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Database: UniProt
Entry: W5UCS5_ICTPU
LinkDB: W5UCS5_ICTPU
Original site: W5UCS5_ICTPU 
ID   W5UCS5_ICTPU            Unreviewed;       986 AA.
AC   W5UCS5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   Name=MAN2B1 {ECO:0000313|EMBL:AHH39379.1};
GN   Synonyms=man2b1 {ECO:0000313|RefSeq:XP_017314503.1};
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|EMBL:AHH39379.1};
RN   [1] {ECO:0000313|EMBL:AHH39379.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mixed {ECO:0000313|EMBL:AHH39379.1};
RX   PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA   Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA   Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA   Peatman E., Liu Z.;
RT   "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT   Seq analysis of a doubled haploid homozygote.";
RL   BMC Genomics 13:595-595(2012).
RN   [2] {ECO:0000313|RefSeq:XP_017314503.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017314503.1};
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   EMBL; JT411314; AHH39379.1; -; mRNA.
DR   RefSeq; XP_017314503.1; XM_017459014.3.
DR   STRING; 7998.ENSIPUP00000004064; -.
DR   Ensembl; ENSIPUT00000004258; ENSIPUP00000004064; ENSIPUG00000002847.
DR   GeneID; 108259485; -.
DR   KEGG; ipu:108259485; -.
DR   CTD; 4125; -.
DR   OMA; LEFIWRP; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000221080; Chromosome 27.
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; cd10810; GH38N_AMII_LAM_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; 2.
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   InterPro; IPR048534; Man2a1-like_dom.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF3; LYSOSOMAL 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   Pfam; PF21260; Laman-like_dom; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199}; Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           24..986
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5013540152"
FT   DOMAIN          368..447
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   986 AA;  111280 MW;  690D24373905DF2E CRC64;
     MAADRLFPLA GFLLLCSAAG VWCFPSLREP VCGYKSCPAT KPSMLNVHLV PHTHDDVGWL
     KTVDQYYYGG RNNIQHAGVQ YILDSVVSEL QKDPARRFIY VETAFFYRWW KQQDQQTRNI
     VTQLVEQGRL EFVNGGWCMS DEASTHYSAV IDQMTLGLRF LNDTFGDCGR PRVAWHIDPF
     GHAREHASMF AQMGYDGLFF GRLDYQDKAR RMKMQEMEMV WRASESLEPP TADLFTGVLP
     NGYNPPDGFC WDQSCSDAPV QDDPDLEDYN VDQLVDAFIN LSGVQAEKYK TNHIIMTMGS
     DFQYENAIPW YKNMDKLIHY VNARQVQGSR VHVLYSTPSC YLQELNLANF TWPLKTDDFF
     PYADAAHDFW TGYFTSRPAL KRYERLSNSF LQTCNQLEVL GGLKSTHGPF GEGNSDTLKR
     AMAVAQHHDA VSGTEKQHVA DDYAKRLAIG SAHCQVLVSN SLAFLSGSEV PRVFCENLNI
     SACPLTESSK QFLLNVYNPL ARPVSWSVHL PVNGTVYNVT DSDGAPVDNQ VIPVSKATRA
     LRRDRGSAQF ELVFQVQAPS MGFNTYTVTL LKNSPAPASI KPVAPPSIQN KYLKVTFDTQ
     TGLVSGLTNL ETQQTIKLTQ NFYWYNASVG NSESLQPSGA YIFRPNSSTP VIINTKPEVT
     TLQNSVVQEV RQQFSPWVSQ VIRLYTESKH LELEWTVGPI PVNDGFGKEV ITRLDSSIET
     EGYFYTDSNG REILQRRKDY RPTWDLKQTE PIAGNYYPIN TRAFIKDEQN QMTVVTDRSQ
     GIGSIYNGSL EIMVHRRLLR DDNRGVAEPL SEPGEYYDGL AVRGRLLLAL TPPSTAADTH
     RPLGQEMVFQ PTLSFQQGAT HSTTPQFSGL ISALPPAVHV LTLSQWDQDS VLLRLEHQYE
     RSESHAHSQP ITISLQKLFS TLDVVGVSEM SLGANQWKED MKRMQWKPDS GETAVPLHEH
     VGDPSSWEIT LNPMEIRTFL LRVRHK
//
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