AGR2_HUMAN
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 03-AUG-2022, entry version 158.
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).
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). Interacts with MUC2; disulfide-linked.
CC {ECO:0000269|PubMed:12592373, ECO:0000269|PubMed:19359471,
CC ECO:0000269|PubMed:23274113}.
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=6; 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; A0A024R4Z4: hCG_2042749; NbExp=3; IntAct=EBI-712648, EBI-14231181;
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=2; 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; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-712648, EBI-14096082;
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; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-712648, EBI-11741890;
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 -!- SIMILARITY: Belongs to the AGR family. {ECO:0000305}.
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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_006408.3.
DR RefSeq; XP_005249638.1; XM_005249581.4.
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; 938.
DR DIP; DIP-48825N; -.
DR IntAct; O95994; 100.
DR STRING; 9606.ENSP00000391490; -.
DR iPTMnet; O95994; -.
DR PhosphoSitePlus; O95994; -.
DR BioMuta; AGR2; -.
DR CPTAC; CPTAC-1293; -.
DR CPTAC; CPTAC-456; -.
DR EPD; O95994; -.
DR jPOST; O95994; -.
DR MassIVE; O95994; -.
DR PaxDb; O95994; -.
DR PeptideAtlas; O95994; -.
DR PRIDE; O95994; -.
DR ProteomicsDB; 51169; -.
DR TopDownProteomics; O95994; -.
DR Antibodypedia; 1524; 905 antibodies from 40 providers.
DR DNASU; 10551; -.
DR Ensembl; ENST00000419304.7; ENSP00000391490.2; ENSG00000106541.12.
DR GeneID; 10551; -.
DR KEGG; hsa:10551; -.
DR MANE-Select; ENST00000419304.7; ENSP00000391490.2; NM_006408.4; NP_006399.1.
DR CTD; 10551; -.
DR DisGeNET; 10551; -.
DR GeneCards; AGR2; -.
DR HGNC; HGNC:328; AGR2.
DR HPA; ENSG00000106541; Tissue enhanced (cervix, intestine, stomach).
DR MIM; 606358; gene.
DR neXtProt; NX_O95994; -.
DR OpenTargets; ENSG00000106541; -.
DR PharmGKB; PA24625; -.
DR VEuPathDB; HostDB:ENSG00000106541; -.
DR eggNOG; ENOG502RYQ8; Eukaryota.
DR GeneTree; ENSGT00530000063273; -.
DR HOGENOM; CLU_088048_1_1_1; -.
DR InParanoid; O95994; -.
DR OMA; VFAEHKD; -.
DR OrthoDB; 1382017at2759; -.
DR PhylomeDB; O95994; -.
DR TreeFam; TF321449; -.
DR PathwayCommons; O95994; -.
DR SignaLink; O95994; -.
DR BioGRID-ORCS; 10551; 23 hits in 1071 CRISPR screens.
DR ChiTaRS; AGR2; human.
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 142 other tissues.
DR ExpressionAtlas; O95994; baseline and differential.
DR Genevisible; O95994; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP:UniProtKB.
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:0048546; P:digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0060480; P:lung goblet cell differentiation; IEA:Ensembl.
DR GO; GO:0070254; P:mucus secretion; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP: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 InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Proto-oncogene; Reference proteome; Secreted;
KW 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 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
