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   24-JAN-2024, entry version 136.
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}.
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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.ENSRNOP00000070004; -.
DR   BindingDB; P21139; -.
DR   ChEMBL; CHEMBL2852; -.
DR   CAZy; GH38; Glycoside Hydrolase Family 38.
DR   PhosphoSitePlus; P21139; -.
DR   jPOST; P21139; -.
DR   PaxDb; 10116-ENSRNOP00000041867; -.
DR   GeneID; 246136; -.
DR   KEGG; rno:246136; -.
DR   UCSC; RGD:628787; rat.
DR   AGR; RGD:628787; -.
DR   CTD; 4123; -.
DR   RGD; 628787; Man2c1.
DR   eggNOG; KOG4342; Eukaryota.
DR   InParanoid; P21139; -.
DR   OrthoDB; 2786490at2759; -.
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:0005829; C:cytosol; ISO: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; ISO:RGD.
DR   CDD; cd10813; GH38N_AMII_Man2C1; 1.
DR   Gene3D; 2.60.40.2220; -; 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   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; 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   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
//