Full text data of DHRS11
DHRS11
[Confidence: low (only semi-automatic identification from reviews)]
Dehydrogenase/reductase SDR family member 11; 1.-.-.-; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dehydrogenase/reductase SDR family member 11; 1.-.-.-; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6UWP2
ID DHR11_HUMAN Reviewed; 260 AA.
AC Q6UWP2; B2RDZ3; Q9BUC7; Q9H674;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Dehydrogenase/reductase SDR family member 11;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=DHRS11; ORFNames=UNQ836/PRO1774;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex, and Small intestine;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 1-256 (ISOFORM 1) IN COMPLEX
RP WITH NADP AND ACETATE, AND SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Structure of the putative human dehydrogenase MGC4172.";
RL Submitted (OCT-2004) to the PDB data bank.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6UWP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UWP2-2; Sequence=VSP_016987;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
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; AY358712; AAQ89074.1; -; mRNA.
DR EMBL; AK026196; BAB15390.1; -; mRNA.
DR EMBL; AK315735; BAG38090.1; -; mRNA.
DR EMBL; CR457356; CAG33637.1; -; mRNA.
DR EMBL; BC002731; AAH02731.2; -; mRNA.
DR RefSeq; NP_077284.2; NM_024308.3.
DR UniGene; Hs.462859; -.
DR PDB; 1XG5; X-ray; 1.53 A; A/B/C/D=1-256.
DR PDBsum; 1XG5; -.
DR ProteinModelPortal; Q6UWP2; -.
DR SMR; Q6UWP2; 2-256.
DR STRING; 9606.ENSP00000251312; -.
DR PhosphoSite; Q6UWP2; -.
DR DMDM; 74749397; -.
DR PaxDb; Q6UWP2; -.
DR PRIDE; Q6UWP2; -.
DR Ensembl; ENST00000251312; ENSP00000251312; ENSG00000108272.
DR Ensembl; ENST00000568873; ENSP00000456222; ENSG00000261508.
DR Ensembl; ENST00000590554; ENSP00000467412; ENSG00000108272.
DR GeneID; 79154; -.
DR KEGG; hsa:79154; -.
DR UCSC; uc002hnd.3; human.
DR CTD; 79154; -.
DR GeneCards; GC17P034948; -.
DR HGNC; HGNC:28639; DHRS11.
DR HPA; HPA041226; -.
DR HPA; HPA048236; -.
DR HPA; HPA053623; -.
DR neXtProt; NX_Q6UWP2; -.
DR PharmGKB; PA164718841; -.
DR eggNOG; COG4221; -.
DR HOVERGEN; HBG105262; -.
DR InParanoid; Q6UWP2; -.
DR OMA; CGHRVPP; -.
DR ChiTaRS; DHRS11; human.
DR EvolutionaryTrace; Q6UWP2; -.
DR GenomeRNAi; 79154; -.
DR NextBio; 68076; -.
DR PRO; PR:Q6UWP2; -.
DR ArrayExpress; Q6UWP2; -.
DR Bgee; Q6UWP2; -.
DR Genevestigator; Q6UWP2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; NADP;
KW Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1 30 Potential.
FT CHAIN 31 260 Dehydrogenase/reductase SDR family member
FT 11.
FT /FTId=PRO_0000045490.
FT NP_BIND 69 71 NADP.
FT NP_BIND 166 170 NADP.
FT NP_BIND 198 208 NADP.
FT ACT_SITE 166 166 Proton acceptor (By similarity).
FT BINDING 151 151 Substrate (By similarity).
FT VAR_SEQ 1 79 Missing (in isoform 2).
FT /FTId=VSP_016987.
FT CONFLICT 81 81 F -> S (in Ref. 2; BAB15390 and 3;
FT CAG33637).
FT HELIX 7 9
FT STRAND 13 18
FT HELIX 22 33
FT STRAND 37 43
FT HELIX 45 57
FT STRAND 61 68
FT HELIX 74 88
FT STRAND 92 96
FT TURN 106 108
FT HELIX 111 121
FT HELIX 123 138
FT STRAND 145 149
FT HELIX 152 154
FT HELIX 161 163
FT HELIX 164 186
FT STRAND 192 199
FT HELIX 205 209
FT TURN 210 212
FT HELIX 214 221
FT HELIX 229 241
FT STRAND 246 255
SQ SEQUENCE 260 AA; 28308 MW; 88DFF656874F19F4 CRC64;
MARPGMERWR DRLALVTGAS GGIGAAVARA LVQQGLKVVG CARTVGNIEE LAAECKSAGY
PGTLIPYRCD LSNEEDILSM FSAIRSQHSG VDICINNAGL ARPDTLLSGS TSGWKDMFNV
NVLALSICTR EAYQSMKERN VDDGHIININ SMSGHRVLPL SVTHFYSATK YAVTALTEGL
RQELREAQTH IRATCISPGV VETQFAFKLH DKDPEKAAAT YEQMKCLKPE DVAEAVIYVL
STPAHIQIGD IQMRPTEQVT
//
ID DHR11_HUMAN Reviewed; 260 AA.
AC Q6UWP2; B2RDZ3; Q9BUC7; Q9H674;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Dehydrogenase/reductase SDR family member 11;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=DHRS11; ORFNames=UNQ836/PRO1774;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex, and Small intestine;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 1-256 (ISOFORM 1) IN COMPLEX
RP WITH NADP AND ACETATE, AND SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Structure of the putative human dehydrogenase MGC4172.";
RL Submitted (OCT-2004) to the PDB data bank.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6UWP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UWP2-2; Sequence=VSP_016987;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
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; AY358712; AAQ89074.1; -; mRNA.
DR EMBL; AK026196; BAB15390.1; -; mRNA.
DR EMBL; AK315735; BAG38090.1; -; mRNA.
DR EMBL; CR457356; CAG33637.1; -; mRNA.
DR EMBL; BC002731; AAH02731.2; -; mRNA.
DR RefSeq; NP_077284.2; NM_024308.3.
DR UniGene; Hs.462859; -.
DR PDB; 1XG5; X-ray; 1.53 A; A/B/C/D=1-256.
DR PDBsum; 1XG5; -.
DR ProteinModelPortal; Q6UWP2; -.
DR SMR; Q6UWP2; 2-256.
DR STRING; 9606.ENSP00000251312; -.
DR PhosphoSite; Q6UWP2; -.
DR DMDM; 74749397; -.
DR PaxDb; Q6UWP2; -.
DR PRIDE; Q6UWP2; -.
DR Ensembl; ENST00000251312; ENSP00000251312; ENSG00000108272.
DR Ensembl; ENST00000568873; ENSP00000456222; ENSG00000261508.
DR Ensembl; ENST00000590554; ENSP00000467412; ENSG00000108272.
DR GeneID; 79154; -.
DR KEGG; hsa:79154; -.
DR UCSC; uc002hnd.3; human.
DR CTD; 79154; -.
DR GeneCards; GC17P034948; -.
DR HGNC; HGNC:28639; DHRS11.
DR HPA; HPA041226; -.
DR HPA; HPA048236; -.
DR HPA; HPA053623; -.
DR neXtProt; NX_Q6UWP2; -.
DR PharmGKB; PA164718841; -.
DR eggNOG; COG4221; -.
DR HOVERGEN; HBG105262; -.
DR InParanoid; Q6UWP2; -.
DR OMA; CGHRVPP; -.
DR ChiTaRS; DHRS11; human.
DR EvolutionaryTrace; Q6UWP2; -.
DR GenomeRNAi; 79154; -.
DR NextBio; 68076; -.
DR PRO; PR:Q6UWP2; -.
DR ArrayExpress; Q6UWP2; -.
DR Bgee; Q6UWP2; -.
DR Genevestigator; Q6UWP2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; NADP;
KW Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1 30 Potential.
FT CHAIN 31 260 Dehydrogenase/reductase SDR family member
FT 11.
FT /FTId=PRO_0000045490.
FT NP_BIND 69 71 NADP.
FT NP_BIND 166 170 NADP.
FT NP_BIND 198 208 NADP.
FT ACT_SITE 166 166 Proton acceptor (By similarity).
FT BINDING 151 151 Substrate (By similarity).
FT VAR_SEQ 1 79 Missing (in isoform 2).
FT /FTId=VSP_016987.
FT CONFLICT 81 81 F -> S (in Ref. 2; BAB15390 and 3;
FT CAG33637).
FT HELIX 7 9
FT STRAND 13 18
FT HELIX 22 33
FT STRAND 37 43
FT HELIX 45 57
FT STRAND 61 68
FT HELIX 74 88
FT STRAND 92 96
FT TURN 106 108
FT HELIX 111 121
FT HELIX 123 138
FT STRAND 145 149
FT HELIX 152 154
FT HELIX 161 163
FT HELIX 164 186
FT STRAND 192 199
FT HELIX 205 209
FT TURN 210 212
FT HELIX 214 221
FT HELIX 229 241
FT STRAND 246 255
SQ SEQUENCE 260 AA; 28308 MW; 88DFF656874F19F4 CRC64;
MARPGMERWR DRLALVTGAS GGIGAAVARA LVQQGLKVVG CARTVGNIEE LAAECKSAGY
PGTLIPYRCD LSNEEDILSM FSAIRSQHSG VDICINNAGL ARPDTLLSGS TSGWKDMFNV
NVLALSICTR EAYQSMKERN VDDGHIININ SMSGHRVLPL SVTHFYSATK YAVTALTEGL
RQELREAQTH IRATCISPGV VETQFAFKLH DKDPEKAAAT YEQMKCLKPE DVAEAVIYVL
STPAHIQIGD IQMRPTEQVT
//