ID F1MPT2_BOVIN Unreviewed; 956 AA.
AC F1MPT2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Glycoside hydrolase family 38 central domain-containing protein {ECO:0000259|SMART:SM00872};
GN Name=LOC781835 {ECO:0000313|Ensembl:ENSBTAP00000039261.5};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000039261.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000039261.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000039261.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000039261.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000039261.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR AlphaFoldDB; F1MPT2; -.
DR Ensembl; ENSBTAT00000039467.5; ENSBTAP00000039261.5; ENSBTAG00000017829.6.
DR VEuPathDB; HostDB:ENSBTAG00000017829; -.
DR eggNOG; KOG1959; Eukaryota.
DR GeneTree; ENSGT01030000234638; -.
DR HOGENOM; CLU_004690_3_0_1; -.
DR TreeFam; TF332447; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000017829; Expressed in corpus epididymis and 5 other cell types or tissues.
DR ExpressionAtlas; F1MPT2; baseline.
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; 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; 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:SF28; EPIDIDYMIS-SPECIFIC ALPHA-MANNOSIDASE; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 312..392
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 492..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 109234 MW; 2BC1FEE97A83EE90 CRC64;
ALVPSQITVF VVPHHLVTQA YVTTVYTSVV EDLTRNKQHR FIIVDQEFFR LWWDGVASAK
QKVQVHELVA QRRLEFVLGG QVMHDEAVTH VDDQILQLTE GHGFLYETFG IQPQFSWQVY
SFGASTTTPT LFALAGFSGH IISRIDYDLK VTMQQKQMQF VWRGSKSLMA QQETFTHDLD
ENGYCLGTEK HPEHRAWELV WELVAHQGEW ERVEEELTLF SLGSASRSAG CCFWPTGLQC
FSAICQHGPS DELHQQPHTQ DRCLLGVRHT DYFQAIHSTH ISWHIRNHHN FLPYSSGDLT
PTPGLFLLDM FHSGTGFYAS RSGLKGLARR ASALLYAGES MFTRFMLAPH RFLDQAWGLQ
QLQKLRWAVS EVTPHLSGLT PPKVRDMFVE HLGAGMQGVC KLMASIIQDR PAAPSAGPGG
HFAMVYHPLA WTVTTIVTPT ADFPEVNLTD ETGNPVPAQV QNSKETPSAY DLLVLTTIPG
FSYRHYVIRP MRRAQKDTQE TGASVDSTKQ FGRRPRTNRR QAGRRPVHME NDCYTVYLDK
DTNLMHSIWE RQSNRTIQVT QEFMEYHDNS DEGQISISNN YVFAPNGTSK PVWAAVEMEI
LEGQLLTEIQ RCFYRTVNDR DPTYTIYSQL ARGPPGADGE LLCHRIEQEY RVGPLELNHE
AIWRTSTHLN TAQVLYSDNN GYQMQRRAYK QYMVNTITRN YYPMTQSAFI QDRQSRLVLL
SEQVHGVSSQ GSGQMEDFFH RQLLIKQQWA LSVNVTLNDT SVVHSVLWLL LGPSTLTRDL
GQRSGVALQH RPVVLIRELS ETTRVHPDFQ QQEAVMLPPS LHLQILSIPG WTYNLNHTKH
LQNLQKGHQG QAKVDFCRVL LWLHHLYEKG QHPVLSQPVM VNLQSVLWSL GSVVSMEECS
LTGTWDVGTL QRWSWKIQDG HQHRGGAHRP LPPHRGPDIA IHPKEIRMFF IHFQEQ
//
