MA2B2_HUMAN
ID MA2B2_HUMAN Reviewed; 1009 AA.
AC Q9Y2E5; Q66MP2; Q86T67;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Epididymis-specific alpha-mannosidase;
DE EC=3.2.1.24;
DE AltName: Full=Alpha-1,6-mannosidase;
DE AltName: Full=Mannosidase alpha class 2B member 2;
DE Flags: Precursor;
GN Name=MAN2B2; Synonyms=KIAA0935;
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 MRNA] (ISOFORM 1), AND VARIANT MET-320.
RC TISSUE=Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-243;
RP VAL-446 AND SER-541.
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1009 (ISOFORM 2), AND VARIANTS
RP PRO-243; VAL-446 AND SER-541.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [5]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-516.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC Q9Y2E5; Q92624: APPBP2; NbExp=3; IntAct=EBI-12243024, EBI-743771;
CC Q9Y2E5; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-12243024, EBI-1045797;
CC Q9Y2E5; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-12243024, EBI-18013275;
CC Q9Y2E5; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12243024, EBI-6942903;
CC Q9Y2E5; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-12243024, EBI-3918971;
CC Q9Y2E5; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12243024, EBI-11721746;
CC Q9Y2E5; O95279: KCNK5; NbExp=3; IntAct=EBI-12243024, EBI-3934936;
CC Q9Y2E5; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-12243024, EBI-751260;
CC Q9Y2E5; Q9H400: LIME1; NbExp=3; IntAct=EBI-12243024, EBI-2830566;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2E5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2E5-2; Sequence=VSP_013816;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; AL833071; CAD89971.1; -; mRNA.
DR EMBL; AC004480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033307; AAH33307.1; -; mRNA.
DR EMBL; AB023152; BAA76779.2; -; mRNA.
DR CCDS; CCDS33951.1; -. [Q9Y2E5-1]
DR RefSeq; NP_001278967.1; NM_001292038.1.
DR RefSeq; NP_056089.1; NM_015274.2. [Q9Y2E5-1]
DR AlphaFoldDB; Q9Y2E5; -.
DR SMR; Q9Y2E5; -.
DR BioGRID; 116912; 118.
DR IntAct; Q9Y2E5; 17.
DR MINT; Q9Y2E5; -.
DR STRING; 9606.ENSP00000285599; -.
DR BindingDB; Q9Y2E5; -.
DR ChEMBL; CHEMBL2682; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR GlyConnect; 1216; 10 N-Linked glycans (3 sites).
DR GlyGen; Q9Y2E5; 14 sites, 10 N-linked glycans (3 sites), 2 O-linked glycans (2 sites).
DR iPTMnet; Q9Y2E5; -.
DR PhosphoSitePlus; Q9Y2E5; -.
DR BioMuta; MAN2B2; -.
DR DMDM; 296439484; -.
DR EPD; Q9Y2E5; -.
DR jPOST; Q9Y2E5; -.
DR MassIVE; Q9Y2E5; -.
DR MaxQB; Q9Y2E5; -.
DR PaxDb; Q9Y2E5; -.
DR PeptideAtlas; Q9Y2E5; -.
DR PRIDE; Q9Y2E5; -.
DR ProteomicsDB; 85747; -. [Q9Y2E5-1]
DR ProteomicsDB; 85748; -. [Q9Y2E5-2]
DR Antibodypedia; 22659; 87 antibodies from 20 providers.
DR DNASU; 23324; -.
DR Ensembl; ENST00000285599.8; ENSP00000285599.3; ENSG00000013288.9. [Q9Y2E5-1]
DR GeneID; 23324; -.
DR KEGG; hsa:23324; -.
DR MANE-Select; ENST00000285599.8; ENSP00000285599.3; NM_015274.3; NP_056089.1.
DR UCSC; uc003gjf.2; human. [Q9Y2E5-1]
DR CTD; 23324; -.
DR DisGeNET; 23324; -.
DR GeneCards; MAN2B2; -.
DR HGNC; HGNC:29623; MAN2B2.
DR HPA; ENSG00000013288; Low tissue specificity.
DR MIM; 618899; gene.
DR neXtProt; NX_Q9Y2E5; -.
DR OpenTargets; ENSG00000013288; -.
DR PharmGKB; PA128394625; -.
DR VEuPathDB; HostDB:ENSG00000013288; -.
DR eggNOG; KOG1959; Eukaryota.
DR GeneTree; ENSGT01030000234638; -.
DR InParanoid; Q9Y2E5; -.
DR OMA; VVAHSHM; -.
DR OrthoDB; 201312at2759; -.
DR PhylomeDB; Q9Y2E5; -.
DR TreeFam; TF332447; -.
DR PathwayCommons; Q9Y2E5; -.
DR Reactome; R-HSA-8853383; Lysosomal oligosaccharide catabolism.
DR SignaLink; Q9Y2E5; -.
DR BioGRID-ORCS; 23324; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; MAN2B2; human.
DR GeneWiki; MAN2B2; -.
DR GenomeRNAi; 23324; -.
DR Pharos; Q9Y2E5; Tbio.
DR PRO; PR:Q9Y2E5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9Y2E5; protein.
DR Bgee; ENSG00000013288; Expressed in tendon of biceps brachii and 205 other tissues.
DR ExpressionAtlas; Q9Y2E5; baseline and differential.
DR Genevisible; Q9Y2E5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:Ensembl.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1009
FT /note="Epididymis-specific alpha-mannosidase"
FT /id="PRO_0000012077"
FT REGION 972..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 939..1009
FT /note="AVLQALGSVVAVEERSLTGTWDLSMLHRWSWRTGPGRHRGDTTSPSRPPGGP
FT IITVHPKEIRTFFIHFQQQ -> VNFPTPIQTISQGSKP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_013816"
FT VARIANT 243
FT /note="Q -> P (in dbSNP:rs2301796)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_025328"
FT VARIANT 320
FT /note="V -> M (in dbSNP:rs2301795)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_025329"
FT VARIANT 365
FT /note="R -> C (in dbSNP:rs6858328)"
FT /id="VAR_055840"
FT VARIANT 446
FT /note="M -> V (in dbSNP:rs2301790)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_025330"
FT VARIANT 541
FT /note="N -> S (in dbSNP:rs2301788)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_025331"
FT CONFLICT 79
FT /note="F -> S (in Ref. 1; CAD89971)"
FT /evidence="ECO:0000305"
FT CONFLICT 938
FT /note="E -> Q (in Ref. 1; CAD89971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1009 AA; 113979 MW; 21BB879400E0F387 CRC64;
MGQLCWLPLL APLLLLRPPG VQSAGPIRAF VVPHSHMDVG WVYTVQESMR AYAANVYTSV
VEELARGQQR RFIAVEQEFF RLWWDGVASD QQKYQVRQLL EEGRLEFVIG GQVMHDEAVT
HLDDQILQLT EGHGFLYETF GIRPQFSWHV DPFGASATTP TLFALAGFNA HLGSRIDYDL
KAAMQEARGL QFVWRGSPSL SERQEIFTHI MDQYSYCTPS HIPFSNRSGF YWNGVAVFPK
PPQDGVYPNM SEPVTPANIN LYAEALVANV KQRAAWFRTP HVLWPWGCDK QFFNASVQFA
NMDPLLDHIN SHAAELGVSV QYATLGDYFR ALHALNVTWR VRDHHDFLPY STEPFQAWTG
FYTSRSSLKG LARRASALLY AGESMFTRYL WPAPRGHLDP TWALQQLQQL RWAVSEVQHH
DAITGTESPK VRDMYATHLA SGMLGMRKLM ASIVLDELQP QAPMAASSDA GPAGHFASVY
NPLAWTVTTI VTLTVGFPGV RVTDEAGHPV PSQIQNSTET PSAYDLLILT TIPGLSYRHY
NIRPTAGAQE GTQEPAATVA STLQFGRRLR RRTSHAGRYL VPVANDCYIV LLDQDTNLMH
SIWERQSNRT VRVTQEFLEY HVNGDVKQGP ISDNYLFTPG KAAVPAWEAV EMEIVAGQLV
TEIRQYFYRN MTAQNYTYAI RSRLTHVPQG HDGELLCHRI EQEYQAGPLE LNREAVLRTS
TNLNSQQVIY SDNNGYQMQR RPYVSYVNNS IARNYYPMVQ SAFMEDGKSR LVLLSERAHG
ISSQGNGQVE VMLHRRLWNN FDWDLGYNLT LNDTSVVHPV LWLLLGSWSL TTALRQRSAL
ALQHRPVVLF GDLAGTAPKL PGPQQQEAVT LPPNLHLQIL SIPGWRYSSN HTEHSQNLRK
GHRGEAQADL RRVLLRLYHL YEVGEDPVLS QPVTVNLEAV LQALGSVVAV EERSLTGTWD
LSMLHRWSWR TGPGRHRGDT TSPSRPPGGP IITVHPKEIR TFFIHFQQQ
