ID   MA2B2_PONAB             Reviewed;        1009 AA.
AC   Q5RDJ3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 87.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR   EMBL; CR857915; CAH90164.1; -; mRNA.
DR   RefSeq; NP_001125051.1; NM_001131579.1.
DR   AlphaFoldDB; Q5RDJ3; -.
DR   SMR; Q5RDJ3; -.
DR   CAZy; GH38; Glycoside Hydrolase Family 38.
DR   GlyCosmos; Q5RDJ3; 12 sites, No reported glycans.
DR   GeneID; 100171932; -.
DR   KEGG; pon:100171932; -.
DR   CTD; 23324; -.
DR   eggNOG; KOG1959; Eukaryota.
DR   InParanoid; Q5RDJ3; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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   CDD; cd10811; GH38N_AMII_Epman_like; 1.
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   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1009
FT                   /note="Epididymis-specific alpha-mannosidase"
FT                   /id="PRO_0000012080"
FT   REGION          972..992
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:0000255"
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"
SQ   SEQUENCE   1009 AA;  113832 MW;  0F25A14EEA5D30C5 CRC64;
     MGRLYWLPLL APLLLLRPPG VQSAGPIRAF VVPHSHMDVG WVYTVQESMQ AYAANVYTSV
     VEELARGQQR RFIAVEQEFF RLWWGGVASD QQKHQVHQLL EEGRLEFVIG GQVMHDEAVT
     HLDDQILQLT EGHGFLYETF GIRPQFSWHV DPFGASATTP TLFALAGFNA HLSSRIDYDL
     KAAMQEARGL QFVWRGSPSL SEQEEIFTHI MDQYSYCTPS HIPFSNRSGF YWNGVAIFPK
     PPPDGVYPNM SEPVTPANIN LYAEALVANV KQRAAWFRTP HVLWPWGCDK QFFNASVQFA
     NMNPLLDHIN SHAAKLGVSV QYATLGDYFR ALHTLNITWR VRDHHDFLPY STEPFQAWTG
     FYTSRSALKG LARRASALLY AGESMFTHYM WPAPCGHLDP TWALQQLQQL RWAVSEVQHH
     DAITGTESPK VRDMYVMHLA SGMLGVRKLM ASIILDKLQP QAPMAASSGA GPAGHFASVY
     NPLAWTVTTI VTLTVGFPGV HVTDEAGHPV PSQIQNSTET PSVYDLLILT TIPGLSYRHY
     SIRPTAGAQE GTQEPAATVA TTLQFGRRLR RRTSHVGRHL VPVANDCYTV LLDQDTNLMH
     SIWERQSNQT VRVTQEFLEY HVNGDVKQGP ISDNYLFTPG KAAVPAWEAV EMEIVAGQLV
     TEIRQYFYRN MTARNYTYAI RSRLTHVPQG HDGELLCHRI EQEYQAGPLE LNREAVLRTS
     TNLNSQQVIY SDNNGYQMQR RPYVSYVNNS IARNYYPMVQ SAFMEDGKSR LVLLSERAHG
     ISSQGNGQVE VMLHRRLWNN FDWDLGYNLT LNDTSIVHPV LWLLLGSWSL TTALRQRSAM
     ALQHRPVVLF GDLAGTAPKL PGPQQQEAVT LPPNLHLQIL SIPGWRYSSN HTEHAQNLRK
     GNRGEVQADL HRVLLRLHHL YEVGEDPVLS QPVTVNLEAV LQALGSVVAV EERSLTGTWD
     VSMLHRWSWR TGSGRRRGDT TSPSRPPGGP IITVHPKEIR TFFIHFQQQ
//