TC753_ARATH
ID TC753_ARATH Reviewed; 818 AA.
AC Q9STE8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein TOC75-3, chloroplastic {ECO:0000305};
DE AltName: Full=75 kDa translocon at the outer-envelope-membrane of chloroplasts 3 {ECO:0000303|PubMed:15908591};
DE Short=AtTOC75-III {ECO:0000303|PubMed:15908591};
DE Flags: Precursor;
GN Name=TOC75-3 {ECO:0000303|PubMed:15908591};
GN Synonyms=TOC75 {ECO:0000303|PubMed:17708964}; OrderedLocusNames=At3g46740;
GN ORFNames=T6H20.230;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NOMENCLATURE.
RX PubMed=17708964; DOI=10.1016/s0962-8924(97)01111-2;
RA Schnell D.J., Blobel G., Keegstra K., Kessler F., Ko K., Soll J.;
RT "A consensus nomenclature for the protein-import components of the
RT chloroplast envelope.";
RL Trends Cell Biol. 7:303-304(1997).
RN [5]
RP INDUCTION.
RX PubMed=11549763; DOI=10.2307/3871427;
RA Sun C.-W., Chen L.-J., Lin L.-C., Li H.-M.;
RT "Leaf-specific upregulation of chloroplast translocon genes by a CCT motif-
RT containing protein, CIA2.";
RL Plant Cell 13:2053-2061(2001).
RN [6]
RP TOC CORE COMPLEX COMPOSITION AND ARCHITECTURE.
RX PubMed=12591914; DOI=10.1083/jcb.200210060;
RA Schleiff E., Soll J., Kuechler M., Kuehlbrandt W., Harrer R.;
RT "Characterization of the translocon of the outer envelope of
RT chloroplasts.";
RL J. Cell Biol. 160:541-551(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [8]
RP PROTEOLYTIC PROCESSING.
RX PubMed=12787247; DOI=10.1046/j.1365-313x.2003.01755.x;
RA Inoue K., Keegstra K.;
RT "A polyglycine stretch is necessary for proper targeting of the protein
RT translocation channel precursor to the outer envelope membrane of
RT chloroplasts.";
RL Plant J. 34:661-669(2003).
RN [9]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH TOC132;
RP TOC120 AND TOC159.
RX PubMed=15090618; DOI=10.1091/mbc.e03-12-0923;
RA Ivanova Y., Smith M.D., Chen K., Schnell D.J.;
RT "Members of the Toc159 import receptor family represent distinct pathways
RT for protein targeting to plastids.";
RL Mol. Biol. Cell 15:3379-3392(2004).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND TRANSMEMBRANE
RP DOMAINS.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=15908591; DOI=10.1104/pp.105.063289;
RA Baldwin A., Wardle A., Patel R., Dudley P., Park S.K., Twell D., Inoue K.,
RA Jarvis P.;
RT "A molecular-genetic study of the Arabidopsis toc75 gene family.";
RL Plant Physiol. 138:715-733(2005).
RN [11]
RP INTERACTION WITH SP1.
RX PubMed=23118188; DOI=10.1126/science.1225053;
RA Ling Q., Huang W., Baldwin A., Jarvis P.;
RT "Chloroplast biogenesis is regulated by direct action of the ubiquitin-
RT proteasome system.";
RL Science 338:655-659(2012).
RN [12]
RP INTERACTION WITH TIC236.
RX PubMed=30464337; DOI=10.1038/s41586-018-0713-y;
RA Chen Y.L., Chen L.J., Chu C.C., Huang P.K., Wen J.R., Li H.M.;
RT "TIC236 links the outer and inner membrane translocons of the
RT chloroplast.";
RL Nature 564:125-129(2018).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 141-449, AND DOMAIN POTRA.
RX PubMed=28559331; DOI=10.1073/pnas.1621179114;
RA O'Neil P.K., Richardson L.G.L., Paila Y.D., Piszczek G., Chakravarthy S.,
RA Noinaj N., Schnell D.;
RT "The POTRA domains of Toc75 exhibit chaperone-like function to facilitate
RT import into chloroplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E4868-E4876(2017).
CC -!- FUNCTION: Essential protein. Mediates the insertion of proteins
CC targeted to the outer membrane of chloroplasts (By similarity).
CC Required for the import of protein precursors into chloroplasts. Forms
CC the voltage-dependent preprotein translocation channels (hydrophilic
CC beta barrel) of the TOC complex in the chloroplastic outer membrane.
CC {ECO:0000250, ECO:0000269|PubMed:15908591}.
CC -!- SUBUNIT: Part of the TOC core complex that includes a protein for the
CC specific recognition of transit peptides surrounded by a ring composed
CC of four proteins forming translocation channels, and four to five GTP-
CC binding proteins providing energy. This core complex can interact with
CC components of the TIC complex to form a larger import complex.
CC Chloroplastic protein precursors such as prSS (precursor of the RuBisCO
CC small subunit) also interact with these complexes. The TOC complex
CC contains a specific subset of polar lipids such as
CC digalactosyldiacylglyceride (DGDG), phosphatidylcholine (PC) and
CC phosphatidylglycerol (PG). TOC75-3 interacts with TOC34/OEP34,
CC TOC159/TOC86, TOC132 and TOC120 (PubMed:15090618). Interacts with SP1
CC (PubMed:23118188). Interacts with TIC236 (PubMed:30464337).
CC {ECO:0000269|PubMed:15090618, ECO:0000269|PubMed:23118188,
CC ECO:0000269|PubMed:30464337}.
CC -!- INTERACTION:
CC Q9STE8; Q8L7N4: SP1; NbExp=2; IntAct=EBI-639078, EBI-6559199;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:15090618}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12766230,
CC ECO:0000269|PubMed:15090618}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in young and actively dividing
CC photosynthetic tissues and, to a lower extent, in old leaves and roots.
CC Particularly low levels in leaves after etiolation.
CC {ECO:0000269|PubMed:15908591}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly during the early stages of
CC plant growth, peaking at three weeks after germination (at protein
CC level). {ECO:0000269|PubMed:15090618}.
CC -!- INDUCTION: Up-regulated by CIA2 in leaves.
CC {ECO:0000269|PubMed:11549763}.
CC -!- DOMAIN: Contains 3 N-terminal periplasmic polypeptide transport-
CC associated (POTRA) domains which may serve as a binding site for the
CC preprotein in the chloroplast intermembrane space, and provide a
CC chaperone-like activity to prevent misfolding or aggregation in the
CC intermembrane space (Probable). Transmembrane regions consist mainly of
CC membrane-spanning sided beta-sheets, which are not predicted by
CC sequence analysis tools (Probable). {ECO:0000305|PubMed:15908591,
CC ECO:0000305|PubMed:28559331}.
CC -!- DISRUPTION PHENOTYPE: Plants have an embryo development arrested at the
CC two cells stage. {ECO:0000269|PubMed:15908591}.
CC -!- SIMILARITY: Belongs to the TOC75 family. {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; AL096859; CAB51191.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78199.1; -; Genomic_DNA.
DR EMBL; AY127014; AAM83239.1; -; mRNA.
DR EMBL; BT006358; AAP21166.1; -; mRNA.
DR PIR; T12975; T12975.
DR RefSeq; NP_190258.1; NM_114541.3.
DR PDB; 5UAY; X-ray; 2.50 A; A=141-449.
DR PDB; 5UBC; X-ray; 2.86 A; A/B=141-449.
DR PDBsum; 5UAY; -.
DR PDBsum; 5UBC; -.
DR AlphaFoldDB; Q9STE8; -.
DR SMR; Q9STE8; -.
DR BioGRID; 9147; 6.
DR IntAct; Q9STE8; 3.
DR STRING; 3702.AT3G46740.1; -.
DR PaxDb; Q9STE8; -.
DR PRIDE; Q9STE8; -.
DR ProteomicsDB; 246468; -.
DR EnsemblPlants; AT3G46740.1; AT3G46740.1; AT3G46740.
DR GeneID; 823827; -.
DR Gramene; AT3G46740.1; AT3G46740.1; AT3G46740.
DR KEGG; ath:AT3G46740; -.
DR Araport; AT3G46740; -.
DR TAIR; locus:2102767; AT3G46740.
DR eggNOG; ENOG502QTZ3; Eukaryota.
DR HOGENOM; CLU_000837_26_1_1; -.
DR InParanoid; Q9STE8; -.
DR OMA; DERSHIC; -.
DR OrthoDB; 455003at2759; -.
DR PhylomeDB; Q9STE8; -.
DR PRO; PR:Q9STE8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STE8; baseline and differential.
DR Genevisible; Q9STE8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0001401; C:SAM complex; IBA:GO_Central.
DR GO; GO:0010006; C:Toc complex; ISS:TAIR.
DR GO; GO:0061927; C:TOC-TIC supercomplex I; IDA:TAIR.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0045036; P:protein targeting to chloroplast; IDA:TAIR.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR InterPro; IPR039910; D15-like.
DR InterPro; IPR005689; IAP75.
DR PANTHER; PTHR12815; PTHR12815; 1.
DR Pfam; PF01103; Omp85; 1.
DR TIGRFAMs; TIGR00992; 3a0901s03IAP75; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Membrane; Plastid; Plastid outer membrane;
KW Protein transport; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane beta strand; Transport.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 80..140
FT /note="Chloroplast; outer membrane"
FT /evidence="ECO:0000255"
FT CHAIN 141..818
FT /note="Protein TOC75-3, chloroplastic"
FT /id="PRO_0000042821"
FT TOPO_DOM 141..473
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305|PubMed:28559331"
FT TRANSMEM 474..482
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..518
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..562
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..570
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..586
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..693
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..702
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..723
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..785
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..792
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..806
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 807..814
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 815..818
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 141..246
FT /note="POTRA 1"
FT /evidence="ECO:0000305|PubMed:28559331"
FT DOMAIN 247..364
FT /note="POTRA 2"
FT /evidence="ECO:0000305|PubMed:28559331"
FT DOMAIN 365..448
FT /note="POTRA 3"
FT /evidence="ECO:0000305|PubMed:28559331"
FT REGION 15..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:5UAY"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 219..231
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 276..296
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 322..338
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 365..374
FT /evidence="ECO:0007829|PDB:5UAY"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:5UBC"
FT HELIX 387..393
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:5UAY"
FT HELIX 406..417
FT /evidence="ECO:0007829|PDB:5UAY"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 422..431
FT /evidence="ECO:0007829|PDB:5UAY"
FT STRAND 436..447
FT /evidence="ECO:0007829|PDB:5UAY"
SQ SEQUENCE 818 AA; 89189 MW; 332E04D308F370F6 CRC64;
MAAFSVNGQL IPTATSSTAS TSLSSRRKFL SPSSSRLPRI STQSPRVPSI KCSKSLPNRD
TETSSKDSLL KNLAKPLAVA SVSSAASFFL FRISNLPSVL TGGGGGGDGN FGGFGGGGGG
GDGNDGGFWG KLFSPSPAVA DEEQSPDWDS HGLPANIVVQ LNKLSGFKKY KVSDIMFFDR
RRQTTIGTED SFFEMVSIRP GGVYTKAQLQ KELETLATCG MFEKVDLEGK TKPDGTLGVT
ISFAESTWQS ADRFRCINVG LMVQSKPIEM DSDMTDKEKL EYYRSLEKDY KRRIDRARPC
LLPAPVYGEV MQMLRDQGKV SARLLQRIRD RVQKWYHDEG YACAQVVNFG NLNTKEVVCE
VVEGDITQLV IQFQDKLGNV VEGNTQVPVV RRELPKQLRQ GYVFNIEAGK KALSNINSLG
LFSNIEVNPR PDEKNEGGII VEIKLKELEQ KSAEVSTEWS IVPGRGGAPT LASFQPGGSV
TFEHRNLQGL NRSLMGSVTT SNFLNPQDDL SFKLEYVHPY LDGVYNPRNR TFKTSCFNSR
KLSPVFTGGP GVEEVPPIWV DRAGVKANIT ENFTRQSKFT YGLVMEEITT RDESSHIAAN
GQRLLPSGGI SADGPPTTLS GTGVDRMAFL QANITRDNTK FVNGAVVGQR TVFQVDQGLG
IGSKFPFFNR HQLTMTKFIQ LREVEQGAGK SPPPVLVLHG HYGGCVGDLP SYDAFVLGGP
YSVRGYNMGE LGAARNIAEV GAEIRIPVKN THVYAFVEHG NDLGSSKDVK GNPTAVYRRT
GQGSSYGAGV KLGLVRAEYA VDHNNGTGAL FFRFGERY
