ID D2HDB2_AILME Unreviewed; 1145 AA.
AC D2HDB2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
DE Flags: Fragment;
GN ORFNames=PANDA_008666 {ECO:0000313|EMBL:EFB14867.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB14867.1};
RN [1] {ECO:0000313|EMBL:EFB14867.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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; GL192710; EFB14867.1; -; Genomic_DNA.
DR RefSeq; XP_002919988.1; XM_002919942.3.
DR AlphaFoldDB; D2HDB2; -.
DR STRING; 9646.ENSAMEP00000012493; -.
DR GeneID; 100474640; -.
DR KEGG; aml:100474640; -.
DR CTD; 4124; -.
DR eggNOG; KOG1958; Eukaryota.
DR HOGENOM; CLU_004690_1_0_1; -.
DR InParanoid; D2HDB2; -.
DR OMA; WRQNWDM; -.
DR OrthoDB; 5474711at2759; -.
DR TreeFam; TF313152; -.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005797; C:Golgi medial cisterna; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0006491; P:N-glycan processing; IEA:Ensembl.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0007033; P:vacuole organization; IEA:Ensembl.
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:SF70; ALPHA-MANNOSIDASE 2; 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 503..589
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT NON_TER 1145
FT /evidence="ECO:0000313|EMBL:EFB14867.1"
SQ SEQUENCE 1145 AA; 131018 MW; 6474A16E890AA9CD CRC64;
MKLSRQFTVF GSAIFCVVIF SLYLMLDRGH LDYPKSPRRE GSFPQGQLSM LQEKIDHLER
LLAENNEIIS NIRDSVINLS ESVEDGPKSS QGNFSQGAGS PLLPSKQSSL VVDPEDCSFA
LQSGSRNSDV QMLDVYSLIP FDNPDGGVWK QGFDISYLFN EWDSKPLQVF VVPHSHNDPG
WLKTFDDYFR EMTQYIFNNM VIKLKEDSRR KFMWSEISYL SKWWDTIDKP KKDAVKSLLQ
NGQFEIVTGG WVMPDEAAAH YFALIDQLIE GHQWVEKNLG VKPRSGWAID PFGHSPTMAY
LLKRAGFSHM LIQRVHYAVK KHFALHKTLE FYWRQNWDLE SGTDIFCHMM PFYSYDIPHT
CGPDPKICCQ FDFKRLPGGR FGCPWGVPPE TIHLGNVQKR AEMLLDQYRK KSKLFRTTVV
LAPLGDDFRY CERTEWDHQF KNYQLLFDYM NSHPEYNVKI QFGTLSDYFD ALDKEDVTIG
KNSQSTFPVL SGDFFTYADR DDHYWSGYFT SRPFYKRMDR ILESHLRAAE ILYYFALKQA
QKYKISKFLS SSHYMALTEA RRNLGLFQHH DAITGTAKDW VVVDYGTRLF HSLTNLKKII
GYSALLLILK DKNSYNSYSF DNLLDTDLKQ NSQGSLPQKT IITLSAEPRY LVVCNPSEQD
RTSVVSVYVS SPTAQVTSAS GKPVEIQMSA VWNTASTVSQ TAYEISFLVQ MPPLGLKVYT
ILESASSDPH LAEYVLHNGN VKDKGIFNMK NVKSTEEDLT LENSFIKLRF GQSGLMEELI
NKEDGKRHEV KVQFSWYGTT SKKDKSGAYL FLPDGEAKPY VYTALPFVRV QHGRFYSDVT
CFLEHVTHRV RLYNIQGIEG QSVEVSNIVD IRKEHNREIA MRISSSINSQ NRFYTDLNGY
QIQPRMTMSK LPLQANVYPM TTMAYIQDAK HRLTLLSAQS LGVSSLKSGQ IEVIMDRRLM
QDDNRGLEQG VHDNKVTANL FRILLEKRSV VNMEEEKKSV SYPSLVSHVT SSFLNHPVFT
MTEKIPVPTL QLLGEFSPLL SSLPCDIHLV NLRTIQSKVD GKHSDEAALI LHRKGFDCRF
SSRDTGLLCS TTHGKILVQK LFSMFTVASL IPSSLSLMHS PPDARNISEI NLSPMEISTF
RIQLR
//
