ID A0A3B1J4J1_ASTMX Unreviewed; 995 AA.
AC A0A3B1J4J1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN Name=MAN2C1 {ECO:0000313|Ensembl:ENSAMXP00000037148.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000037148.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000037148.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR AlphaFoldDB; A0A3B1J4J1; -.
DR Ensembl; ENSAMXT00000046470.1; ENSAMXP00000037148.1; ENSAMXG00000017902.2.
DR GeneTree; ENSGT01030000234638; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000017902; Expressed in intestine and 14 other cell types or tissues.
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 Gene3D; 2.60.40.2220; -; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 2.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
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 PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 2.
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:UP000018467}.
FT DOMAIN 493..572
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 995 AA; 112367 MW; 5B0EB5795448DFED CRC64;
MYHLPVLKNR RTLLERGEKF ISDVYFTDCN LRGRLYGDTC PLESITVFQT AKRIPYSEAV
QQNFQPCKVG DSFGPTWWTC WFKIALKIPE AWKGKEVHLR WESDGEGMVW RDQEPVQGLT
KEGEKTSYIL TECLTENEPY SITLFVELAC NGLFGAGQGS MIAAPDPNRK YTLQKAELVV
FNSEVQELLT DFEMLLDIVK LLGEGEQRGY QALFTMNEMV NLCDPANPGT WSKARSLAQK
FFSQKNGESQ HIVHAMGHCH IDSAWLWPYE ETIRKCARSW VTAVRLMEKN PEFIFTCSQN
MMQSISLISL SQDGNLPSGE SMVRQFLEGQ NFFKAEFGQY CKEFWLPDTF GYSAQLPQLM
QGSGISRFLT QKLSWNLVNT FPHNTFFWEG INGSLVLTHF PPGNSYEMKG RVEDLINTLK
NNKDKGRANH SAVLFGFGDG GGGPTQLMLD RLQRVQDSDG LPRVHMSNPD RLFSELQADS
SLLCTWSGEL FLELHNGTYT TQAKIKLENR RCEALLHDIE VASCLALTQT AGFEYPTEKL
QKLWRLLLLN QFHDVIPGSC IEIVVEDALE YYNEIEKTGS GLLHSACNAL RTSPWLGAGS
SPAFLNTLPW ERTEVIALTE DGAQTKLVLF SPTHQRSEAW LSELQADGSV RMENGLLSAV
LDNMGRLVSL ILVQTNREAI SDGCFGNQFV VFDDVPLYWD AWDVMDYHLQ TRKPIVDVTR
PVEVVSTGGL RGSVKFSLQI SGKSSITQEV ILDANCPYIK FKTKVDWAEA HKFLKVEFPV
QVRSPNATYE IQFGHLQRPT HRNTSWDWAR FEVWGHKWAD LSEHGFGVAL LNDCKYGYSV
YQNIMTLSLL RAPKAPDANA DMGQHEFTYA VMPHAGSFQE AAVIQHAYNL NFPLRLIHDV
KVAQPWSAFT LNTSAVILET VKQAEGKKNA LVVRLYESHG SSVSAVLSTS LSVQEAWYCD
LLERPDTAHP ASFTGSKISL TFKPFQIISL LLQLH
//
