   GlyCosmos; O88668; 2 sites, 5 glycans.
DR   GlyGen; O88668; 3 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; O88668; -.
DR   PhosphoSitePlus; O88668; -.
DR   EPD; O88668; -.
DR   jPOST; O88668; -.
DR   MaxQB; O88668; -.
DR   PaxDb; 10090-ENSMUSP00000107060; -.
DR   PeptideAtlas; O88668; -.
DR   ProteomicsDB; 285306; -.
DR   Pumba; O88668; -.
DR   Antibodypedia; 20531; 361 antibodies from 34 providers.
DR   DNASU; 433375; -.
DR   Ensembl; ENSMUST00000111432.10; ENSMUSP00000107060.4; ENSMUSG00000040713.13.
DR   GeneID; 433375; -.
DR   KEGG; mmu:433375; -.
DR   UCSC; uc007djm.1; mouse.
DR   AGR; MGI:1344382; -.
DR   CTD; 8804; -.
DR   MGI; MGI:1344382; Creg1.
DR   VEuPathDB; HostDB:ENSMUSG00000040713; -.
DR   eggNOG; KOG3374; Eukaryota.
DR   GeneTree; ENSGT00390000005914; -.
DR   HOGENOM; CLU_083635_3_1_1; -.
DR   InParanoid; O88668; -.
DR   OMA; AQTPYCR; -.
DR   OrthoDB; 56593at2759; -.
DR   PhylomeDB; O88668; -.
DR   TreeFam; TF324680; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 433375; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Creg1; mouse.
DR   PRO; PR:O88668; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; O88668; Protein.
DR   Bgee; ENSMUSG00000040713; Expressed in placenta labyrinth and 253 other cell types or tissues.
DR   ExpressionAtlas; O88668; baseline and differential.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR   GO; GO:0006914; P:autophagy; IMP:MGI.
DR   GO; GO:0006897; P:endocytosis; IMP:MGI.
DR   GO; GO:0007042; P:lysosomal lumen acidification; IMP:MGI.
DR   GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR   InterPro; IPR014631; CREG.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   PANTHER; PTHR13343; CREG1 PROTEIN; 1.
DR   PANTHER; PTHR13343:SF21; PROTEIN CREG1; 1.
DR   Pfam; PF13883; Pyrid_oxidase_2; 1.
DR   PIRSF; PIRSF036911; CREG; 1.
DR   SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR   Genevisible; O88668; MM.
PE   1: Evidence at protein level;
KW   Glycoprotein; Growth regulation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..220
FT                   /note="Protein CREG1"
FT                   /id="PRO_0000006204"
FT   REGION          30..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        62
FT                   /note="V -> M (in Ref. 2; BAC39549)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   220 AA;  24452 MW;  EF3A8CFD3186163D CRC64;
     MAARAPELAR SLLAALLAPA LVALLVSPAS GRGGRDHGDW DVDRRLPPLP PREDGPRVAR
     FVTHVSDWGS LATISTIKEV RGWPFADIIS ISDGPPGEGT GEPYMYLSPL QQAVSDLQEN
     PEATLTMSLA QTVYCRNHGF DPQSPLCVHI MMSGTVTKVN KTEEDYARDS LFVRHPEMKH
     WPSSHNWFFA KLKISRIWVL DYFGGPKVVT PEEYFNVTLQ
//