MA2C1_RAT
ID MA2C1_RAT Reviewed; 1040 AA.
AC P21139;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Alpha-mannosidase 2C1;
DE EC=3.2.1.24 {ECO:0000269|PubMed:2211613};
DE AltName: Full=Alpha-D-mannoside mannohydrolase;
DE AltName: Full=Mannosidase alpha class 2C member 1;
GN Name=Man2c1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2211613; DOI=10.1016/s0021-9258(17)44876-9;
RA Bischoff J., Moremen K., Lodish H.F.;
RT "Isolation, characterization, and expression of cDNA encoding a rat liver
RT endoplasmic reticulum alpha-mannosidase.";
RL J. Biol. Chem. 265:17110-17117(1990).
CC -!- FUNCTION: Cleaves alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose
CC residues from glycoproteins (PubMed:2211613). Involved in the
CC degradation of free oligosaccharides in the cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:Q9NTJ4, ECO:0000269|PubMed:2211613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC Evidence={ECO:0000269|PubMed:2211613};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q9NTJ4};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NTJ4}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in testis,
CC adrenal gland, and kidney. {ECO:0000269|PubMed:2211613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M57547; AAA41565.1; -; mRNA.
DR PIR; A38306; A38306.
DR RefSeq; NP_640349.1; NM_139256.1.
DR AlphaFoldDB; P21139; -.
DR SMR; P21139; -.
DR BioGRID; 251507; 1.
DR IntAct; P21139; 1.
DR MINT; P21139; -.
DR STRING; 10116.ENSRNOP00000041867; -.
DR BindingDB; P21139; -.
DR ChEMBL; CHEMBL2852; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR jPOST; P21139; -.
DR PaxDb; P21139; -.
DR PRIDE; P21139; -.
DR GeneID; 246136; -.
DR KEGG; rno:246136; -.
DR UCSC; RGD:628787; rat.
DR CTD; 4123; -.
DR RGD; 628787; Man2c1.
DR eggNOG; KOG4342; Eukaryota.
DR InParanoid; P21139; -.
DR OrthoDB; 85892at2759; -.
DR PhylomeDB; P21139; -.
DR Reactome; R-RNO-8853383; Lysosomal oligosaccharide catabolism.
DR SABIO-RK; P21139; -.
DR PRO; PR:P21139; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; NAS:RGD.
DR GO; GO:0004559; F:alpha-mannosidase activity; IDA:RGD.
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 GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 3.20.110.10; -; 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 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; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Cobalt; Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase;
KW Metal-binding; Reference proteome.
FT CHAIN 1..1040
FT /note="Alpha-mannosidase 2C1"
FT /id="PRO_0000206909"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 259
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305"
FT BINDING 261
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305"
FT BINDING 371
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305"
FT BINDING 576
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1040 AA; 115971 MW; 144F6EB97C8F7EA7 CRC64;
MAAAPFLKHW RTTFERVEKF VSPIYFTDCN LRGRLFGDSC PVTLSSFLTP ERLPYEKAVQ
QNFSPAQVGD SFGPTWWTCW FRVELVIPEV WVGKEVHLCW ESDGESLVWR DGEPVQGLTK
EGEKTSYVLS ERLHAADPRS LTLYVEVACN GLLGAGKGSM IAAPDPEKMF QLSQAKLAVF
HRDVHNLLVD LELLLGVAKG LGEDNQRSFQ ALYTANQMVN ICDPAQPETY PAAEALASKF
FGQRGGESQH TIHATGHCHI DTAWLWPFKE TVRKCARSWS TAVKLMERNT EFTFACSQAQ
QLEWVKNQYP GLYAQLQEFA CRGQFVPVGG TWVEMDGNLP SGEAMVRQFL QGQNFFLQEF
GKMCSEFWLP DTFGYSAQLP QIMQGCGIKR FLTQKLSWNL VNSFPHHTFF WEGLDGSQVL
VHFPPGDSYG MQGSVEEVLK TVTNNRDKGR TNHSGFLFGF GDGGGGPTQT MLDRLKRLGN
TDGQPRVQLS SPGQLFTALE RDSGQLCTWV GELFLELHNG TYTTHAQLKK GNRECEQILH
DVELLSSLAL ARSAQFLYPA VQLQRLWRLL LLNQFHDVVT GSCIQLVAED AMNYYEDIRS
HGNTLLSAAA AALCAGEPGP KGLRHYQHTA LEAHRSVGTT QGLVGLTRLA LVTVPSIGYA
PAPTPTSLQP LLPQQPVFVM QETDGSVTLD NGIIRVRLDP TGCLTSLVLV ASGREAIAEG
ALGNQFVLFD DVPLYWDAWD VMDYHLETRK PVRGQAGTLA VGAEGGLRGS AWFLLQISPN
SRLSQEVVLD VGCPYVRFHT EVHWHETHKF LKVEFPARVR SPQATYEIQF GHLQEADPQQ
HSWDWARYEV WAHRWIDLSE CDFGLALLNN CKYGTSVRGN VLSLSLLRAP KAPDVTADMG
RHEFTYALMP HKGSFQEAGV IQAAYNLNFP LLALPAPGPA PDTTWSAFSV SSPAVVLETI
KQAEKSHQHR TLVLRLYEAH GSHVDCWLHT SLPVQEATLC DLLEQRDPTG HLSLQDNRLK
LTFSPFQVRS LLLVLQPPAN
