ID   F1RMI9_PIG              Unreviewed;      1167 AA.
AC   F1RMI9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:HDA96764.1};
RN   [1] {ECO:0000313|EMBL:HDA96764.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361199};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR   EMBL; DQIR01141288; HDA96764.1; -; Transcribed_RNA.
DR   RefSeq; XP_001929413.2; XM_001929378.4.
DR   AlphaFoldDB; F1RMI9; -.
DR   PeptideAtlas; F1RMI9; -.
DR   GeneID; 100154397; -.
DR   KEGG; ssc:100154397; -.
DR   CTD; 4122; -.
DR   HOGENOM; CLU_004690_1_0_1; -.
DR   OrthoDB; 5474711at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
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; cd11667; GH38N_Man2A2; 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:SF57; ALPHA-MANNOSIDASE 2X; 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   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   TRANSMEM        24..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          519..605
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1167 AA;  132542 MW;  9C9B3F1999001DFE CRC64;
     MREELCQALF LVCVEASMKL KKQVTVCGAA IFCVAVFSLY LMLDRVQHDP TRHQNGGNFP
     RSQISVLQNR IEQLEQLLEE NHEIISHIKD SVLELTANVE GPPALLPYSM ANGSWVVPPE
     PRPSFFSVSP QDCQFALGSR GQKPELQMLA LSEELPFDNL DGGVWKQGFD ISYSPHDWDT
     EDLQVFVVPH SHNDPGWLKT FDKYYTEQTQ HILNNMLSKL QEDPRRRFLW AEVSFFAKWW
     DNINAQKRAA VRRLVGNGQL EIATGGWVMP DEANSHYFAL IDQLIEGHQW LEKNLGATPR
     SGWAVDPFGY SSTMPYLLRR ANLTSMLIQR VHYTIKKHFA ATHSLEFMWR QTWDSDSSTD
     IFCHMMPFYS YDVPHTCGPD PKICCQFDFK RLPGGRINCP WKVPPRAITE ANVAERAGLL
     LDQYRKKSRL FRSNVLLVPL GDDFRYDKPQ EWDAQFFNYQ RLFDFLNSKP DLHVQAQFGT
     LSDYFDALYK RTGVEPGARP PGFPVLSGDF FSYADREDHY WTGYYTSRPF YKGLDRVLEA
     HLRGAEILYS LAVAHARRSG LASQYPLSNL ALLTEARRTL GLFQHHDAIT GTAKEAVVVD
     YGVRLLRSLV NLKQVIINAA HYLVLGDKET YHFDPEAPFL QMDDSRTNHD ALPERTVIQL
     ESSPRYVVLF NPLEQERLSL VSLLVNSPRV RVLSEEGQPL AIQISVHWSS ATDLVPDVYQ
     VSVPVRLPAL GLSVLQLQLG LDGPRTLPSS VRVYLYGRQL SVSRHEAFPI RVIDSGTSDF
     ALSNRYMQVW FSGLTGLLKS IQRVDEEQER RVDTEFLIYG TRTSKDKSGA YLFLPDGEAK
     PYVPKDPPVL RITEGPFFSE VVAHYEHVHQ IVRLYNLPGV EGLSLDMSFL VDIRDYINKE
     LALRIHTDIN SQATFFTDLN GFQVQPRRFL KKLPLQANFY PMPVMAYLQD AQNRLTLHTA
     QALGVSSLRS GQLEVILDRR LMQDDNRGLG QGLKDNKRTC NHFRLLLERR TPVREVHDGL
     PTSYPSLLSH LTSMYLNTPV FALPVAKKQP PGLALRSFHP LASSLPCDFH LLNLRSLQAK
     DENVPAAETA LILHRKGFDC GLEAKNLGFN CTTSQGKVAL GSLFHGLDVL FLQPTSLTLL
     YPLASPSNST DIFVEPMEIA TFCLRLG
//