MA2B2_PIG
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 03-AUG-2022, entry version 116.
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.ENSSSCP00000023573; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PaxDb; Q28949; -.
DR PeptideAtlas; Q28949; -.
DR PRIDE; Q28949; -.
DR GeneID; 396847; -.
DR KEGG; ssc:396847; -.
DR CTD; 23324; -.
DR eggNOG; KOG1959; Eukaryota.
DR InParanoid; Q28949; -.
DR OrthoDB; 201312at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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; 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 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
