ID   MA2C1_HUMAN             Reviewed;        1040 AA.
AC   Q9NTJ4; H3BMX2; H3BQY8; H3BUT6; Q13358; Q68EM8; Q9UL64;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Alpha-mannosidase 2C1;
DE            EC=3.2.1.24 {ECO:0000269|PubMed:16848760};
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., Cai Y.-Y.,
RA   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., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   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 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., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   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., 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 (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 project:
RT   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 alpha-
RT   mannosidase.";
RL   Zhonghua Wei Sheng Wu Xue He Mian Yi Xue Za Zhi 17:34-39(1997).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=16848760; DOI=10.1042/bj20060945;
RA   Suzuki T., Hara I., Nakano M., Shigeta M., Nakagawa T., Kondo A.,
RA   Funakoshi Y., Taniguchi N.;
RT   "Man2C1, an alpha-mannosidase, is involved in the trimming of free
RT   oligosaccharides in the cytosol.";
RL   Biochem. J. 400:33-41(2006).
RN   [9]
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   [10]
RP   VARIANTS CDDG2 ARG-203; GLN-768 AND SER-871, INVOLVEMENT IN CDDG2,
RP   CHARACTERIZATION OF VARIANTS CDDG2 ARG-203; GLN-768 AND SER-871, AND
RP   FUNCTION.
RX   PubMed=35045343; DOI=10.1016/j.ajhg.2021.12.010;
RA   Maia N., Potelle S., Yildirim H., Duvet S., Akula S.K., Schulz C.,
RA   Wiame E., Gheldof A., O'Kane K., Lai A., Sermon K., Proisy M., Loget P.,
RA   Attie-Bitach T., Quelin C., Fortuna A.M., Soares A.R., de Brouwer A.P.M.,
RA   Van Schaftingen E., Nassogne M.C., Walsh C.A., Stouffs K., Jorge P.,
RA   Jansen A.C., Foulquier F.;
RT   "Impaired catabolism of free oligosaccharides due to MAN2C1 variants causes
RT   a neurodevelopmental disorder.";
RL   Am. J. Hum. Genet. 109:345-360(2022).
CC   -!- FUNCTION: Cleaves alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose
CC       residues on cytoplasmatic free oligosaccharides generated by N-
CC       glycoprotein degradation pathways. {ECO:0000269|PubMed:16848760}.
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:16848760};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:16848760};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by swainsonine. Also inhibited
CC       to a lesser extent by deoxymannojirimycin (DMM).
CC       {ECO:0000269|PubMed:16848760}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16848760}.
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       Name=3;
CC         IsoId=Q9NTJ4-3; Sequence=VSP_046395;
CC       Name=4;
CC         IsoId=Q9NTJ4-4; Sequence=VSP_046895;
CC   -!- DISEASE: Congenital disorder of deglycosylation 2 (CDDG2) [MIM:619775]:
CC       An autosomal recessive disorder characterized by facial dysmorphism,
CC       congenital anomalies such as tongue hamartoma, variable degrees of
CC       intellectual disability, and brain anomalies including polymicrogyria,
CC       interhemispheric cysts, hypothalamic hamartoma, callosal anomalies, and
CC       hypoplasia of brainstem and cerebellar vermis.
CC       {ECO:0000269|PubMed:35045343}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC00190.2; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAC00568.1; Type=Frameshift; Evidence={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; 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   CCDS; CCDS32298.1; -. [Q9NTJ4-1]
DR   CCDS; CCDS58389.1; -. [Q9NTJ4-3]
DR   CCDS; CCDS58390.1; -. [Q9NTJ4-2]
DR   CCDS; CCDS58391.1; -. [Q9NTJ4-4]
DR   PIR; T46931; T46931.
DR   RefSeq; NP_001243423.1; NM_001256494.1. [Q9NTJ4-4]
DR   RefSeq; NP_001243424.1; NM_001256495.1. [Q9NTJ4-2]
DR   RefSeq; NP_001243425.1; NM_001256496.1. [Q9NTJ4-3]
DR   RefSeq; NP_006706.2; NM_006715.3. [Q9NTJ4-1]
DR   AlphaFoldDB; Q9NTJ4; -.
DR   SMR; Q9NTJ4; -.
DR   BioGRID; 110296; 38.
DR   IntAct; Q9NTJ4; 13.
DR   MINT; Q9NTJ4; -.
DR   STRING; 9606.ENSP00000457788; -.
DR   CAZy; GH38; Glycoside Hydrolase Family 38.
DR   GlyGen; Q9NTJ4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NTJ4; -.
DR   PhosphoSitePlus; Q9NTJ4; -.
DR   BioMuta; MAN2C1; -.
DR   DMDM; 27923805; -.
DR   EPD; Q9NTJ4; -.
DR   jPOST; Q9NTJ4; -.
DR   MassIVE; Q9NTJ4; -.
DR   MaxQB; Q9NTJ4; -.
DR   PaxDb; 9606-ENSP00000457788; -.
DR   PeptideAtlas; Q9NTJ4; -.
DR   ProteomicsDB; 41029; -.
DR   ProteomicsDB; 41922; -.
DR   ProteomicsDB; 43020; -.
DR   ProteomicsDB; 82619; -. [Q9NTJ4-1]
DR   Pumba; Q9NTJ4; -.
DR   Antibodypedia; 27278; 126 antibodies from 20 providers.
DR   DNASU; 4123; -.
DR   Ensembl; ENST00000267978.10; ENSP00000267978.4; ENSG00000140400.18. [Q9NTJ4-1]
DR   Ensembl; ENST00000563622.5; ENSP00000454589.1; ENSG00000140400.18. [Q9NTJ4-3]
DR   Ensembl; ENST00000565683.5; ENSP00000457788.1; ENSG00000140400.18. [Q9NTJ4-4]
DR   Ensembl; ENST00000569482.5; ENSP00000455998.1; ENSG00000140400.18. [Q9NTJ4-2]
DR   GeneID; 4123; -.
DR   KEGG; hsa:4123; -.
DR   MANE-Select; ENST00000267978.10; ENSP00000267978.4; NM_006715.4; NP_006706.2.
DR   UCSC; uc002baf.5; human. [Q9NTJ4-1]
DR   AGR; HGNC:6827; -.
DR   CTD; 4123; -.
DR   DisGeNET; 4123; -.
DR   GeneCards; MAN2C1; -.
DR   HGNC; HGNC:6827; MAN2C1.
DR   HPA; ENSG00000140400; Low tissue specificity.
DR   MalaCards; MAN2C1; -.
DR   MIM; 154580; gene.
DR   MIM; 619775; phenotype.
DR   neXtProt; NX_Q9NTJ4; -.
DR   OpenTargets; ENSG00000140400; -.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   PharmGKB; PA30576; -.
DR   VEuPathDB; HostDB:ENSG00000140400; -.
DR   eggNOG; KOG4342; Eukaryota.
DR   GeneTree; ENSGT01030000234638; -.
DR   HOGENOM; CLU_003442_0_1_1; -.
DR   InParanoid; Q9NTJ4; -.
DR   OMA; GQYWDAW; -.
DR   OrthoDB; 2786490at2759; -.
DR   PhylomeDB; Q9NTJ4; -.
DR   TreeFam; TF300335; -.
DR   BRENDA; 3.2.1.24; 2681.
DR   PathwayCommons; Q9NTJ4; -.
DR   Reactome; R-HSA-8853383; Lysosomal oligosaccharide catabolism.
DR   SignaLink; Q9NTJ4; -.
DR   BioGRID-ORCS; 4123; 15 hits in 1160 CRISPR screens.
DR   ChiTaRS; MAN2C1; human.
DR   GenomeRNAi; 4123; -.
DR   Pharos; Q9NTJ4; Tbio.
DR   PRO; PR:Q9NTJ4; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9NTJ4; Protein.
DR   Bgee; ENSG00000140400; Expressed in right lobe of thyroid gland and 149 other cell types or tissues.
DR   ExpressionAtlas; Q9NTJ4; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
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   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.
DR   Genevisible; Q9NTJ4; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cobalt; Cytoplasm; Glycosidase; Hydrolase;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..1040
FT                   /note="Alpha-mannosidase 2C1"
FT                   /id="PRO_0000206907"
FT   ACT_SITE        372
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q29451"
FT   BINDING         260
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000305"
FT   BINDING         262
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000305"
FT   BINDING         372
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000305"
FT   BINDING         577
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         201..299
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_046395"
FT   VAR_SEQ         650..682
FT                   /note="ALVTVPSMGYAPVPPPTSLQPLLPQQPVFVVQE -> GLTPSPGDSAQHGLC
FT                   SCSSPHLTAAPAAPAACVRSARAPTDSASRPPPTK (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046895"
FT   VAR_SEQ         913..935
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046375"
FT   VARIANT         203
FT                   /note="G -> R (in CDDG2; uncertain significance; results in
FT                   defective processing of free oligosaccharides as shown by
FT                   complementation assay in MAN2C1-deficient cells;
FT                   dbSNP:rs190692217)"
FT                   /evidence="ECO:0000269|PubMed:35045343"
FT                   /id="VAR_087012"
FT   VARIANT         323
FT                   /note="R -> C (in dbSNP:rs200595616)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_069180"
FT   VARIANT         768
FT                   /note="R -> Q (in CDDG2; uncertain significance; severely
FT                   decreased mannosidase activity; results in defective
FT                   processing of free oligosaccharides as shown by
FT                   complementation assay in MAN2C1-deficient cells;
FT                   dbSNP:rs62029711)"
FT                   /evidence="ECO:0000269|PubMed:35045343"
FT                   /id="VAR_087013"
FT   VARIANT         818
FT                   /note="R -> H (in dbSNP:rs58557444)"
FT                   /id="VAR_061192"
FT   VARIANT         871
FT                   /note="C -> S (in CDDG2; uncertain significance; has no
FT                   effect on processing of free oligosaccharides as shown by
FT                   complementation assay in MAN2C1-deficient cells;
FT                   dbSNP:rs143755898)"
FT                   /evidence="ECO:0000269|PubMed:35045343"
FT                   /id="VAR_087014"
FT   VARIANT         950
FT                   /note="V -> M (in dbSNP:rs3803467)"
FT                   /id="VAR_049211"
FT   VARIANT         960
FT                   /note="V -> I (in dbSNP:rs3803466)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_021914"
FT   VARIANT         975
FT                   /note="R -> K (in dbSNP:rs5745934)"
FT                   /id="VAR_049212"
FT   CONFLICT        6
FT                   /note="A -> F (in Ref. 1; AAC00190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="L -> F (in Ref. 1; AAC00190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="L -> I (in Ref. 1; AAC00190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="M -> I (in Ref. 1; AAC00190)"
FT                   /evidence="ECO:0000305"
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
//