MANEA_HUMAN
ID MANEA_HUMAN Reviewed; 462 AA.
AC Q5SRI9; A6H8M6; Q5SRJ0; Q6MZV0; Q70JE9; Q7Z3V7; Q8WWX5; Q9H9D2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glycoprotein endo-alpha-1,2-mannosidase;
DE Short=Endo-alpha mannosidase;
DE Short=Endomannosidase;
DE Short=hEndo;
DE EC=3.2.1.130 {ECO:0000269|PubMed:15677381, ECO:0000269|PubMed:15760709};
DE AltName: Full=Mandaselin;
GN Name=MANEA;
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], SUBCELLULAR LOCATION, TOPOLOGY, AND CATALYTIC
RP ACTIVITY.
RX PubMed=15760709; DOI=10.1016/j.biochi.2004.11.004;
RA Hardt B., Voelker C., Mundt S., Salska-Navarro M., Hauptmann M., Bause E.;
RT "Human endo-alpha1,2-mannosidase is a Golgi-resident type II membrane
RT protein.";
RL Biochimie 87:169-179(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, PTM, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC TISSUE=Liver;
RX PubMed=15677381; DOI=10.1093/glycob/cwi045;
RA Hamilton S.R., Li H., Wischnewski H., Prasad A., Kerley-Hamilton J.S.,
RA Mitchell T., Walling A.J., Davidson R.C., Wildt S., Gerngross T.U.;
RT "Intact alpha-1,2-endomannosidase is a typical type II membrane protein.";
RL Glycobiology 15:615-624(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [LARGE SCALE MRNA] OF 1-214.
RC TISSUE=Liver;
RA Zeng L., Liu F., Xu X., Zhang X., Chen Z., Han Z.;
RT "Novel gene expressed in human liver.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-331.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-{alpha-Glc-(1->3)-alpha-Man-(1->2)-alpha-Man-(1->2)-
CC alpha-Man-(1->3)-[alpha-Man-(1->2)-alpha-Man-(1->3)-[alpha-Man-
CC (1->2)-alpha-Man-(1->6)]-alpha-Man-(1->6)]-beta-Man-(1->4)-beta-
CC GlcNAc-(1->4)-beta-GlcNAc}-L-asparaginyl-[protein] = alpha-D-
CC glucosyl-(1->3)-D-mannopyranose + N(4)-{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-GlaNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 8A1,2,3B1,2); Xref=Rhea:RHEA:54824, Rhea:RHEA-
CC COMP:14010, Rhea:RHEA-COMP:14011, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:52996, ChEBI:CHEBI:59080, ChEBI:CHEBI:60627;
CC EC=3.2.1.130; Evidence={ECO:0000269|PubMed:15677381,
CC ECO:0000269|PubMed:15760709};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.2. {ECO:0000269|PubMed:15677381};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15677381};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15677381, ECO:0000269|PubMed:15760709}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:15677381,
CC ECO:0000269|PubMed:15760709}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and kidney. Expressed
CC at lower levels in muscle, pancreas, heart, placenta, lung and brain.
CC {ECO:0000269|PubMed:15677381}.
CC -!- PTM: Undergoes proteolytic cleavage in the C-terminal region.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 99 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL07306.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD97640.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ577574; CAE12165.1; -; mRNA.
DR EMBL; AY372528; AAQ75077.1; -; mRNA.
DR EMBL; AK022900; BAB14298.1; -; mRNA.
DR EMBL; AK291940; BAF84629.1; -; mRNA.
DR EMBL; BX537398; CAD97640.1; ALT_INIT; mRNA.
DR EMBL; BX640869; CAE45927.1; -; mRNA.
DR EMBL; AL671884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137014; AAI37015.1; -; mRNA.
DR EMBL; BC137016; AAI37017.1; -; mRNA.
DR EMBL; BC146671; AAI46672.1; -; mRNA.
DR EMBL; BC150199; AAI50200.1; -; mRNA.
DR EMBL; AY048774; AAL07306.1; ALT_FRAME; mRNA.
DR CCDS; CCDS5032.1; -.
DR RefSeq; NP_078917.2; NM_024641.3.
DR RefSeq; XP_005267204.1; XM_005267147.3.
DR PDB; 6ZDC; X-ray; 2.25 A; A=98-462.
DR PDB; 6ZDF; X-ray; 3.00 A; A/B/C=98-462.
DR PDB; 6ZDK; X-ray; 2.00 A; AAA=98-462.
DR PDB; 6ZDL; X-ray; 1.90 A; AAA=98-462.
DR PDB; 6ZFA; X-ray; 1.80 A; AAA=98-462.
DR PDB; 6ZFN; X-ray; 1.10 A; AAA=98-462.
DR PDB; 6ZFQ; X-ray; 1.20 A; AAA=98-462.
DR PDB; 6ZJ1; X-ray; 1.96 A; AAA=98-462.
DR PDB; 6ZJ5; X-ray; 2.27 A; AAA=98-462.
DR PDBsum; 6ZDC; -.
DR PDBsum; 6ZDF; -.
DR PDBsum; 6ZDK; -.
DR PDBsum; 6ZDL; -.
DR PDBsum; 6ZFA; -.
DR PDBsum; 6ZFN; -.
DR PDBsum; 6ZFQ; -.
DR PDBsum; 6ZJ1; -.
DR PDBsum; 6ZJ5; -.
DR AlphaFoldDB; Q5SRI9; -.
DR SMR; Q5SRI9; -.
DR BioGRID; 122815; 57.
DR IntAct; Q5SRI9; 16.
DR STRING; 9606.ENSP00000351669; -.
DR CAZy; GH99; Glycoside Hydrolase Family 99.
DR iPTMnet; Q5SRI9; -.
DR PhosphoSitePlus; Q5SRI9; -.
DR SwissPalm; Q5SRI9; -.
DR BioMuta; MANEA; -.
DR DMDM; 74743637; -.
DR EPD; Q5SRI9; -.
DR jPOST; Q5SRI9; -.
DR MassIVE; Q5SRI9; -.
DR MaxQB; Q5SRI9; -.
DR PaxDb; Q5SRI9; -.
DR PeptideAtlas; Q5SRI9; -.
DR PRIDE; Q5SRI9; -.
DR ProteomicsDB; 63853; -.
DR Antibodypedia; 2637; 60 antibodies from 19 providers.
DR DNASU; 79694; -.
DR Ensembl; ENST00000358812.9; ENSP00000351669.4; ENSG00000172469.17.
DR Ensembl; ENST00000682663.1; ENSP00000507267.1; ENSG00000172469.17.
DR Ensembl; ENST00000684753.1; ENSP00000506887.1; ENSG00000172469.17.
DR GeneID; 79694; -.
DR KEGG; hsa:79694; -.
DR MANE-Select; ENST00000358812.9; ENSP00000351669.4; NM_024641.4; NP_078917.2.
DR UCSC; uc003poo.3; human.
DR CTD; 79694; -.
DR DisGeNET; 79694; -.
DR GeneCards; MANEA; -.
DR HGNC; HGNC:21072; MANEA.
DR HPA; ENSG00000172469; Low tissue specificity.
DR MIM; 612327; gene.
DR neXtProt; NX_Q5SRI9; -.
DR OpenTargets; ENSG00000172469; -.
DR PharmGKB; PA134891001; -.
DR VEuPathDB; HostDB:ENSG00000172469; -.
DR eggNOG; ENOG502QPJV; Eukaryota.
DR GeneTree; ENSGT00390000016054; -.
DR HOGENOM; CLU_042710_1_1_1; -.
DR InParanoid; Q5SRI9; -.
DR OMA; ASYNNWP; -.
DR OrthoDB; 975667at2759; -.
DR PhylomeDB; Q5SRI9; -.
DR TreeFam; TF324051; -.
DR BioCyc; MetaCyc:HS16090-MON; -.
DR BRENDA; 3.2.1.130; 2681.
DR PathwayCommons; Q5SRI9; -.
DR Reactome; R-HSA-964739; N-glycan trimming and elongation in the cis-Golgi.
DR SignaLink; Q5SRI9; -.
DR BioGRID-ORCS; 79694; 15 hits in 1077 CRISPR screens.
DR GeneWiki; MANEA; -.
DR GenomeRNAi; 79694; -.
DR Pharos; Q5SRI9; Tbio.
DR PRO; PR:Q5SRI9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5SRI9; protein.
DR Bgee; ENSG00000172469; Expressed in adrenal tissue and 174 other tissues.
DR ExpressionAtlas; Q5SRI9; baseline and differential.
DR Genevisible; Q5SRI9; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0004569; F:glycoprotein endo-alpha-1,2-mannosidase activity; IDA:FlyBase.
DR CDD; cd11574; GH99; 1.
DR InterPro; IPR026071; Glyco_Hydrolase_99.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR13572; PTHR13572; 1.
DR Pfam; PF16317; Glyco_hydro_99; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Golgi apparatus; Hydrolase; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..462
FT /note="Glycoprotein endo-alpha-1,2-mannosidase"
FT /id="PRO_0000282315"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..462
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 60..462
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT VARIANT 331
FT /note="Y -> C (in a breast cancer sample; somatic mutation;
FT dbSNP:rs780723017)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036242"
FT CONFLICT 129
FT /note="E -> G (in Ref. 4; CAD97640)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="N -> S (in Ref. 1; CAE12165)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="F -> I (in Ref. 2; AAQ75077, 3; BAB14298 and 4;
FT CAE45927)"
FT /evidence="ECO:0000305"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:6ZDF"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6ZDF"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6ZDC"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:6ZDC"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:6ZDC"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:6ZDC"
FT HELIX 434..450
FT /evidence="ECO:0007829|PDB:6ZDC"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:6ZDF"
SQ SEQUENCE 462 AA; 53671 MW; CB593CB9B3DAA056 CRC64;
MAKFRRRTCI ILALFILFIF SLMMGLKMLR PNTATFGAPF GLDLLPELHQ RTIHLGKNFD
FQKSDRINSE TNTKNLKSVE ITMKPSKASE LNLDELPPLN NYLHVFYYSW YGNPQFDGKY
IHWNHPVLEH WDPRIAKNYP QGRHNPPDDI GSSFYPELGS YSSRDPSVIE THMRQMRSAS
IGVLALSWYP PDVNDENGEP TDNLVPTILD KAHKYNLKVT FHIEPYSNRD DQNMYKNVKY
IIDKYGNHPA FYRYKTKTGN ALPMFYVYDS YITKPEKWAN LLTTSGSRSI RNSPYDGLFI
ALLVEEKHKY DILQSGFDGI YTYFATNGFT YGSSHQNWAS LKLFCDKYNL IFIPSVGPGY
IDTSIRPWNT QNTRNRINGK YYEIGLSAAL QTRPSLISIT SFNEWHEGTQ IEKAVPKRTS
NTVYLDYRPH KPGLYLELTR KWSEKYSKER ATYALDRQLP VS
