AGR2_MOUSE
ID AGR2_MOUSE Reviewed; 175 AA.
AC O88312; A2CGA2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Anterior gradient protein 2 homolog;
DE Short=AG-2;
DE Short=mAG-2;
DE AltName: Full=Protein Gob-4;
DE AltName: Full=Secreted cement gland protein XAG-2 homolog;
DE Flags: Precursor;
GN Name=Agr2; Synonyms=Gob4;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster; TISSUE=Embryo;
RX PubMed=9790916; DOI=10.1006/bbrc.1998.9440;
RA Thompson D.A., Weigel R.J.;
RT "hAG-2, the human homologue of the Xenopus laevis cement gland gene XAG-2,
RT is coexpressed with estrogen receptor in breast cancer cell lines.";
RL Biochem. Biophys. Res. Commun. 251:111-116(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Intestine;
RX PubMed=10095068; DOI=10.1016/s0167-4781(99)00010-x;
RA Komiya T., Hirohashi S.;
RT "Cloning of a gene, gob-4, which is expressed in intestinal goblet cells in
RT mice.";
RL Biochim. Biophys. Acta 1444:434-438(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19359471; DOI=10.1073/pnas.0808722106;
RA Park S.-W., Zhen G., Verhaeghe C., Nakagami Y., Nguyenvu L.T.,
RA Barczak A.J., Killeen N., Erle D.J.;
RT "The protein disulfide isomerase AGR2 is essential for production of
RT intestinal mucus.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6950-6955(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Pancreas;
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: Required for MUC2 post-transcriptional synthesis and
CC secretion. May play a role in the production of mucus by intestinal
CC cells. Proto-oncogene that may play a role in cell migration, cell
CC differentiation and cell growth (By similarity). Promotes cell adhesion
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O95994,
CC ECO:0000269|PubMed:19359471}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with LYPD3 and DAG1
CC (alphaDAG1). Interacts with MUC2; disulfide-linked.
CC {ECO:0000250|UniProtKB:O95994}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O95994}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:19359471}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, skeletal muscle, testis, liver,
CC stomach, colon, small intestine, the goblet cells of the intestine and
CC the mucuous neck cells of the stomach. {ECO:0000269|PubMed:10095068,
CC ECO:0000269|PubMed:9790916}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 15 dpc onwards.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but display altered production of
CC mucus with loss of production of MUC2 despite expression of its mRNA.
CC They also display an increase in mast cells in the intestine, an
CC increased expression of inflammation-specific genes, and frequent
CC rectal prolapse. This is associated with a higher susceptibility to
CC colitis. {ECO:0000269|PubMed:19359471}.
CC -!- SIMILARITY: Belongs to the AGR family. {ECO:0000305}.
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DR EMBL; AF044262; AAC72705.1; -; mRNA.
DR EMBL; AB016592; BAA32044.1; -; mRNA.
DR EMBL; AK007677; BAB25181.1; -; mRNA.
DR EMBL; CT030196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013334; AAH13334.1; -; mRNA.
DR CCDS; CCDS25881.1; -.
DR RefSeq; NP_035913.1; NM_011783.2.
DR AlphaFoldDB; O88312; -.
DR SMR; O88312; -.
DR IntAct; O88312; 1.
DR STRING; 10090.ENSMUSP00000020898; -.
DR iPTMnet; O88312; -.
DR PhosphoSitePlus; O88312; -.
DR MaxQB; O88312; -.
DR PaxDb; O88312; -.
DR PeptideAtlas; O88312; -.
DR PRIDE; O88312; -.
DR ProteomicsDB; 281955; -.
DR Antibodypedia; 1524; 905 antibodies from 40 providers.
DR DNASU; 23795; -.
DR Ensembl; ENSMUST00000020898; ENSMUSP00000020898; ENSMUSG00000020581.
DR GeneID; 23795; -.
DR KEGG; mmu:23795; -.
DR UCSC; uc007njm.1; mouse.
DR CTD; 10551; -.
DR MGI; MGI:1344405; Agr2.
DR VEuPathDB; HostDB:ENSMUSG00000020581; -.
DR eggNOG; ENOG502RYQ8; Eukaryota.
DR GeneTree; ENSGT00530000063273; -.
DR HOGENOM; CLU_088048_1_1_1; -.
DR InParanoid; O88312; -.
DR OMA; VFAEHKD; -.
DR OrthoDB; 1382017at2759; -.
DR PhylomeDB; O88312; -.
DR TreeFam; TF321449; -.
DR BioGRID-ORCS; 23795; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Agr2; mouse.
DR PRO; PR:O88312; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O88312; protein.
DR Bgee; ENSMUSG00000020581; Expressed in prostate gland ventral lobe and 80 other tissues.
DR Genevisible; O88312; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0002162; F:dystroglycan binding; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:UniProtKB.
DR GO; GO:0060480; P:lung goblet cell differentiation; IDA:MGI.
DR GO; GO:0070254; P:mucus secretion; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0048639; P:positive regulation of developmental growth; IMP:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; ISO:MGI.
DR GO; GO:1903899; P:positive regulation of PERK-mediated unfolded protein response; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Proto-oncogene; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250|UniProtKB:O95994"
FT CHAIN 21..175
FT /note="Anterior gradient protein 2 homolog"
FT /id="PRO_0000001038"
FT REGION 21..40
FT /note="Required to promote cell adhesion"
FT /evidence="ECO:0000250|UniProtKB:O95994"
FT REGION 24..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..54
FT /note="Homodimer stabilization; interchain"
FT /evidence="ECO:0000250|UniProtKB:O95994"
FT MOTIF 60..67
FT /note="Homodimer stabilization; interchain"
FT /evidence="ECO:0000250|UniProtKB:O95994"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 175 AA; 19920 MW; ACC3CFE429B668CA CRC64;
MEKFSVSAIL LLVAISGTLA KDTTVKSGAK KDPKDSRPKL PQTLSRGWGD QLIWTQTYEE
ALYRSKTSNR PLMVIHHLDE CPHSQALKKV FAEHKEIQKL AEQFVLLNLV YETTDKHLSP
DGQYVPRIVF VDPSLTVRAD ITGRYSNRLY AYEPSDTALL YDNMKKALKL LKTEL
