Full text data of MAN2C1
MAN2C1
(MANA, MANA1)
[Confidence: low (only semi-automatic identification from reviews)]
Alpha-mannosidase 2C1; 3.2.1.24 (Alpha mannosidase 6A8B; Alpha-D-mannoside mannohydrolase; Mannosidase alpha class 2C member 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Alpha-mannosidase 2C1; 3.2.1.24 (Alpha mannosidase 6A8B; Alpha-D-mannoside mannohydrolase; Mannosidase alpha class 2C member 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NTJ4
ID MA2C1_HUMAN Reviewed; 1040 AA.
AC Q9NTJ4; H3BMX2; H3BQY8; H3BUT6; Q13358; Q68EM8; Q9UL64;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Alpha-mannosidase 2C1;
DE EC=3.2.1.24;
DE AltName: Full=Alpha mannosidase 6A8B;
DE AltName: Full=Alpha-D-mannoside mannohydrolase;
DE AltName: Full=Mannosidase alpha class 2C member 1;
GN Name=MAN2C1; Synonyms=MANA, MANA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Li B., Ma F.-R., Shi G.-X., Zhao F.-T., Li J., Li L., Wang Y.,
RA Cai Y.-Y., Zhu L.-P.;
RT "Cloning of a human full-length cDNA encoding an alpha-mannosidase.";
RL Ji Chu Yi Xue Yu Lin Chuang 19:409-415(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP ILE-960.
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP CYS-323.
RC TISSUE=Skin, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 630-1040 (ISOFORM 1).
RC TISSUE=Tonsil;
RA Zhang L.-X., Zhu L.-P., Shi W., Ma F.-R.;
RT "Cloning of a human cDNA homologous to the cDNA encoding a rat ER
RT alpha-mannosidase.";
RL Zhonghua Wei Sheng Wu Xue He Mian Yi Xue Za Zhi 17:34-39(1997).
RN [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing alpha-D-
CC mannose residues in alpha-D-mannosides.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NTJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTJ4-2; Sequence=VSP_046375;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9NTJ4-3; Sequence=VSP_046395;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NTJ4-4; Sequence=VSP_046895;
CC Note=Gene prediction based on EST data;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00190.2; Type=Frameshift; Positions=1013;
CC Sequence=AAC00568.1; Type=Frameshift; Positions=1013;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF044414; AAC00190.2; ALT_FRAME; mRNA.
DR EMBL; AL136876; CAB66810.1; -; mRNA.
DR EMBL; AK225145; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC068338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99253.1; -; Genomic_DNA.
DR EMBL; BC050550; AAH50550.1; -; mRNA.
DR EMBL; BC080191; AAH80191.1; -; mRNA.
DR EMBL; U37248; AAC00568.1; ALT_SEQ; mRNA.
DR PIR; T46931; T46931.
DR RefSeq; NP_001243423.1; NM_001256494.1.
DR RefSeq; NP_001243424.1; NM_001256495.1.
DR RefSeq; NP_001243425.1; NM_001256496.1.
DR RefSeq; NP_006706.2; NM_006715.3.
DR UniGene; Hs.26232; -.
DR UniGene; Hs.598731; -.
DR ProteinModelPortal; Q9NTJ4; -.
DR IntAct; Q9NTJ4; 1.
DR MINT; MINT-1035933; -.
DR STRING; 9606.ENSP00000267978; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PhosphoSite; Q9NTJ4; -.
DR DMDM; 27923805; -.
DR PaxDb; Q9NTJ4; -.
DR PRIDE; Q9NTJ4; -.
DR Ensembl; ENST00000267978; ENSP00000267978; ENSG00000140400.
DR Ensembl; ENST00000563622; ENSP00000454589; ENSG00000140400.
DR Ensembl; ENST00000565683; ENSP00000457788; ENSG00000140400.
DR Ensembl; ENST00000569482; ENSP00000455998; ENSG00000140400.
DR GeneID; 4123; -.
DR KEGG; hsa:4123; -.
DR UCSC; uc010bkk.4; human.
DR CTD; 4123; -.
DR GeneCards; GC15M075648; -.
DR HGNC; HGNC:6827; MAN2C1.
DR HPA; HPA040627; -.
DR MIM; 154580; gene.
DR neXtProt; NX_Q9NTJ4; -.
DR PharmGKB; PA30576; -.
DR eggNOG; COG0383; -.
DR HOGENOM; HOG000048425; -.
DR HOVERGEN; HBG055567; -.
DR InParanoid; Q9NTJ4; -.
DR KO; K01191; -.
DR OMA; CHYEDIR; -.
DR OrthoDB; EOG78M015; -.
DR ChiTaRS; MAN2C1; human.
DR GenomeRNAi; 4123; -.
DR NextBio; 16188; -.
DR PRO; PR:Q9NTJ4; -.
DR ArrayExpress; Q9NTJ4; -.
DR Bgee; Q9NTJ4; -.
DR CleanEx; HS_MAN2C1; -.
DR Genevestigator; Q9NTJ4; -.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR027291; Glyco_hydro_38/57_N.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen_dom.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF01074; Glyco_hydro_38; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Glycosidase; Hydrolase;
KW Metal-binding; Polymorphism; Reference proteome; Zinc.
FT CHAIN 1 1040 Alpha-mannosidase 2C1.
FT /FTId=PRO_0000206907.
FT ACT_SITE 372 372 Nucleophile (By similarity).
FT METAL 260 260 Zinc (By similarity).
FT METAL 262 262 Zinc (By similarity).
FT METAL 372 372 Zinc (By similarity).
FT METAL 577 577 Zinc (By similarity).
FT VAR_SEQ 201 299 Missing (in isoform 3).
FT /FTId=VSP_046395.
FT VAR_SEQ 650 682 ALVTVPSMGYAPVPPPTSLQPLLPQQPVFVVQE -> GLTP
FT SPGDSAQHGLCSCSSPHLTAAPAAPAACVRSARAPTDSASR
FT PPPTK (in isoform 4).
FT /FTId=VSP_046895.
FT VAR_SEQ 913 935 Missing (in isoform 2).
FT /FTId=VSP_046375.
FT VARIANT 323 323 R -> C (in dbSNP:rs200595616).
FT /FTId=VAR_069180.
FT VARIANT 818 818 R -> H (in dbSNP:rs58557444).
FT /FTId=VAR_061192.
FT VARIANT 950 950 V -> M (in dbSNP:rs3803467).
FT /FTId=VAR_049211.
FT VARIANT 960 960 V -> I (in dbSNP:rs3803466).
FT /FTId=VAR_021914.
FT VARIANT 975 975 R -> K (in dbSNP:rs5745934).
FT /FTId=VAR_049212.
FT CONFLICT 6 6 A -> F (in Ref. 1; AAC00190).
FT CONFLICT 14 14 L -> F (in Ref. 1; AAC00190).
FT CONFLICT 24 24 L -> I (in Ref. 1; AAC00190).
FT CONFLICT 170 170 M -> I (in Ref. 1; AAC00190).
SQ SEQUENCE 1040 AA; 115835 MW; 2B40AE6E03AC1E3C CRC64;
MAAAPALKHW RTTLERVEKF VSPLYFTDCN LRGRLFGASC PVAVLSSFLT PERLPYQEAV
QRDFRPAQVG DSFGPTWWTC WFRVELTIPE AWVGQEVHLC WESDGEGLVW RDGEPVQGLT
KEGEKTSYVL TDRLGERDPR SLTLYVEVAC NGLLGAGKGS MIAAPDPEKM FQLSRAELAV
FHRDVHMLLV DLELLLGIAK GLGKDNQRSF QALYTANQMV NVCDPAQPET FPVAQALASR
FFGQHGGESQ HTIHATGHCH IDTAWLWPFK ETVRKCARSW VTALQLMERN PEFIFACSQA
QQLEWVKSRY PGLYSRIQEF ACRGQFVPVG GTWVEMDGNL PSGEAMVRQF LQGQNFFLQE
FGKMCSEFWL PDTFGYSAQL PQIMHGCGIR RFLTQKLSWN LVNSFPHHTF FWEGLDGSRV
LVHFPPGDSY GMQGSVEEVL KTVANNRDKG RANHSAFLFG FGDGGGGPTQ TMLDRLKRLS
NTDGLPRVQL SSPRQLFSAL ESDSEQLCTW VGELFLELHN GTYTTHAQIK KGNRECERIL
HDVELLSSLA LARSAQFLYP AAQLQHLWRL LLLNQFHDVV TGSCIQMVAE EAMCHYEDIR
SHGNTLLSAA AAALCAGEPG PEGLLIVNTL PWKRIEVMAL PKPGGAHSLA LVTVPSMGYA
PVPPPTSLQP LLPQQPVFVV QETDGSVTLD NGIIRVKLDP TGRLTSLVLV ASGREAIAEG
AVGNQFVLFD DVPLYWDAWD VMDYHLETRK PVLGQAGTLA VGTEGGLRGS AWFLLQISPN
SRLSQEVVLD VGCPYVRFHT EVHWHEAHKF LKVEFPARVR SSQATYEIQF GHLQRPTHYN
TSWDWARFEV WAHRWMDLSE HGFGLALLND CKYGASVRGS ILSLSLLRAP KAPDATADTG
RHEFTYALMP HKGSFQDAGV IQAAYSLNFP LLALPAPSPA PATSWSAFSV SSPAVVLETV
KQAESSPQRR SLVLRLYEAH GSHVDCWLHL SLPVQEAILC DLLERPDPAG HLTLRDNRLK
LTFSPFQVLS LLLVLQPPPH
//
ID MA2C1_HUMAN Reviewed; 1040 AA.
AC Q9NTJ4; H3BMX2; H3BQY8; H3BUT6; Q13358; Q68EM8; Q9UL64;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Alpha-mannosidase 2C1;
DE EC=3.2.1.24;
DE AltName: Full=Alpha mannosidase 6A8B;
DE AltName: Full=Alpha-D-mannoside mannohydrolase;
DE AltName: Full=Mannosidase alpha class 2C member 1;
GN Name=MAN2C1; Synonyms=MANA, MANA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Li B., Ma F.-R., Shi G.-X., Zhao F.-T., Li J., Li L., Wang Y.,
RA Cai Y.-Y., Zhu L.-P.;
RT "Cloning of a human full-length cDNA encoding an alpha-mannosidase.";
RL Ji Chu Yi Xue Yu Lin Chuang 19:409-415(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP ILE-960.
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP CYS-323.
RC TISSUE=Skin, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 630-1040 (ISOFORM 1).
RC TISSUE=Tonsil;
RA Zhang L.-X., Zhu L.-P., Shi W., Ma F.-R.;
RT "Cloning of a human cDNA homologous to the cDNA encoding a rat ER
RT alpha-mannosidase.";
RL Zhonghua Wei Sheng Wu Xue He Mian Yi Xue Za Zhi 17:34-39(1997).
RN [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing alpha-D-
CC mannose residues in alpha-D-mannosides.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NTJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTJ4-2; Sequence=VSP_046375;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9NTJ4-3; Sequence=VSP_046395;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NTJ4-4; Sequence=VSP_046895;
CC Note=Gene prediction based on EST data;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00190.2; Type=Frameshift; Positions=1013;
CC Sequence=AAC00568.1; Type=Frameshift; Positions=1013;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF044414; AAC00190.2; ALT_FRAME; mRNA.
DR EMBL; AL136876; CAB66810.1; -; mRNA.
DR EMBL; AK225145; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC068338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99253.1; -; Genomic_DNA.
DR EMBL; BC050550; AAH50550.1; -; mRNA.
DR EMBL; BC080191; AAH80191.1; -; mRNA.
DR EMBL; U37248; AAC00568.1; ALT_SEQ; mRNA.
DR PIR; T46931; T46931.
DR RefSeq; NP_001243423.1; NM_001256494.1.
DR RefSeq; NP_001243424.1; NM_001256495.1.
DR RefSeq; NP_001243425.1; NM_001256496.1.
DR RefSeq; NP_006706.2; NM_006715.3.
DR UniGene; Hs.26232; -.
DR UniGene; Hs.598731; -.
DR ProteinModelPortal; Q9NTJ4; -.
DR IntAct; Q9NTJ4; 1.
DR MINT; MINT-1035933; -.
DR STRING; 9606.ENSP00000267978; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PhosphoSite; Q9NTJ4; -.
DR DMDM; 27923805; -.
DR PaxDb; Q9NTJ4; -.
DR PRIDE; Q9NTJ4; -.
DR Ensembl; ENST00000267978; ENSP00000267978; ENSG00000140400.
DR Ensembl; ENST00000563622; ENSP00000454589; ENSG00000140400.
DR Ensembl; ENST00000565683; ENSP00000457788; ENSG00000140400.
DR Ensembl; ENST00000569482; ENSP00000455998; ENSG00000140400.
DR GeneID; 4123; -.
DR KEGG; hsa:4123; -.
DR UCSC; uc010bkk.4; human.
DR CTD; 4123; -.
DR GeneCards; GC15M075648; -.
DR HGNC; HGNC:6827; MAN2C1.
DR HPA; HPA040627; -.
DR MIM; 154580; gene.
DR neXtProt; NX_Q9NTJ4; -.
DR PharmGKB; PA30576; -.
DR eggNOG; COG0383; -.
DR HOGENOM; HOG000048425; -.
DR HOVERGEN; HBG055567; -.
DR InParanoid; Q9NTJ4; -.
DR KO; K01191; -.
DR OMA; CHYEDIR; -.
DR OrthoDB; EOG78M015; -.
DR ChiTaRS; MAN2C1; human.
DR GenomeRNAi; 4123; -.
DR NextBio; 16188; -.
DR PRO; PR:Q9NTJ4; -.
DR ArrayExpress; Q9NTJ4; -.
DR Bgee; Q9NTJ4; -.
DR CleanEx; HS_MAN2C1; -.
DR Genevestigator; Q9NTJ4; -.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR027291; Glyco_hydro_38/57_N.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen_dom.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF01074; Glyco_hydro_38; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Glycosidase; Hydrolase;
KW Metal-binding; Polymorphism; Reference proteome; Zinc.
FT CHAIN 1 1040 Alpha-mannosidase 2C1.
FT /FTId=PRO_0000206907.
FT ACT_SITE 372 372 Nucleophile (By similarity).
FT METAL 260 260 Zinc (By similarity).
FT METAL 262 262 Zinc (By similarity).
FT METAL 372 372 Zinc (By similarity).
FT METAL 577 577 Zinc (By similarity).
FT VAR_SEQ 201 299 Missing (in isoform 3).
FT /FTId=VSP_046395.
FT VAR_SEQ 650 682 ALVTVPSMGYAPVPPPTSLQPLLPQQPVFVVQE -> GLTP
FT SPGDSAQHGLCSCSSPHLTAAPAAPAACVRSARAPTDSASR
FT PPPTK (in isoform 4).
FT /FTId=VSP_046895.
FT VAR_SEQ 913 935 Missing (in isoform 2).
FT /FTId=VSP_046375.
FT VARIANT 323 323 R -> C (in dbSNP:rs200595616).
FT /FTId=VAR_069180.
FT VARIANT 818 818 R -> H (in dbSNP:rs58557444).
FT /FTId=VAR_061192.
FT VARIANT 950 950 V -> M (in dbSNP:rs3803467).
FT /FTId=VAR_049211.
FT VARIANT 960 960 V -> I (in dbSNP:rs3803466).
FT /FTId=VAR_021914.
FT VARIANT 975 975 R -> K (in dbSNP:rs5745934).
FT /FTId=VAR_049212.
FT CONFLICT 6 6 A -> F (in Ref. 1; AAC00190).
FT CONFLICT 14 14 L -> F (in Ref. 1; AAC00190).
FT CONFLICT 24 24 L -> I (in Ref. 1; AAC00190).
FT CONFLICT 170 170 M -> I (in Ref. 1; AAC00190).
SQ SEQUENCE 1040 AA; 115835 MW; 2B40AE6E03AC1E3C CRC64;
MAAAPALKHW RTTLERVEKF VSPLYFTDCN LRGRLFGASC PVAVLSSFLT PERLPYQEAV
QRDFRPAQVG DSFGPTWWTC WFRVELTIPE AWVGQEVHLC WESDGEGLVW RDGEPVQGLT
KEGEKTSYVL TDRLGERDPR SLTLYVEVAC NGLLGAGKGS MIAAPDPEKM FQLSRAELAV
FHRDVHMLLV DLELLLGIAK GLGKDNQRSF QALYTANQMV NVCDPAQPET FPVAQALASR
FFGQHGGESQ HTIHATGHCH IDTAWLWPFK ETVRKCARSW VTALQLMERN PEFIFACSQA
QQLEWVKSRY PGLYSRIQEF ACRGQFVPVG GTWVEMDGNL PSGEAMVRQF LQGQNFFLQE
FGKMCSEFWL PDTFGYSAQL PQIMHGCGIR RFLTQKLSWN LVNSFPHHTF FWEGLDGSRV
LVHFPPGDSY GMQGSVEEVL KTVANNRDKG RANHSAFLFG FGDGGGGPTQ TMLDRLKRLS
NTDGLPRVQL SSPRQLFSAL ESDSEQLCTW VGELFLELHN GTYTTHAQIK KGNRECERIL
HDVELLSSLA LARSAQFLYP AAQLQHLWRL LLLNQFHDVV TGSCIQMVAE EAMCHYEDIR
SHGNTLLSAA AAALCAGEPG PEGLLIVNTL PWKRIEVMAL PKPGGAHSLA LVTVPSMGYA
PVPPPTSLQP LLPQQPVFVV QETDGSVTLD NGIIRVKLDP TGRLTSLVLV ASGREAIAEG
AVGNQFVLFD DVPLYWDAWD VMDYHLETRK PVLGQAGTLA VGTEGGLRGS AWFLLQISPN
SRLSQEVVLD VGCPYVRFHT EVHWHEAHKF LKVEFPARVR SSQATYEIQF GHLQRPTHYN
TSWDWARFEV WAHRWMDLSE HGFGLALLND CKYGASVRGS ILSLSLLRAP KAPDATADTG
RHEFTYALMP HKGSFQDAGV IQAAYSLNFP LLALPAPSPA PATSWSAFSV SSPAVVLETV
KQAESSPQRR SLVLRLYEAH GSHVDCWLHL SLPVQEAILC DLLERPDPAG HLTLRDNRLK
LTFSPFQVLS LLLVLQPPPH
//
MIM
154580
*RECORD*
*FIELD* NO
154580
*FIELD* TI
*154580 MANNOSIDASE, ALPHA, CLASS 2C, MEMBER 1; MAN2C1
;;MANNOSIDASE, ALPHA A, CYTOPLASMIC; MANA
read more*FIELD* TX
Cytoplasmic alpha-mannosidase (MANA) was assigned to 15q11-qter by study
of an X;15 translocation in man-mouse hybrids (Champion et al., 1978).
Lysosomal alpha-mannosidase (MANB) has been assigned to chromosome 19 by
somatic cell hybridization (see 609458). Neri et al. (1983) described a
boy with a ring chromosome 15 derived from a t(15q;15q) chromosome of
the mother. The ring chromosome was duplicated for a portion of the long
arms near the centromere, probably cen-q13. Dosage effects suggested
that the alpha-mannosidase gene is located in this segment. Since a
shortest region of overlap (SRO) of 15q11-qter had been estimated by
Ferguson-Smith and Westerveld (1979), the new information places the
MAN2C1 gene in the 15q11-q13 segment.
*FIELD* RF
1. Champion, M. J.; Brown, J. A.; Shows, T. B.: Assignment of cytoplasmic
alpha-mannosidase (MAN-A) and confirmation of the mitochondrial isocitrate
dehydrogenase (IDH-M) genes to the q11--qter region of chromosome
15 in man. Cytogenet. Cell Genet. 22: 498-502, 1978.
2. Ferguson-Smith, M. A.; Westerveld, A.: Report of the committee
on the genetic constitution of chromosomes 13, 14, 15, 16, 17, 18,
19, 20, 21, and 22 (HGM5). Cytogenet. Cell Genet. 25: 59-73, 1979.
3. Neri, G.; Ricci, R.; Pelino, A.; Bova, R.; Tedeschi, B.; Serra,
A.: A boy with ring chromosome 15 derived from a t(15q;15q) Robertsonian
translocation in the mother: cytogenetic and biochemical findings. Am.
J. Med. Genet. 14: 307-314, 1983.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 07/27/2005
carol: 9/20/1999
carol: 1/13/1993
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 6/2/1986
*RECORD*
*FIELD* NO
154580
*FIELD* TI
*154580 MANNOSIDASE, ALPHA, CLASS 2C, MEMBER 1; MAN2C1
;;MANNOSIDASE, ALPHA A, CYTOPLASMIC; MANA
read more*FIELD* TX
Cytoplasmic alpha-mannosidase (MANA) was assigned to 15q11-qter by study
of an X;15 translocation in man-mouse hybrids (Champion et al., 1978).
Lysosomal alpha-mannosidase (MANB) has been assigned to chromosome 19 by
somatic cell hybridization (see 609458). Neri et al. (1983) described a
boy with a ring chromosome 15 derived from a t(15q;15q) chromosome of
the mother. The ring chromosome was duplicated for a portion of the long
arms near the centromere, probably cen-q13. Dosage effects suggested
that the alpha-mannosidase gene is located in this segment. Since a
shortest region of overlap (SRO) of 15q11-qter had been estimated by
Ferguson-Smith and Westerveld (1979), the new information places the
MAN2C1 gene in the 15q11-q13 segment.
*FIELD* RF
1. Champion, M. J.; Brown, J. A.; Shows, T. B.: Assignment of cytoplasmic
alpha-mannosidase (MAN-A) and confirmation of the mitochondrial isocitrate
dehydrogenase (IDH-M) genes to the q11--qter region of chromosome
15 in man. Cytogenet. Cell Genet. 22: 498-502, 1978.
2. Ferguson-Smith, M. A.; Westerveld, A.: Report of the committee
on the genetic constitution of chromosomes 13, 14, 15, 16, 17, 18,
19, 20, 21, and 22 (HGM5). Cytogenet. Cell Genet. 25: 59-73, 1979.
3. Neri, G.; Ricci, R.; Pelino, A.; Bova, R.; Tedeschi, B.; Serra,
A.: A boy with ring chromosome 15 derived from a t(15q;15q) Robertsonian
translocation in the mother: cytogenetic and biochemical findings. Am.
J. Med. Genet. 14: 307-314, 1983.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 07/27/2005
carol: 9/20/1999
carol: 1/13/1993
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 6/2/1986