TPST1_HUMAN
ID TPST1_HUMAN Reviewed; 370 AA.
AC O60507; A4D2M0; Q6FGM7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein-tyrosine sulfotransferase 1;
DE EC=2.8.2.20 {ECO:0000269|PubMed:28821720, ECO:0000269|PubMed:9501187, ECO:0000269|PubMed:9733778};
DE AltName: Full=Tyrosylprotein sulfotransferase 1;
DE Short=TPST-1;
GN Name=TPST1;
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], FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=9501187; DOI=10.1073/pnas.95.6.2896;
RA Ouyang Y.-B., Lane W.S., Moore K.L.;
RT "Tyrosylprotein sulfotransferase: purification and molecular cloning of an
RT enzyme that catalyzes tyrosine O-sulfation, a common posttranslational
RT modification of eukaryotic proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2896-2901(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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 GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9733778; DOI=10.1074/jbc.273.38.24770;
RA Ouyang Y.-B., Moore K.L.;
RT "Molecular cloning and expression of human and mouse tyrosylprotein
RT sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 273:24770-24774(1998).
RN [8]
RP GLYCOSYLATION AT ASN-60 AND ASN-262, SUBUNIT, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND MUTAGENESIS OF ASN-60 AND ASN-262.
RX PubMed=16859706; DOI=10.1016/j.jmb.2006.06.023;
RA Goettsch S., Badea R.A., Mueller J.W., Wotzlaw C., Schoelermann B.,
RA Schulz L., Rabiller M., Bayer P., Hartmann-Fatu C.;
RT "Human TPST1 transmembrane domain triggers enzyme dimerisation and
RT localisation to the Golgi compartment.";
RL J. Mol. Biol. 361:436-449(2006).
RN [9]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH TPST2.
RX PubMed=25660941; DOI=10.1016/j.jmb.2015.01.021;
RA Hartmann-Fatu C., Trusch F., Moll C.N., Michin I., Hassinen A.,
RA Kellokumpu S., Bayer P.;
RT "Heterodimers of tyrosylprotein sulfotransferases suggest existence of a
RT higher organization level of transferases in the membrane of the trans-
RT Golgi apparatus.";
RL J. Mol. Biol. 427:1404-1412(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 43-341 IN COMPLEX WITH ADENOSINE
RP 3',5'-BISPHOSPHATE AND SUBSTRATE PEPTIDE, FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=28821720; DOI=10.1038/s41598-017-07141-8;
RA Tanaka S., Nishiyori T., Kojo H., Otsubo R., Tsuruta M., Kurogi K.,
RA Liu M.C., Suiko M., Sakakibara Y., Kakuta Y.;
RT "Structural basis for the broad substrate specificity of the human
RT tyrosylprotein sulfotransferase-1.";
RL Sci. Rep. 7:8776-8776(2017).
CC -!- FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic
CC motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as
CC cosubstrate. {ECO:0000269|PubMed:28821720, ECO:0000269|PubMed:9501187,
CC ECO:0000269|PubMed:9733778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine
CC 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein];
CC Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20;
CC Evidence={ECO:0000269|PubMed:28821720, ECO:0000269|PubMed:9501187,
CC ECO:0000269|PubMed:9733778};
CC -!- SUBUNIT: Homodimer (PubMed:16859706, PubMed:28821720). Can also form
CC heterodimers with TPST2 (PubMed:25660941).
CC {ECO:0000269|PubMed:16859706, ECO:0000269|PubMed:25660941,
CC ECO:0000269|PubMed:28821720}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16859706, ECO:0000269|PubMed:25660941}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:25660941,
CC ECO:0000305|PubMed:16859706}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, placenta,
CC lung, liver, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:9501187}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16859706,
CC ECO:0000269|PubMed:9501187}.
CC -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {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; AF038009; AAC13552.1; -; mRNA.
DR EMBL; AK313098; BAG35922.1; -; mRNA.
DR EMBL; CR542060; CAG46857.1; -; mRNA.
DR EMBL; CR542080; CAG46877.1; -; mRNA.
DR EMBL; CH236961; EAL23739.1; -; Genomic_DNA.
DR EMBL; CH471140; EAX07937.1; -; Genomic_DNA.
DR EMBL; BC013188; AAH13188.1; -; mRNA.
DR CCDS; CCDS5533.1; -.
DR RefSeq; NP_003587.1; NM_003596.3.
DR RefSeq; XP_016868214.1; XM_017012725.1.
DR RefSeq; XP_016868215.1; XM_017012726.1.
DR RefSeq; XP_016868216.1; XM_017012727.1.
DR PDB; 5WRI; X-ray; 1.60 A; A/B=43-341.
DR PDB; 5WRJ; X-ray; 2.31 A; A/B/C/D=43-341.
DR PDBsum; 5WRI; -.
DR PDBsum; 5WRJ; -.
DR AlphaFoldDB; O60507; -.
DR SMR; O60507; -.
DR BioGRID; 114038; 19.
DR IntAct; O60507; 5.
DR STRING; 9606.ENSP00000302413; -.
DR GlyGen; O60507; 2 sites.
DR iPTMnet; O60507; -.
DR PhosphoSitePlus; O60507; -.
DR BioMuta; TPST1; -.
DR EPD; O60507; -.
DR jPOST; O60507; -.
DR MassIVE; O60507; -.
DR MaxQB; O60507; -.
DR PaxDb; O60507; -.
DR PeptideAtlas; O60507; -.
DR PRIDE; O60507; -.
DR ProteomicsDB; 49449; -.
DR Antibodypedia; 35330; 160 antibodies from 18 providers.
DR DNASU; 8460; -.
DR Ensembl; ENST00000304842.6; ENSP00000302413.5; ENSG00000169902.15.
DR Ensembl; ENST00000649664.1; ENSP00000497281.1; ENSG00000169902.15.
DR GeneID; 8460; -.
DR KEGG; hsa:8460; -.
DR MANE-Select; ENST00000304842.6; ENSP00000302413.5; NM_003596.4; NP_003587.1.
DR UCSC; uc003tuw.4; human.
DR CTD; 8460; -.
DR DisGeNET; 8460; -.
DR GeneCards; TPST1; -.
DR HGNC; HGNC:12020; TPST1.
DR HPA; ENSG00000169902; Low tissue specificity.
DR MIM; 603125; gene.
DR neXtProt; NX_O60507; -.
DR OpenTargets; ENSG00000169902; -.
DR PharmGKB; PA36699; -.
DR VEuPathDB; HostDB:ENSG00000169902; -.
DR eggNOG; KOG3988; Eukaryota.
DR GeneTree; ENSGT00390000006030; -.
DR HOGENOM; CLU_046916_0_1_1; -.
DR InParanoid; O60507; -.
DR OMA; LNDFRQC; -.
DR OrthoDB; 671992at2759; -.
DR PhylomeDB; O60507; -.
DR TreeFam; TF312910; -.
DR BioCyc; MetaCyc:HS10030-MON; -.
DR BRENDA; 2.8.2.20; 2681.
DR PathwayCommons; O60507; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-HSA-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR Reactome; R-HSA-9674519; Defective F8 sulfation at Y1699.
DR SignaLink; O60507; -.
DR BioGRID-ORCS; 8460; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; TPST1; human.
DR GenomeRNAi; 8460; -.
DR Pharos; O60507; Tbio.
DR PRO; PR:O60507; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O60507; protein.
DR Bgee; ENSG00000169902; Expressed in stromal cell of endometrium and 170 other tissues.
DR ExpressionAtlas; O60507; baseline and differential.
DR Genevisible; O60507; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; TAS:Reactome.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026634; TPST.
DR PANTHER; PTHR12788; PTHR12788; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="Protein-tyrosine sulfotransferase 1"
FT /id="PRO_0000189826"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 102..106
FT /note="Interaction with peptide substrate"
FT /evidence="ECO:0000269|PubMed:28821720"
FT ACT_SITE 100
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 79..83
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:28821720,
FT ECO:0007744|PDB:5WRI, ECO:0007744|PDB:5WRJ"
FT BINDING 184
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:28821720,
FT ECO:0007744|PDB:5WRI, ECO:0007744|PDB:5WRJ"
FT BINDING 192
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:28821720,
FT ECO:0007744|PDB:5WRI, ECO:0007744|PDB:5WRJ"
FT BINDING 196
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:28821720,
FT ECO:0007744|PDB:5WRI"
FT BINDING 239
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:28821720,
FT ECO:0007744|PDB:5WRI, ECO:0007744|PDB:5WRJ"
FT BINDING 286..295
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:28821720,
FT ECO:0007744|PDB:5WRI, ECO:0007744|PDB:5WRJ"
FT BINDING 301
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:28821720,
FT ECO:0007744|PDB:5WRI, ECO:0007744|PDB:5WRJ"
FT SITE 159
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 286
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16859706"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16859706"
FT DISULFID 97..157
FT /evidence="ECO:0000269|PubMed:28821720"
FT DISULFID 226..234
FT /evidence="ECO:0000269|PubMed:28821720"
FT MUTAGEN 60
FT /note="N->A: Loss of one glycosylation site. Loss of N-
FT glycosylation; when associated with A-262."
FT /evidence="ECO:0000269|PubMed:16859706"
FT MUTAGEN 262
FT /note="N->A: Loss of one glycosylation site. Loss of N-
FT glycosylation; when associated with A-60."
FT /evidence="ECO:0000269|PubMed:16859706"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:5WRI"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:5WRI"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:5WRI"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 208..229
FT /evidence="ECO:0007829|PDB:5WRI"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:5WRI"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:5WRI"
FT TURN 301..305
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:5WRI"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:5WRI"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5WRJ"
SQ SEQUENCE 370 AA; 42188 MW; FB9EB341AFE36407 CRC64;
MVGKLKQNLL LACLVISSVT VFYLGQHAME CHHRIEERSQ PVKLESTRTT VRTGLDLKAN
KTFAYHKDMP LIFIGGVPRS GTTLMRAMLD AHPDIRCGEE TRVIPRILAL KQMWSRSSKE
KIRLDEAGVT DEVLDSAMQA FLLEIIVKHG EPAPYLCNKD PFALKSLTYL SRLFPNAKFL
LMVRDGRASV HSMISRKVTI AGFDLNSYRD CLTKWNRAIE TMYNQCMEVG YKKCMLVHYE
QLVLHPERWM RTLLKFLQIP WNHSVLHHEE MIGKAGGVSL SKVERSTDQV IKPVNVGALS
KWVGKIPPDV LQDMAVIAPM LAKLGYDPYA NPPNYGKPDP KIIENTRRVY KGEFQLPDFL
KEKPQTEQVE
