ID   MA2B2_PIG               Reviewed;         995 AA.
AC   Q28949;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   24-JAN-2024, entry version 122.
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;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Epididymis;
RX   PubMed=8562059; DOI=10.1002/mrd.1080420203;
RA   Okamura N., Tamba M., Liao H.-J., Onoe S., Sugita Y., Dacheux F.,
RA   Dacheux J.-L.;
RT   "Cloning of complementary DNA encoding a 135-kilodalton protein secreted
RT   from porcine corpus epididymis and its identification as an epididymis-
RT   specific alpha-mannosidase.";
RL   Mol. Reprod. Dev. 42:141-148(1995).
CC   -!- FUNCTION: Can digest both p-nitro-phenyl-alpha-D-mannoside and high
CC       mannose oligosaccharide (Man(8)-GlcNAc(2)). May be involved in sperm
CC       maturation. Has a possible role in specific sperm-egg interaction since
CC       sperm surface mannosidase acts like a receptor for mannose-containing
CC       oligosaccharides located on the zona pellucida.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5.;
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Found at the sperm surface as a 27
CC       kDa fragment.
CC   -!- TISSUE SPECIFICITY: Specific to the caput and corpus of the epididymis.
CC   -!- PTM: Processed into a 27 kDa fragment localized on the equatorial
CC       segment and the apical rim of the head of mature sperm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA05877.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D28521; BAA05877.1; ALT_INIT; mRNA.
DR   PIR; T42762; T42762.
DR   RefSeq; NP_999014.1; NM_213849.1.
DR   AlphaFoldDB; Q28949; -.
DR   SMR; Q28949; -.
DR   STRING; 9823.ENSSSCP00000065480; -.
DR   CAZy; GH38; Glycoside Hydrolase Family 38.
DR   GlyCosmos; Q28949; 8 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000023573; -.
DR   PeptideAtlas; Q28949; -.
DR   GeneID; 396847; -.
DR   KEGG; ssc:396847; -.
DR   CTD; 23324; -.
DR   eggNOG; KOG1959; Eukaryota.
DR   InParanoid; Q28949; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
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; 2.60.40.1360; -; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
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   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF28; EPIDIDYMIS-SPECIFIC ALPHA-MANNOSIDASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Metal-binding; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..21
FT   CHAIN           22..995
FT                   /note="Epididymis-specific alpha-mannosidase"
FT                   /id="PRO_0000012079"
FT   REGION          956..977
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         411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        593
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        657
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        733
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        793
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        875
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        977
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        945
FT                   /note="D -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   995 AA;  114230 MW;  79D21B8CE5AE6FC2 CRC64;
     MGPHSWLPLF MQLALLGPQW ALHFYKVKVF VVPHSHMDVG WLHTVQESMQ VYVPDVYNSV
     VEALTRGKRR RFIAVEQEYF RLWWDGFASA KRKQQVRQLL AEQRLEFVLG GQVMHDEAVT
     HFDDQILQLT EGHGFLYETF GIRPQFSWQV DPFGASATTP TLLALAGFNG HIISRIDYDL
     KDTMQHTQGL QFVWRGSRSL EARQEIFTHV LDQYSYCSDG FMWNGSPRFP DRPFDMDYSA
     VEMPVSQDSM NHYVLNLVDN VNKRAAWFRT QHVLWPWGCD RQFFNASQQF ANMDRLMDHI
     NKHTPELGIS MQYATLAEYF QAVFAQDVSW QVRDHRDFLP YSSAPEQTWT GFYTSQSGLK
     RLARRASALL YAGESLFTRY MLSAAHRFLD PAWALTQLQQ LRWAVSEVQH HDGITGTHIL
     AVRDMFVEHL TTGMAGVRKL MDSIAQDMPL THSGPEPGGH VAMVYNPLAW TVTTVITLTV
     SFPEVSVTDE SGRPVLAQVQ DSKETPSAYD LHVLTTIPGL SYQHYIIKPI RKAREDSQEA
     AATVPSTIQF GLKLRRQDGQ VGRNLVPVKN SCYTVFLDKD TNLMHSIWER QSNRTVRMSQ
     EFLAYRSVYG YEEAVTSDNY LFTPNGTAEP AWAAVRMEVV EGQLLSEIRQ YFYRQANDSD
     HTYAIYSRLA HGPQDSAGEL LCHRIEQEYR VGPLELNHEV VLRTSTSLNT GLVLYSDNNG
     YQMQRRTYRH DRNNSVSLNY YPMAQSAFIQ DGGSRLVLLS EQAHGVSSQG NGQVEVMLHR
     RLWNKLEWTL QYNLTHDVTS VVRPVLWLLL GPRTLTTGLR QRSGLELQHR PVVLFRELGG
     TVQNGPGPRK QEPVTLPPSL HLQILSIPGW KYSSNHTVHL KNLQKGHYRR AKADFRRVLL
     RLHHLYEAGE HQALSRPVTL NLQSVLRGLG SVVAVEERSL TGTWDVNSLH RWSWKTEDGH
     HHRGSSRRPL PPLRGPNVTI HPKEIRTFFI HFQEQ
//