MGAL_HUMAN
ID MGAL_HUMAN Reviewed; 2515 AA.
AC Q2M2H8; A4D2I3; C9JNC2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable maltase-glucoamylase 2 {ECO:0000305};
DE AltName: Full=Maltase-glucoamylase (alpha-glucosidase) pseudogene;
DE Includes:
DE RecName: Full=Glucoamylase;
DE EC=3.2.1.3;
DE AltName: Full=Glucan 1,4-alpha-glucosidase;
GN Name=MGAM2 {ECO:0000312|HGNC:HGNC:28101};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC successively from non-reducing ends of the chains with release of
CC beta-D-glucose.; EC=3.2.1.3;
CC -!- INTERACTION:
CC Q2M2H8; Q93009: USP7; NbExp=2; IntAct=EBI-20850333, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2M2H8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2M2H8-3; Sequence=VSP_055415, VSP_055416;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 31 family, it
CC lacks one active site residue, thus suggesting it may lack some enzyme
CC activity. {ECO:0000305}.
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DR EMBL; AC091742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236959; EAL23771.1; -; Genomic_DNA.
DR EMBL; CH471198; EAW51984.1; -; Genomic_DNA.
DR EMBL; BC111973; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC111975; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001280555.1; NM_001293626.1. [Q2M2H8-1]
DR AlphaFoldDB; Q2M2H8; -.
DR SMR; Q2M2H8; -.
DR BioGRID; 125025; 3.
DR IntAct; Q2M2H8; 3.
DR STRING; 9606.ENSP00000447431; -.
DR BindingDB; Q2M2H8; -.
DR ChEMBL; CHEMBL3833502; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR GlyGen; Q2M2H8; 4 sites.
DR iPTMnet; Q2M2H8; -.
DR PhosphoSitePlus; Q2M2H8; -.
DR BioMuta; MGAM2; -.
DR DMDM; 190359876; -.
DR EPD; Q2M2H8; -.
DR jPOST; Q2M2H8; -.
DR MassIVE; Q2M2H8; -.
DR PeptideAtlas; Q2M2H8; -.
DR PRIDE; Q2M2H8; -.
DR Antibodypedia; 70894; 4 antibodies from 4 providers.
DR DNASU; 93432; -.
DR Ensembl; ENST00000477922.4; ENSP00000420449.3; ENSG00000257743.9. [Q2M2H8-1]
DR Ensembl; ENST00000550469.6; ENSP00000447431.2; ENSG00000257743.9. [Q2M2H8-3]
DR Ensembl; ENST00000622623.2; ENSP00000484330.1; ENSG00000278563.2. [Q2M2H8-3]
DR Ensembl; ENST00000632823.1; ENSP00000488423.1; ENSG00000278563.2. [Q2M2H8-1]
DR GeneID; 93432; -.
DR KEGG; hsa:93432; -.
DR MANE-Select; ENST00000477922.4; ENSP00000420449.3; NM_001293626.2; NP_001280555.1.
DR UCSC; uc064isf.1; human. [Q2M2H8-1]
DR CTD; 93432; -.
DR DisGeNET; 93432; -.
DR GeneCards; MGAM2; -.
DR HGNC; HGNC:28101; MGAM2.
DR HPA; ENSG00000257743; Group enriched (intestine, pancreas, salivary gland).
DR neXtProt; NX_Q2M2H8; -.
DR OpenTargets; ENSG00000257743; -.
DR VEuPathDB; HostDB:ENSG00000257743; -.
DR eggNOG; KOG1065; Eukaryota.
DR GeneTree; ENSGT00940000163091; -.
DR HOGENOM; CLU_000631_3_0_1; -.
DR OMA; GVNSTYV; -.
DR OrthoDB; 151244at2759; -.
DR PhylomeDB; Q2M2H8; -.
DR PathwayCommons; Q2M2H8; -.
DR SignaLink; Q2M2H8; -.
DR BioGRID-ORCS; 93432; 1 hit in 81 CRISPR screens.
DR ChiTaRS; MGAM2; human.
DR GenomeRNAi; 93432; -.
DR Pharos; Q2M2H8; Tdark.
DR PRO; PR:Q2M2H8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q2M2H8; protein.
DR Bgee; ENSG00000257743; Expressed in duodenum and 46 other tissues.
DR Genevisible; Q2M2H8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00111; Trefoil; 2.
DR Gene3D; 2.60.40.1180; -; 4.
DR Gene3D; 4.10.110.10; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR Pfam; PF13802; Gal_mutarotas_2; 2.
DR Pfam; PF01055; Glyco_hydro_31; 2.
DR Pfam; PF16863; NtCtMGAM_N; 2.
DR Pfam; PF00088; Trefoil; 2.
DR SMART; SM00018; PD; 2.
DR SUPFAM; SSF51445; SSF51445; 2.
DR SUPFAM; SSF57492; SSF57492; 2.
DR SUPFAM; SSF74650; SSF74650; 2.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Membrane; Reference proteome; Repeat; Signal-anchor; Sulfation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..2515
FT /note="Probable maltase-glucoamylase 2"
FT /id="PRO_0000341380"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..482
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 41..88
FT /note="P-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 904..950
FT /note="P-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REGION 152..865
FT /note="Maltase"
FT /evidence="ECO:0000250"
FT REGION 1023..1766
FT /note="Glucoamylase"
FT /evidence="ECO:0000250"
FT REGION 1816..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2037..2091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 478
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 481
FT /evidence="ECO:0000250"
FT ACT_SITE 1375
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 1378
FT /evidence="ECO:0000250"
FT MOD_RES 371
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1238
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 54..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 65..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 608..619
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 916..933
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 928..946
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT VAR_SEQ 478..482
FT /note="EMNEV -> VSYYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055415"
FT VAR_SEQ 483..2515
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055416"
FT CONFLICT 327
FT /note="F -> L (in Ref. 4; BC111973/BC111975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2515 AA; 277990 MW; F6E8F08987335A4F CRC64;
MARKLSVLEV LLIIFCLIVV TIDILLLLLV LEETSDTSFT PECPEIPQSE RIDCTPDQEV
TEDICRWQYK CCWSPVADAN VPRCFFPWNW GYEASNGHTN TSTGFTAQLK RLPSPSLFGN
DVATTLFTAE YQTSNRFHFK ITDFNNIRYE VSHENINLVD GIADASNLSY YVEVTDKPFS
IKIMRTSNRR VLLDTSIGPL QFAQQYLQLS FRLPSANVYG LGEHVHQQYR HNMTWKTWPI
FTRDATPTEG MINLYGAHTF FLCLEDARGS SFGVFLMNSN AMEVTLQPAP AITYRTIGGI
LDFYVFLGNT PEQVVQEYLE LVGRPFFPPY WSLGFQLSRR DYGGINKLKE VVSRNRLAEI
PYDVQYSDID YMDGKKDFTV DEVAYSGLPD FVKELHDNGQ KYLIIMNPGI SKNSNYEPYN
NGSLKRVWIL GSNGFAVGEG YPGPTVFPDY TNPVCTEWWT DQVAKFHDHL EFDGVWIEMN
EVSSLLQASN NQCESNNLNF PPFLPRVLDH LLFARTLCMD TEFHGGLHYD IHSLYGHSMA
RTTNLALETI FMNNRSFILS RSTFAGSGKF AAHWLGDNAA TWDDLRWSIP TILEFNLFGI
PMVGANICGY NNNVTEELCR RWMQLGAFYP LPRNHNGPGF RDQDPAAFGV DSLLLKSSRH
YLNIRYTLLP YLYTLFYHAH TRGETVARPL VHEFYQDSAT WDVHEQFLWG PGLLITPVLY
EGVDEVKAYI PDATWYDYET GVAISWRKQL VNMLLPGDKI GLHLRGGYIF PTQKPNTTTE
ASRRNSLGLI IALDYKREAK GELYWDDGVS KDAVTEKKYI LYDFSVTSNH LQAKIINNNY
MDTDNLMFTD ITILGMDKQP ANFIVLLNNV ATSSPSVVYN ASTKVVTITD LQGLVLGQEF
SIRWNLPVSD LEKFNCYPDD PTASEESCRQ RGCLWEDTST PGVPTCYYDT IPNYVASDIQ
YLNTSITADL SLPMAPESAA AAASDSLSAK ISFLHLKVIY HTATMLQVKI YDPTNKRYEV
PVPLNTPPQP VGDPENRLYD VRIQNNPFGI QIQRKNSSTV IWDSQLPGFI FNDMFLSIST
RLPSQYIYGF GETEHTTFRR NMNWNTWGMF AHDEPPAYKK NSYGVHPYYM ALEEDGSAHG
VLLLNSNAMD VTLQPTPALT YRTTGGILDF YIVLGPTPEL VTQQYTELIG RPAMIPYWAL
GFHLSRYGYQ NDAEISSLYD AMVAAQIPYD VQHVDIDYMN RKLDFTLSAN FQNLSLLIEQ
MKKNGMRFIL ILDPAISGNE TQYLPFIRGQ ENNVFIKWPD TNDIVWGKVW PDLPNVIVDG
SLDHETQVKL YRAYVAFPDF FRNSTAAWWK KEIEELYANP REPEKSLKFD GLWIDMNEPS
NFVDGSVRGC SNEMLNNPPY MPYLESRDKG LSSKTLCMES QQILPDSSPV EHYNVHNLYG
WSQTRPTYEA VQEVTGQRGV IITRSTFPSS GRWGGHRLGN NTAAWDQLGK SIIGMMEFSL
FGIPYTGADI CGFFGDAEYE MCVRWMQLGA FYPFSRNHNN IGTRRQDPVA WNSTFEMLSR
KVLETRYTLL PYLYTLMHKA HVEGSTVVRP LLHEFTDDRT TWDIDRQFML GPAILISPVL
ETSTFEISAY FPRARWYDYS TGTSSTSTGQ RKILKAPLDH INLHVRGGYI LPWQEPAMNT
HSSRQNFMGL IVALDDNGTA EGQVFWDDGQ SIDTYENGNY FLANFIAAQN ILQIQTIHNK
YLSDSNPLKV GYIRIWGVNT YVTQVSFTYD NRQFMETNFK SEPYNQILTI QLTDKTINLE
KLTEVTWIDG GPVLPTPTKT STIPMSSHPS PSTTNATSSE TITSSASANT TTGTTDTVPI
TTTSFPSTTS VTTNTTVPDT TSPFPTSTTN ASTNATVPIT TTPFPTSTIG VTTNATVPNT
TAPFPTNAST ASTNATVPIT TTCFATSTIG VTTNATVPDT TAPFPTNTTT ASTNATIPIT
TTPFATSTIS VTTSTTVPDT TAPFPTSTTS ASTNATPVPI TTTLFATSTI GVTTGTTVPD
TTAPFPTSTT STSTSATVPI TTTPSPTNTA DANTSNTVPN TTMPSPTSST TVSTIATVPI
SVTPSLTSTA DATISTTVLI ATTSSLTGTT DVSTSTTINN ISTPVQTNTT NASTSTNVAN
ITATSHTSTD DTVPNNTVPV TAIPSLANTG VDTTSNSFSI MTTSFSESTN AMNTTVIMAT
TSPTSTDVAS TNNDASMTNF LLATMSAGNI TSNSISITTT SFGNSVPFVT TPSPSTDATT
TSNNTNPGMT TYYQTSPTIP THTLTSIPSS ITSILSMFPT SNTFTTDKIT NFTTPTNANT
IIFNTLDTKS TMVIDATVTT TSTKDNTMSP DTTVTSIDKF TTHITQFATP HSATTTTLAL
SHTSLAPTNL SNLGTMDITD ADNSSSVTGN TTHISVSNLT TASVTITATG LDSQTPHMVI
NSVATYLPIT ATSATTDTTN ITKYALNTTT PDSTVHTSAT APTYIANAIN ATQVP
