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MA1A1_HUMAN
ID   MA1A1_HUMAN             Reviewed;         653 AA.
AC   P33908; E7EU32; Q6P052; Q9NU44; Q9UJI3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 3.
DT   03-AUG-2022, entry version 191.
DE   RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA;
DE            EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE   AltName: Full=Man(9)-alpha-mannosidase;
DE            Short=Man9-mannosidase;
DE   AltName: Full=Mannosidase alpha class 1A member 1;
DE   AltName: Full=Processing alpha-1,2-mannosidase IA;
DE            Short=Alpha-1,2-mannosidase IA;
GN   Name=MAN1A1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-653 (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=8223597; DOI=10.1111/j.1432-1033.1993.tb18274.x;
RA   Bause E., Bieberich E., Rolfs A., Voelker C., Schmidt B.;
RT   "Molecular cloning and primary structure of Man9-mannosidase from human
RT   kidney.";
RL   Eur. J. Biochem. 217:535-540(1993).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Involved in the maturation of Asn-linked oligosaccharides.
CC       Progressively trim alpha-1,2-linked mannose residues from
CC       Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-
CC         glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-
CC         (alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-
CC         Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-
CC         asparaginyl-[protein] (N-glucan mannose isomer 5A1,2);
CC         Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087,
CC         ChEBI:CHEBI:139493; EC=3.2.1.113;
CC         Evidence={ECO:0000250|UniProtKB:P32906};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC         (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC         8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC         (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]
CC         (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-
CC         COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628;
CC         EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P45700};
CC   -!- ACTIVITY REGULATION: Inhibited by both 1-deoxymannojirimycin and
CC       kifunensine.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P32906}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P33908-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P33908-2; Sequence=VSP_056372, VSP_056373, VSP_056374;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR   EMBL; AL022722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL078600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL138886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48185.1; -; Genomic_DNA.
DR   EMBL; BC065827; AAH65827.1; -; mRNA.
DR   EMBL; X74837; CAA52831.1; -; mRNA.
DR   CCDS; CCDS5122.1; -. [P33908-1]
DR   PIR; S38965; S38965.
DR   RefSeq; NP_005898.2; NM_005907.3. [P33908-1]
DR   AlphaFoldDB; P33908; -.
DR   SMR; P33908; -.
DR   BioGRID; 110294; 111.
DR   IntAct; P33908; 15.
DR   MINT; P33908; -.
DR   STRING; 9606.ENSP00000357453; -.
DR   ChEMBL; CHEMBL5915; -.
DR   CAZy; GH47; Glycoside Hydrolase Family 47.
DR   GlyGen; P33908; 1 site.
DR   iPTMnet; P33908; -.
DR   PhosphoSitePlus; P33908; -.
DR   BioMuta; MAN1A1; -.
DR   DMDM; 62906886; -.
DR   EPD; P33908; -.
DR   jPOST; P33908; -.
DR   MassIVE; P33908; -.
DR   MaxQB; P33908; -.
DR   PaxDb; P33908; -.
DR   PeptideAtlas; P33908; -.
DR   PRIDE; P33908; -.
DR   ProteomicsDB; 54929; -. [P33908-1]
DR   ProteomicsDB; 66803; -.
DR   TopDownProteomics; P33908-1; -. [P33908-1]
DR   Antibodypedia; 32605; 80 antibodies from 18 providers.
DR   DNASU; 4121; -.
DR   Ensembl; ENST00000368468.4; ENSP00000357453.3; ENSG00000111885.7. [P33908-1]
DR   GeneID; 4121; -.
DR   KEGG; hsa:4121; -.
DR   MANE-Select; ENST00000368468.4; ENSP00000357453.3; NM_005907.4; NP_005898.2.
DR   UCSC; uc003pym.3; human. [P33908-1]
DR   CTD; 4121; -.
DR   DisGeNET; 4121; -.
DR   GeneCards; MAN1A1; -.
DR   HGNC; HGNC:6821; MAN1A1.
DR   HPA; ENSG00000111885; Tissue enhanced (liver).
DR   MIM; 604344; gene.
DR   neXtProt; NX_P33908; -.
DR   OpenTargets; ENSG00000111885; -.
DR   PharmGKB; PA30570; -.
DR   VEuPathDB; HostDB:ENSG00000111885; -.
DR   eggNOG; KOG2204; Eukaryota.
DR   GeneTree; ENSGT00940000158188; -.
DR   HOGENOM; CLU_003818_3_2_1; -.
DR   InParanoid; P33908; -.
DR   OMA; MEMKHEF; -.
DR   OrthoDB; 693882at2759; -.
DR   PhylomeDB; P33908; -.
DR   TreeFam; TF313420; -.
DR   BioCyc; MetaCyc:HS03480-MON; -.
DR   BRENDA; 3.2.1.113; 2681.
DR   PathwayCommons; P33908; -.
DR   Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR   Reactome; R-HSA-964827; Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
DR   SignaLink; P33908; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 4121; 9 hits in 1079 CRISPR screens.
DR   ChiTaRS; MAN1A1; human.
DR   GeneWiki; MAN1A1; -.
DR   GenomeRNAi; 4121; -.
DR   Pharos; P33908; Tbio.
DR   PRO; PR:P33908; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P33908; protein.
DR   Bgee; ENSG00000111885; Expressed in synovial joint and 207 other tissues.
DR   Genevisible; P33908; HS.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR   GO; GO:0015923; F:mannosidase activity; TAS:ProtInc.
DR   GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IMP:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1904381; P:Golgi apparatus mannose trimming; TAS:Reactome.
DR   GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; IDA:UniProtKB.
DR   GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045047; P:protein targeting to ER; IMP:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001382; Glyco_hydro_47.
DR   InterPro; IPR036026; Seven-hairpin_glycosidases.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
DR   PRINTS; PR00747; GLYHDRLASE47.
DR   SUPFAM; SSF48225; SSF48225; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Glycosidase;
KW   Golgi apparatus; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..653
FT                   /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA"
FT                   /id="PRO_0000210308"
FT   TOPO_DOM        1..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..653
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          81..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        522
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P31723"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        476..508
FT                   /evidence="ECO:0000250|UniProtKB:P32906"
FT   VAR_SEQ         201
FT                   /note="E -> EEIEARKGQANCPGSSSSCEVEIQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056372"
FT   VAR_SEQ         331..344
FT                   /note="SGIGRNWPWASGGS -> RWMCNIPRAMEATI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056373"
FT   VAR_SEQ         345..653
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056374"
FT   VARIANT         651
FT                   /note="R -> G (in dbSNP:rs35544784)"
FT                   /id="VAR_034102"
FT   CONFLICT        29..47
FT                   /note="KGSGPAALRLTEKFVLLLV -> MNSNFITFDLKMSLLPSNL (in Ref.
FT                   4; CAA52831)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="G -> R (in Ref. 4; CAA52831)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   653 AA;  72969 MW;  9B164926636D8554 CRC64;
     MPVGGLLPLF SSPAGGVLGG GLGGGGGRKG SGPAALRLTE KFVLLLVFSA FITLCFGAIF
     FLPDSSKLLS GVLFHSSPAL QPAADHKPGP GARAEDAAEG RARRREEGAP GDPEAALEDN
     LARIRENHER ALREAKETLQ KLPEEIQRDI LLEKKKVAQD QLRDKAPFRG LPPVDFVPPI
     GVESREPADA AIREKRAKIK EMMKHAWNNY KGYAWGLNEL KPISKGGHSS SLFGNIKGAT
     IVDALDTLFI MEMKHEFEEA KSWVEENLDF NVNAEISVFE VNIRFVGGLL SAYYLSGEEI
     FRKKAVELGV KLLPAFHTPS GIPWALLNMK SGIGRNWPWA SGGSSILAEF GTLHLEFMHL
     SHLSGNPIFA EKVMNIRTVL NKLEKPQGLY PNYLNPSSGQ WGQHHVSVGG LGDSFYEYLL
     KAWLMSDKTD LEAKKMYFDA VQAIETHLIR KSSSGLTYIA EWKGGLLEHK MGHLTCFAGG
     MFALGADAAP EGMAQHYLEL GAEIARTCHE SYNRTFMKLG PEAFRFDGGV EAIATRQNEK
     YYILRPEVME TYMYMWRLTH DPKYRKWAWE AVEALENHCR VNGGYSGLRD VYLLHESYDD
     VQQSFFLAET LKYLYLIFSD DDLLPLEHWI FNSEAHLLPI LPKDKKEVEI REE
 
 
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