ID   A0A2D0SCP8_ICTPU        Unreviewed;      1143 AA.
AC   A0A2D0SCP8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   Name=man2a2 {ECO:0000313|RefSeq:XP_017340499.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017340499.1};
RN   [1] {ECO:0000313|RefSeq:XP_017340499.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017340499.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_017340499.1; XM_017485010.3.
DR   AlphaFoldDB; A0A2D0SCP8; -.
DR   GeneID; 108274717; -.
DR   CTD; 4122; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000221080; Chromosome 14.
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   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        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          495..581
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1143 AA;  129859 MW;  B7EDE5D639B06E1E CRC64;
     MKLKKQVTVC GGAIFCVAVF SLYLMLDRVQ HDPARRQNGG NFPRNRIEQL EQLLEENHQI
     ISHIKDSVLE LTDTGAISPS GQLPFRSANG SWVLPFDGRP TFLTIKPQDC QFALGRHGQS
     DLQMLDVYSL LSFDNVDGGV WKQGFDITYE PSEWDNEPLQ VFVVPHTHND PGWIKTFDKY
     YNDQTQHILN NMVVKLAEDP RRKFIWSEIS FFVKWWESVG ADKHEAIRKL ILGGQLEMVT
     GGWVMTDEAN SHYFAMIDQL IEGHQWLEKN LGVTPRSGWA IDPFGHSATM PYLLKKANLT
     SMLIQRVHYS VKKHFASTQN LEFMWRQAWD RESGTDLFCH MMPFYSYDVP HTCGPDPKVC
     CQFDFKRLPG SRINCPWKVP PRAISEANVA ERVQALLDQY RKKSKLFRSK VLLVPLGDDF
     RYDKAQEWDQ QYINYQKLFD YMNSHPELHV KAQFGTLTDY FNAVYKANGV GQGMRPPGYP
     VLSGDFFAYA DREDHYWSGY YTSRPFYKNL DRVLESHLRG AEILYSLAVA HARHAGMEGR
     YPTSDYSLLT DARRNIALFQ HHDAITGTAK EAVVIDYGTR LLRSLVGLKR VIINAAHFLI
     MKNKDVYRFY QTEPFLETDD RRATQDSLPQ RTLIELDSSP RYLVLFNPVE QERLCVVTVL
     VNSARVRVLT EDGQTLPVQL SAQWSSAVQM DGEVYQASFM TRLPALGLAV FHLYDSIDSP
     MTLRSDTLLR VSGRSQTVHG LDPLPVRSQV ADSQPFYIQT QSLTLGFSGT TGLLESIRRK
     DDPQEVRVQI QFLTYGTRAS KDKSGAYLFL PDGIAMPYVQ IEPPTVRVVE GPLFSEVVAY
     YQHFQQTVCI HNVPGIDGLS LDITTLVDIR DQSNKELAMR LVTDIQSEDT FYTDLNGFQI
     QPRRYFQKIP LQANFYPMPT MAYIQDSQYR LTLHTAQALG VSSLASGQLE VILDRRLMQD
     DNRGLGQGLK DNKRTANRFR LLLERRSSSS RAVDSGPVSF PSLLSHLTSA ILNHEVLALP
     VVPKKRGVPP LRTFSPLATA LPCDFHLLNL RSIQNQDASS PSPHTALLLH RLGLDCSLEL
     QNPGFNCTTT QGKLAVSGLF RGLDLQLLQP MSLTLMFSEP PLSNNSVISL EPMELSAYKL
     KLH
//