ID AGR2_HUMAN Reviewed; 175 AA. AC O95994; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 28-JAN-2026, entry version 174. DE RecName: Full=Anterior gradient protein 2 homolog; DE Short=AG-2; DE Short=hAG-2; DE AltName: Full=HPC8; DE AltName: Full=Secreted cement gland protein XAG-2 homolog; DE Flags: Precursor; GN Name=AGR2; Synonyms=AG2; ORFNames=UNQ515/PRO1030; 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], AND TISSUE SPECIFICITY. RC TISSUE=Mammary gland; 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]. RC TISSUE=Prostatic carcinoma; RA Zhang J.S., Smith D.I.; RT "Identification of human homolog of XAG-2 over-expressed in tumors."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Fan Y.X., Yu L., Zhang X.N., Wan W.C., Wang X.K., Zhao S.Y.; RT "Cloning and expression of a novel human cDNA homology to murine GOB-4 RT mRNA."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 [8] RP PROTEIN SEQUENCE OF 21-35. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [9] RP INTERACTION WITH LYPD3 AND DAG1. RX PubMed=12592373; DOI=10.1038/sj.bjc.6600740; RA Fletcher G.C., Patel S., Tyson K., Adam P.J., Schenker M., Loader J.A., RA Daviet L., Legrain P., Parekh R., Harris A.L., Terrett J.A.; RT "hAG-2 and hAG-3, human homologues of genes involved in differentiation, RT are associated with oestrogen receptor-positive breast tumours and interact RT with metastasis gene C4.4a and dystroglycan."; RL Br. J. Cancer 88:579-585(2003). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=15834940; DOI=10.1002/gcc.20188; RA Zhang J.-S., Gong A., Cheville J.C., Smith D.I., Young C.Y.F.; RT "AGR2, an androgen-inducible secretory protein overexpressed in prostate RT cancer."; RL Genes Chromosomes Cancer 43:249-259(2005). RN [11] RP FUNCTION. RX PubMed=18199544; DOI=10.1158/0008-5472.can-07-2930; RA Wang Z., Hao Y., Lowe A.W.; RT "The adenocarcinoma-associated antigen, AGR2, promotes tumor growth, cell RT migration, and cellular transformation."; RL Cancer Res. 68:492-497(2008). RN [12] RP INTERACTION WITH MUC2, AND MUTAGENESIS OF CYS-81. 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 [13] RP STRUCTURE BY NMR OF 41-175, FUNCTION, SUBUNIT, HOMODIMERIZATION, RP MUTAGENESIS OF GLU-60; TYR-63 AND LYS-64, AND CELL ADHESION REGION. RX PubMed=23274113; DOI=10.1016/j.jmb.2012.12.009; RA Patel P., Clarke C., Barraclough D.L., Jowitt T.A., Rudland P.S., RA Barraclough R., Lian L.Y.; RT "Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin RT fold structure and a role in cell adhesion."; RL J. Mol. Biol. 425:929-943(2013). RN [14] RP VARIANTS RIFTD THR-71; TYR-117 AND GLU-143, AND INVOLVEMENT IN RIFTD. RX PubMed=34952832; DOI=10.1136/jmedgenet-2021-108150; RA Bertoli-Avella A., Hotakainen R., Al Shehhi M., Urzi A., Pareira C., RA Marais A., Al Shidhani K., Aloraimi S., Morales-Torres G., Fisher S., RA Demuth L., Moteleb Selim L.A., Al Menabawy N., Busehail M., AlShaikh M., RA Gilani N., Chalabi D.N., Alharbi N.S., Alfadhel M., Abdelrahman M., RA Venselaar H., Anjum N., Saeed A., Alghamdi M.A., Aljaedi H., Arabi H., RA Karageorgou V., Khan S., Hajjari Z., Radefeldt M., Al-Ali R., RA Tripolszki K., Jamhawi A., Paknia O., Cozma C., Cheema H., Ameziane N., RA Al-Muhsen S., Bauer P.; RT "A disorder clinically resembling cystic fibrosis caused by biallelic RT variants in the AGR2 gene."; RL J. Med. Genet. 59:993-1001(2022). RN [15] RP VARIANT RIFTD TYR-117, CHARACTERIZATION OF VARIANT RIFTD TYR-117, AND RP INTERACTION WITH MUC2. RX PubMed=34237462; DOI=10.1016/j.jcmgh.2021.07.001; RG COLORS in IBD-Qatar Study Group; RA Al-Shaibi A.A., Abdel-Motal U.M., Hubrack S.Z., Bullock A.N., RA Al-Marri A.A., Agrebi N., Al-Subaiey A.A., Ibrahim N.A., Charles A.K., RA Elawad M., Uhlig H.H., Lo B.; RT "Human AGR2 Deficiency Causes Mucus Barrier Dysfunction and Infantile RT Inflammatory Bowel Disease."; RL Cell. Mol. Gastroenterol. Hepatol. 12:1809-1830(2021). CC -!- FUNCTION: Required for MUC2 post-transcriptional synthesis and CC secretion. May play a role in the production of mucus by intestinal CC cells (By similarity). Proto-oncogene that may play a role in cell CC migration, cell differentiation and cell growth. Promotes cell adhesion CC (PubMed:23274113). {ECO:0000250, ECO:0000269|PubMed:18199544, CC ECO:0000269|PubMed:23274113}. CC -!- SUBUNIT: Monomer and homodimer (PubMed:23274113). Interacts with LYPD3 CC and DAG1 (alphaDAG1) (PubMed:12592373). Interacts with MUC2; disulfide- CC linked (PubMed:19359471, PubMed:34237462). CC {ECO:0000269|PubMed:12592373, ECO:0000269|PubMed:19359471, CC ECO:0000269|PubMed:23274113, ECO:0000269|PubMed:34237462}. CC -!- INTERACTION: CC O95994; X5D778: ANKRD11; NbExp=3; IntAct=EBI-712648, EBI-17183751; CC O95994; Q9UH17-2: APOBEC3B; NbExp=3; IntAct=EBI-712648, EBI-17624977; CC O95994; Q12797-6: ASPH; NbExp=3; IntAct=EBI-712648, EBI-12092171; CC O95994; Q96FH0: BORCS8; NbExp=3; IntAct=EBI-712648, EBI-744076; CC O95994; P01024: C3; NbExp=3; IntAct=EBI-712648, EBI-905851; CC O95994; P49069: CAMLG; NbExp=3; IntAct=EBI-712648, EBI-1748958; CC O95994; Q8NEC5: CATSPER1; NbExp=6; IntAct=EBI-712648, EBI-744545; CC O95994; P28906: CD34; NbExp=3; IntAct=EBI-712648, EBI-2836676; CC O95994; P34810: CD68; NbExp=3; IntAct=EBI-712648, EBI-2826276; CC O95994; Q96HQ2: CDKN2AIPNL; NbExp=3; IntAct=EBI-712648, EBI-10038935; CC O95994; O15182: CETN3; NbExp=3; IntAct=EBI-712648, EBI-712959; CC O95994; O95833: CLIC3; NbExp=3; IntAct=EBI-712648, EBI-10192241; CC O95994; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-712648, EBI-741032; CC O95994; O95741-2: CPNE6; NbExp=5; IntAct=EBI-712648, EBI-13312079; CC O95994; O75575-2: CRCP; NbExp=3; IntAct=EBI-712648, EBI-12880830; CC O95994; P16220: CREB1; NbExp=3; IntAct=EBI-712648, EBI-711855; CC O95994; Q24JT5: CRYGA; NbExp=3; IntAct=EBI-712648, EBI-10239205; CC O95994; Q6BCY4-2: CYB5R2; NbExp=3; IntAct=EBI-712648, EBI-12102608; CC O95994; Q8TEB1: DCAF11; NbExp=3; IntAct=EBI-712648, EBI-2213388; CC O95994; O00303: EIF3F; NbExp=3; IntAct=EBI-712648, EBI-711990; CC O95994; O15197-2: EPHB6; NbExp=3; IntAct=EBI-712648, EBI-10182490; CC O95994; P12104: FABP2; NbExp=4; IntAct=EBI-712648, EBI-3905109; CC O95994; Q9BQ89: FAM110A; NbExp=5; IntAct=EBI-712648, EBI-1752811; CC O95994; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-712648, EBI-3893327; CC O95994; O95954: FTCD; NbExp=3; IntAct=EBI-712648, EBI-10192648; CC O95994; Q06547: GABPB1; NbExp=3; IntAct=EBI-712648, EBI-618165; CC O95994; O43681: GET3; NbExp=7; IntAct=EBI-712648, EBI-2515857; CC O95994; P62993: GRB2; NbExp=5; IntAct=EBI-712648, EBI-401755; CC O95994; Q6ZYL4: GTF2H5; NbExp=3; IntAct=EBI-712648, EBI-6380438; CC O95994; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-712648, EBI-740290; CC O95994; P43080: GUCA1A; NbExp=3; IntAct=EBI-712648, EBI-6873005; CC O95994; P08631-2: HCK; NbExp=3; IntAct=EBI-712648, EBI-9834454; CC O95994; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-712648, EBI-740641; CC O95994; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-712648, EBI-3918847; CC O95994; Q9UBH0: IL36RN; NbExp=3; IntAct=EBI-712648, EBI-465156; CC O95994; P12268: IMPDH2; NbExp=3; IntAct=EBI-712648, EBI-353389; CC O95994; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-712648, EBI-6426443; CC O95994; Q15323: KRT31; NbExp=6; IntAct=EBI-712648, EBI-948001; CC O95994; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-712648, EBI-10274069; CC O95994; O15116: LSM1; NbExp=3; IntAct=EBI-712648, EBI-347619; CC O95994; O95983-2: MBD3; NbExp=3; IntAct=EBI-712648, EBI-11978579; CC O95994; Q02817: MUC2; NbExp=3; IntAct=EBI-712648, EBI-2105803; CC O95994; P60660: MYL6; NbExp=3; IntAct=EBI-712648, EBI-300817; CC O95994; Q16656-4: NRF1; NbExp=5; IntAct=EBI-712648, EBI-11742836; CC O95994; Q96L73-2: NSD1; NbExp=3; IntAct=EBI-712648, EBI-11110981; CC O95994; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-712648, EBI-741158; CC O95994; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-712648, EBI-741048; CC O95994; Q9BVL2: NUP58; NbExp=5; IntAct=EBI-712648, EBI-2811583; CC O95994; Q9H1M0: NUP62CL; NbExp=6; IntAct=EBI-712648, EBI-751933; CC O95994; Q8NDX5-7: PHC3; NbExp=5; IntAct=EBI-712648, EBI-12910528; CC O95994; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-712648, EBI-1389308; CC O95994; P62875: POLR2L; NbExp=3; IntAct=EBI-712648, EBI-359527; CC O95994; Q96HA1: POM121; NbExp=4; IntAct=EBI-712648, EBI-739990; CC O95994; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-712648, EBI-11956563; CC O95994; P78424: POU6F2; NbExp=3; IntAct=EBI-712648, EBI-12029004; CC O95994; Q99633: PRPF18; NbExp=3; IntAct=EBI-712648, EBI-2798416; CC O95994; P25786: PSMA1; NbExp=3; IntAct=EBI-712648, EBI-359352; CC O95994; P20618: PSMB1; NbExp=3; IntAct=EBI-712648, EBI-372273; CC O95994; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-712648, EBI-11974061; CC O95994; Q9NZH5-2: PTTG2; NbExp=3; IntAct=EBI-712648, EBI-17630019; CC O95994; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-712648, EBI-12123390; CC O95994; P82980: RBP5; NbExp=3; IntAct=EBI-712648, EBI-3941274; CC O95994; Q6ZR62: RTL4; NbExp=3; IntAct=EBI-712648, EBI-18292412; CC O95994; A0A0S2Z4U3: SDC3; NbExp=3; IntAct=EBI-712648, EBI-10204280; CC O95994; O43765: SGTA; NbExp=3; IntAct=EBI-712648, EBI-347996; CC O95994; Q96EQ0: SGTB; NbExp=6; IntAct=EBI-712648, EBI-744081; CC O95994; O14796: SH2D1B; NbExp=3; IntAct=EBI-712648, EBI-3923013; CC O95994; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-712648, EBI-2623095; CC O95994; O75716: STK16; NbExp=3; IntAct=EBI-712648, EBI-749295; CC O95994; Q15560: TCEA2; NbExp=3; IntAct=EBI-712648, EBI-710310; CC O95994; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-712648, EBI-11952651; CC O95994; Q96FV9: THOC1; NbExp=3; IntAct=EBI-712648, EBI-1765605; CC O95994; Q08117-2: TLE5; NbExp=3; IntAct=EBI-712648, EBI-11741437; CC O95994; Q12933: TRAF2; NbExp=3; IntAct=EBI-712648, EBI-355744; CC O95994; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-712648, EBI-8994397; CC O95994; P29597: TYK2; NbExp=5; IntAct=EBI-712648, EBI-1383454; CC O95994; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-712648, EBI-10180829; CC O95994; Q9UMX0: UBQLN1; NbExp=9; IntAct=EBI-712648, EBI-741480; CC O95994; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-712648, EBI-10173939; CC O95994; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-712648, EBI-947187; CC O95994; Q9Y2K6: USP20; NbExp=3; IntAct=EBI-712648, EBI-2511991; CC O95994; Q14119: VEZF1; NbExp=5; IntAct=EBI-712648, EBI-11980193; CC O95994; Q9Y6T4: WUGSC:H_DJ0726N20.gs.b; NbExp=5; IntAct=EBI-712648, EBI-12369705; CC O95994; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-712648, EBI-10254561; CC O95994; Q96JP5: ZFP91; NbExp=3; IntAct=EBI-712648, EBI-1052613; CC O95994; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-712648, EBI-11741890; CC O95994; Q12140: BSC1; Xeno; NbExp=3; IntAct=EBI-712648, EBI-36401; CC O95994; Q12154: GET3; Xeno; NbExp=3; IntAct=EBI-712648, EBI-2989; CC O95994; Q01589: SED1; Xeno; NbExp=3; IntAct=EBI-712648, EBI-16917; CC O95994; Q12118: SGT2; Xeno; NbExp=3; IntAct=EBI-712648, EBI-31784; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15834940}. CC Endoplasmic reticulum {ECO:0000250|UniProtKB:O88312}. CC -!- TISSUE SPECIFICITY: Expressed strongly in trachea, lung, stomach, CC colon, prostate and small intestine. Expressed weakly in pituitary CC gland, salivary gland, mammary gland, bladder, appendix, ovary, fetal CC lung, uterus, pancreas, kidney, fetal kidney, testis, placenta, thyroid CC gland and in estrogen receptor (ER)-positive breast cancer cell lines. CC {ECO:0000269|PubMed:9790916}. CC -!- DISEASE: Respiratory infections, recurrent, and failure to thrive with CC or without diarrhea (RIFTD) [MIM:620233]: An autosomal recessive CC disorder characterized by neonatal onset of recurrent pulmonary CC infections, coughing, wheezy episodes, interstitial lung disease, and CC bronchiectasis. Episodes of vomiting and chronic diarrhea result in CC failure to thrive. Results of sweat chloride and pancreatic elastase CC tests are normal. {ECO:0000269|PubMed:34237462, CC ECO:0000269|PubMed:34952832}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the AGR 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; AF007791; AAC77358.1; -; mRNA. DR EMBL; AF038451; AAC82614.1; -; mRNA. DR EMBL; AF088867; AAF22484.1; -; mRNA. DR EMBL; AF115926; AAL54870.1; -; mRNA. DR EMBL; AF087879; AAP97179.1; -; mRNA. DR EMBL; AY359009; AAQ89368.1; -; mRNA. DR EMBL; BT007048; AAP35697.1; -; mRNA. DR EMBL; AC073333; AAP22354.1; -; Genomic_DNA. DR EMBL; BC015503; AAH15503.1; -; mRNA. DR CCDS; CCDS5364.1; -. DR PIR; JE0350; JE0350. DR RefSeq; NP_006399.1; NM_006408.4. DR RefSeq; XP_005249638.1; XM_005249581.5. DR RefSeq; XP_054213068.1; XM_054357093.1. DR PDB; 2LNS; NMR; -; A/B=41-175. DR PDB; 2LNT; NMR; -; A=41-175. DR PDBsum; 2LNS; -. DR PDBsum; 2LNT; -. DR AlphaFoldDB; O95994; -. DR BMRB; O95994; -. DR SMR; O95994; -. DR BioGRID; 115802; 946. DR DIP; DIP-48825N; -. DR FunCoup; O95994; 439. DR IntAct; O95994; 110. DR MINT; O95994; -. DR STRING; 9606.ENSP00000391490; -. DR iPTMnet; O95994; -. DR PhosphoSitePlus; O95994; -. DR SwissPalm; O95994; -. DR BioMuta; AGR2; -. DR CPTAC; CPTAC-1293; -. DR CPTAC; CPTAC-456; -. DR jPOST; O95994; -. DR MassIVE; O95994; -. DR PaxDb; 9606-ENSP00000391490; -. DR PeptideAtlas; O95994; -. DR ProteomicsDB; 51169; -. DR Pumba; O95994; -. DR TopDownProteomics; O95994; -. DR Antibodypedia; 1524; 935 antibodies from 42 providers. DR DNASU; 10551; -. DR Ensembl; ENST00000419304.7; ENSP00000391490.2; ENSG00000106541.13. DR GeneID; 10551; -. DR KEGG; hsa:10551; -. DR MANE-Select; ENST00000419304.7; ENSP00000391490.2; NM_006408.4; NP_006399.1. DR AGR; HGNC:328; -. DR CIViC; 10551; 1 evidence item across 1 molecular profile. DR ClinPGx; PA24625; -. DR CTD; 10551; -. DR DisGeNET; 10551; -. DR GeneCards; AGR2; -. DR HGNC; HGNC:328; AGR2. DR HPA; ENSG00000106541; Tissue enhanced (cervix, intestine, stomach). DR MalaCards; AGR2; -. DR MIM; 606358; gene. DR MIM; 620233; phenotype. DR OpenTargets; ENSG00000106541; -. DR VEuPathDB; HostDB:ENSG00000106541; -. DR eggNOG; ENOG502RYQ8; Eukaryota. DR GeneTree; ENSGT00530000063273; -. DR HOGENOM; CLU_088048_1_1_1; -. DR InParanoid; O95994; -. DR OMA; YSNMQKA; -. DR OrthoDB; 262308at2759; -. DR PAN-GO; O95994; 3 GO annotations based on evolutionary models. DR PhylomeDB; O95994; -. DR PathwayCommons; O95994; -. DR SignaLink; O95994; -. DR Agora; ENSG00000106541; -. DR BioGRID-ORCS; 10551; 25 hits in 1150 CRISPR screens. DR ChiTaRS; AGR2; human. DR EvolutionaryTrace; O95994; -. DR GeneWiki; AGR2; -. DR GenomeRNAi; 10551; -. DR Pharos; O95994; Tbio. DR PRO; PR:O95994; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; O95994; protein. DR Bgee; ENSG00000106541; Expressed in mucosa of sigmoid colon and 144 other cell types or tissues. DR ExpressionAtlas; O95994; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0002162; F:dystroglycan binding; IDA:UniProtKB. DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:MGI. DR GO; GO:0060326; P:cell chemotaxis; IDA:MGI. DR GO; GO:0048546; P:digestive tract morphogenesis; ISS:UniProtKB. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:MGI. DR GO; GO:0006954; P:inflammatory response; IMP:MGI. DR GO; GO:0060480; P:lung goblet cell differentiation; IEA:Ensembl. DR GO; GO:0070254; P:mucus secretion; ISS:UniProtKB. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:UniProtKB. DR GO; GO:0048639; P:positive regulation of developmental growth; ISS:UniProtKB. DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; IDA:UniProtKB. DR GO; GO:1903899; P:positive regulation of PERK-mediated unfolded protein response; IDA:UniProtKB. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB. DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IDA:MGI. DR CDD; cd02960; AGR; 1. DR FunFam; 3.40.30.10:FF:000036; anterior gradient protein 2 homolog; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR051099; AGR/TXD. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR15337:SF1; ANTERIOR GRADIENT PROTEIN 2 HOMOLOG; 1. DR PANTHER; PTHR15337; ANTERIOR GRADIENT PROTEIN-RELATED; 1. DR Pfam; PF13899; Thioredoxin_7; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond; KW Endoplasmic reticulum; Proteomics identification; Proto-oncogene; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 21..175 FT /note="Anterior gradient protein 2 homolog" FT /id="PRO_0000001037" FT REGION 21..40 FT /note="Required to promote cell adhesion" FT /evidence="ECO:0000269|PubMed:23274113" FT MOTIF 45..54 FT /note="Homodimer stabilization; interchain" FT /evidence="ECO:0000269|PubMed:23274113, FT ECO:0007744|PDB:2LNS" FT MOTIF 60..67 FT /note="Homodimer stabilization; interchain" FT /evidence="ECO:0000269|PubMed:23274113, FT ECO:0007744|PDB:2LNS" FT VARIANT 71 FT /note="P -> T (in RIFTD; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34952832" FT /id="VAR_088087" FT VARIANT 117 FT /note="H -> Y (in RIFTD; decreased interaction with MUC2; FT dbSNP:rs780638101)" FT /evidence="ECO:0000269|PubMed:34237462, FT ECO:0000269|PubMed:34952832" FT /id="VAR_088088" FT VARIANT 143 FT /note="G -> E (in RIFTD; uncertain significance; FT dbSNP:rs923936131)" FT /evidence="ECO:0000269|PubMed:34952832" FT /id="VAR_088089" FT MUTAGEN 60 FT /note="E->A: Monomer only, and reduced cell adhesion FT efficiency." FT /evidence="ECO:0000269|PubMed:23274113" FT MUTAGEN 63 FT /note="Y->A: Disrupted dimerization." FT /evidence="ECO:0000269|PubMed:23274113" FT MUTAGEN 64 FT /note="K->A: Disrupted dimerization." FT /evidence="ECO:0000269|PubMed:23274113" FT MUTAGEN 81 FT /note="C->S: Loss of interaction with MUC2." FT /evidence="ECO:0000269|PubMed:19359471" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:2LNS" FT HELIX 58..66 FT /evidence="ECO:0007829|PDB:2LNS" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:2LNS" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:2LNS" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:2LNS" FT HELIX 82..91 FT /evidence="ECO:0007829|PDB:2LNS" FT HELIX 95..102 FT /evidence="ECO:0007829|PDB:2LNS" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:2LNS" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:2LNT" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:2LNS" FT STRAND 127..132 FT /evidence="ECO:0007829|PDB:2LNS" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:2LNS" FT TURN 146..150 FT /evidence="ECO:0007829|PDB:2LNS" FT TURN 154..156 FT /evidence="ECO:0007829|PDB:2LNS" FT HELIX 157..167 FT /evidence="ECO:0007829|PDB:2LNS" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:2LNT" SQ SEQUENCE 175 AA; 19979 MW; F271B1BD377BEE11 CRC64; MEKIPVSAFL LLVALSYTLA RDTTVKPGAK KDTKDSRPKL PQTLSRGWGD QLIWTQTYEE ALYKSKTSNK PLMIIHHLDE CPHSQALKKV FAENKEIQKL AEQFVLLNLV YETTDKHLSP DGQYVPRIMF VDPSLTVRAD ITGRYSNRLY AYEPADTALL LDNMKKALKL LKTEL //