MA2B2_MOUSE
ID MA2B2_MOUSE Reviewed; 1018 AA.
AC O54782; Q69ZV1; Q8BH85; Q9DBK2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Epididymis-specific alpha-mannosidase;
DE EC=3.2.1.24;
DE AltName: Full=Mannosidase alpha class 2B member 2;
DE Flags: Precursor;
GN Name=Man2b2; Synonyms=Kiaa0935;
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].
RC STRAIN=ddY; TISSUE=Testis;
RX PubMed=9425289; DOI=10.1006/bbrc.1997.7768;
RA Hiramoto S., Tamba M., Kiuchi S., Jin Y.-Z., Bannai S., Sugita Y.,
RA Dacheux F., Dacheux J.-L., Yoshida M., Okamura N.;
RT "Stage-specific expression of a mouse homologue of the porcine 135kDa
RT alpha-D-mannosidase (MAN2B2) in type A spermatogonia.";
RL Biochem. Biophys. Res. Commun. 241:439-445(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hiramoto S., Noguchi J., Endoh Y., Tamba M., Okamura N.;
RT "Locarization of a mouse homologue of the porcine 135kDa a-D-mannosidase,
RT mMAN2B2, in acrosome and its involvement in the sperm-egg interaction.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Thymus;
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 MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 763-1018.
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
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: Plays an important role in the early step of spermatogenesis.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the narrow region between the
CC caput and corpus epididymis.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in type A spermatogonia at
CC stages IX-XI of spermatogenesis. Detected there until the cell
CC developed into type B spermatogonia.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; AB006458; BAA24266.1; -; mRNA.
DR EMBL; AB083124; BAC53862.1; -; Genomic_DNA.
DR EMBL; AK004900; BAB23655.1; -; mRNA.
DR EMBL; AK040388; BAC30580.1; -; mRNA.
DR EMBL; BC066211; AAH66211.1; -; mRNA.
DR EMBL; AK173067; BAD32345.1; -; mRNA.
DR CCDS; CCDS19243.1; -.
DR PIR; JC5799; JC5799.
DR RefSeq; NP_032576.2; NM_008550.2.
DR AlphaFoldDB; O54782; -.
DR SMR; O54782; -.
DR BioGRID; 201306; 4.
DR STRING; 10090.ENSMUSP00000031002; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR GlyGen; O54782; 10 sites.
DR iPTMnet; O54782; -.
DR PhosphoSitePlus; O54782; -.
DR EPD; O54782; -.
DR MaxQB; O54782; -.
DR PaxDb; O54782; -.
DR PeptideAtlas; O54782; -.
DR PRIDE; O54782; -.
DR ProteomicsDB; 252707; -.
DR Antibodypedia; 22659; 87 antibodies from 20 providers.
DR DNASU; 17160; -.
DR Ensembl; ENSMUST00000031002; ENSMUSP00000031002; ENSMUSG00000029119.
DR GeneID; 17160; -.
DR KEGG; mmu:17160; -.
DR UCSC; uc008xfb.2; mouse.
DR CTD; 23324; -.
DR MGI; MGI:1195262; Man2b2.
DR VEuPathDB; HostDB:ENSMUSG00000029119; -.
DR eggNOG; KOG1959; Eukaryota.
DR GeneTree; ENSGT01030000234638; -.
DR HOGENOM; CLU_004690_3_0_1; -.
DR InParanoid; O54782; -.
DR OMA; VVAHSHM; -.
DR OrthoDB; 201312at2759; -.
DR PhylomeDB; O54782; -.
DR TreeFam; TF332447; -.
DR Reactome; R-MMU-8853383; Lysosomal oligosaccharide catabolism.
DR BioGRID-ORCS; 17160; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Man2b2; mouse.
DR PRO; PR:O54782; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O54782; protein.
DR Bgee; ENSMUSG00000029119; Expressed in spermatocyte and 182 other tissues.
DR ExpressionAtlas; O54782; baseline and differential.
DR Genevisible; O54782; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:InterPro.
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 Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1018
FT /note="Epididymis-specific alpha-mannosidase"
FT /id="PRO_0000012078"
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 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 201
FT /note="S -> T (in Ref. 1; BAA24266)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="M -> I (in Ref. 3; BAB23655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1018 AA; 115610 MW; 41AD7AAEA7CC88A9 CRC64;
MGPLRWLPLL GQLLLLWPRA AQPAGPIRAF VVPHSHMDVG WVFTVQESMR AYAANVYTTV
VAELVRGGQR RFIAVEQEFF RLWWDGVASE QQKQQVRQLL HEGRLEFVLG GQVMHDEAVT
HLDDQILQLT EGHGFLYETF GIRPQFSWHV DPFGASATTP TLFALAGFNA HLISRIDYDL
KDAMQEAQML QFVWHGSPSL SGQQEIFTHV MDHYSYCTPS HIPFSNRSGF YWNGVAVFPE
PPPDGVYPNM SEPVTGANIH LYAEALVANV KQRAAWFRTP HVLWPWGCDK QFFNASVQFD
NMDPLLDYIN QRTAQFGISV QYATLNDYFQ ALHATNMTWG IRDHQDFLPY SSEPLQAWTG
FYTSRSTLKG LARQASALLY AGESMFTRYM WPDPSGTLDP TWALQQLQQL RWAVSEVQHH
DAITGTESPK VKNMYTEHLR MGMLGVRKLM VSIALGGPPG SGTGAPKDIM GPQVTPVLSV
DTRPVGYSAS VYNPLAWKIT TIITLTVAFP NVSVTDELGH PVSTQIQNST KDPSAYDLLI
LTTIPGLNYR HYQVMHARGD QAGTRELVAP RANTLKFSLK LRNQPSQEGK RLVPVMNDCY
ILLFDQDTNM LHSIQDRQSN RTVRMTQEFL EYQANWDVKQ GPISDNYLFA PNNTAEPSWE
AVGMEMVAGT LVTDIRQYFY RYITDQEYIY SIHTRLAHPS LAGELLCQRI EQQYRVGPLD
LNREAILRTS SDLNSQQVLY SDNNGYQMQR RPYKAFKSNP IPRNYYPMVQ SAFIEDDKSR
LVLLAERPHG VSSQGNGQVE VMLHRRLWNN LAWDLKYNLT LNDTSIVHPV LWLMLGPKST
MTALHPRSGV ALQHGPVVLL KELADEETPV HGPHNPWPVT LPPNLHLQIL SVPGWTYSRS
HAQHLRNLQR GHPEKPQANL QRVLLRLRHL YEAGEDPVLS RPATVDLKVV LRGLGSVVAV
EERSLTGTWD VQMLQRWHWS TKTDHLKGHP TSPPRPPGGS IITVYPKEIR TFFIKFQQ
