SIT1_HUMAN
ID SIT1_HUMAN Reviewed; 196 AA.
AC Q9Y3P8; B2RBP9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Signaling threshold-regulating transmembrane adapter 1;
DE AltName: Full=SHP2-interacting transmembrane adapter protein;
DE AltName: Full=Suppression-inducing transmembrane adapter 1;
DE AltName: Full=gp30/40;
DE Flags: Precursor;
GN Name=SIT1; Synonyms=SIT;
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], PROTEIN SEQUENCE OF 148-158, IDENTIFICATION BY
RP MASS SPECTROMETRY, DIMERIZATION, GLYCOSYLATION AT ASN-26, PHOSPHORYLATION
RP AT TYR-148, MUTAGENESIS OF ASN-26 AND TYR-148, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INTERACTION WITH PTPN11, AND FUNCTION.
RX PubMed=10209036; DOI=10.1084/jem.189.8.1181;
RA Marie-Cardine A., Kirchgessner H., Bruyns E., Shevchenko A., Mann M.,
RA Autschbach F., Ratnofsky S., Meuer S., Schraven B.;
RT "SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-
RT linked dimer regulating human T-cell activation.";
RL J. Exp. Med. 189:1181-1194(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11491537; DOI=10.1007/s002510100328;
RA Huebener C., Mincheva A., Lichter P., Schraven B., Bruyns E.;
RT "Complete sequence, genomic organization, and chromosomal localization of
RT the human gene encoding the SHP2-interacting transmembrane adaptor protein
RT (SIT).";
RL Immunogenetics 53:337-341(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 MUTAGENESIS OF TYR-90; TYR-127; TYR-148; TYR-169 AND TYR-188,
RP PHOSPHORYLATION AT TYR-90; TYR-127; TYR-148; TYR-169 AND TYR-188, AND
RP INTERACTION WITH PTPN11; GRB2 AND CSK.
RX PubMed=11433379;
RX DOI=10.1002/1521-4141(200106)31:6<1825::aid-immu1825>3.0.co;2-v;
RA Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A.,
RA Spicka J., Hilgert I., Scherer J., Schraven B.;
RT "Structural and functional dissection of the cytoplasmic domain of the
RT transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor
RT protein).";
RL Eur. J. Immunol. 31:1825-1836(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; TYR-90; THR-144; SER-182
RP AND TYR-188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=16160011; DOI=10.1182/blood-2005-06-2273;
RA Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T.,
RA Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L., Pozzobon M.,
RA Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T., Horejsi V.;
RT "Transmembrane adaptor molecules: a new category of lymphoid-cell
RT markers.";
RL Blood 107:213-221(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; THR-144; TYR-148;
RP SER-182 AND TYR-188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-mediated
CC signaling in T-cells. Involved in positive selection of T-cells.
CC {ECO:0000269|PubMed:10209036}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. When phosphorylated, interacts
CC with PTPN11/SHP2, GRB2 and CSK. {ECO:0000269|PubMed:10209036,
CC ECO:0000269|PubMed:11433379}.
CC -!- INTERACTION:
CC Q9Y3P8; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-6977215, EBI-4290634;
CC Q9Y3P8; O95393: BMP10; NbExp=3; IntAct=EBI-6977215, EBI-3922513;
CC Q9Y3P8; A0PK11: CLRN2; NbExp=3; IntAct=EBI-6977215, EBI-12813623;
CC Q9Y3P8; O43736: ITM2A; NbExp=3; IntAct=EBI-6977215, EBI-2431769;
CC Q9Y3P8; Q13021: MALL; NbExp=3; IntAct=EBI-6977215, EBI-750078;
CC Q9Y3P8; P26678: PLN; NbExp=3; IntAct=EBI-6977215, EBI-692836;
CC Q9Y3P8; P55061: TMBIM6; NbExp=3; IntAct=EBI-6977215, EBI-1045825;
CC Q9Y3P8; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-6977215, EBI-2844246;
CC Q9Y3P8; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-6977215, EBI-12045841;
CC Q9Y3P8; O75841: UPK1B; NbExp=3; IntAct=EBI-6977215, EBI-12237619;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10209036};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:10209036}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in T- and B-cells. Present
CC in plasma cells but not in germinal center B-cells (at protein level).
CC Expressed in T- and B-cell lymphoma. {ECO:0000269|PubMed:10209036,
CC ECO:0000269|PubMed:16160011}.
CC -!- PTM: Phosphorylated on tyrosines by LCK, FYN or ZAP70 upon TCR
CC activation; which leads to the recruitment of PTPN11, GRB2 and CSK.
CC {ECO:0000269|PubMed:10209036, ECO:0000269|PubMed:11433379}.
CC -!- CAUTION: In contrast to its orthologs it harbors a signal sequence.
CC {ECO:0000305}.
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DR EMBL; AJ010059; CAB41504.1; -; mRNA.
DR EMBL; AJ271888; CAC81313.1; -; Genomic_DNA.
DR EMBL; AK314758; BAG37296.1; -; mRNA.
DR EMBL; AL357874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58370.1; -; Genomic_DNA.
DR EMBL; BC102029; AAI02030.1; -; mRNA.
DR EMBL; BC104491; AAI04492.1; -; mRNA.
DR EMBL; BC107484; AAI07485.1; -; mRNA.
DR CCDS; CCDS6582.1; -.
DR RefSeq; NP_055265.1; NM_014450.2.
DR AlphaFoldDB; Q9Y3P8; -.
DR BioGRID; 118088; 17.
DR IntAct; Q9Y3P8; 11.
DR MINT; Q9Y3P8; -.
DR STRING; 9606.ENSP00000259608; -.
DR GlyGen; Q9Y3P8; 1 site.
DR iPTMnet; Q9Y3P8; -.
DR PhosphoSitePlus; Q9Y3P8; -.
DR BioMuta; SIT1; -.
DR DMDM; 74753488; -.
DR jPOST; Q9Y3P8; -.
DR MassIVE; Q9Y3P8; -.
DR MaxQB; Q9Y3P8; -.
DR PaxDb; Q9Y3P8; -.
DR PeptideAtlas; Q9Y3P8; -.
DR PRIDE; Q9Y3P8; -.
DR ProteomicsDB; 86053; -.
DR Antibodypedia; 11587; 218 antibodies from 28 providers.
DR DNASU; 27240; -.
DR Ensembl; ENST00000259608.8; ENSP00000259608.3; ENSG00000137078.10.
DR GeneID; 27240; -.
DR KEGG; hsa:27240; -.
DR MANE-Select; ENST00000259608.8; ENSP00000259608.3; NM_014450.3; NP_055265.1.
DR UCSC; uc003zxe.3; human.
DR CTD; 27240; -.
DR DisGeNET; 27240; -.
DR GeneCards; SIT1; -.
DR HGNC; HGNC:17710; SIT1.
DR HPA; ENSG00000137078; Tissue enriched (lymphoid).
DR MIM; 604964; gene.
DR neXtProt; NX_Q9Y3P8; -.
DR OpenTargets; ENSG00000137078; -.
DR PharmGKB; PA142670914; -.
DR VEuPathDB; HostDB:ENSG00000137078; -.
DR eggNOG; ENOG502S87Q; Eukaryota.
DR GeneTree; ENSGT00390000016476; -.
DR HOGENOM; CLU_111407_0_0_1; -.
DR InParanoid; Q9Y3P8; -.
DR OrthoDB; 1355800at2759; -.
DR PhylomeDB; Q9Y3P8; -.
DR TreeFam; TF337816; -.
DR PathwayCommons; Q9Y3P8; -.
DR SignaLink; Q9Y3P8; -.
DR BioGRID-ORCS; 27240; 7 hits in 1067 CRISPR screens.
DR ChiTaRS; SIT1; human.
DR GeneWiki; SIT1; -.
DR GenomeRNAi; 27240; -.
DR Pharos; Q9Y3P8; Tbio.
DR PRO; PR:Q9Y3P8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y3P8; protein.
DR Bgee; ENSG00000137078; Expressed in granulocyte and 126 other tissues.
DR ExpressionAtlas; Q9Y3P8; baseline and differential.
DR Genevisible; Q9Y3P8; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; TAS:HGNC-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050863; P:regulation of T cell activation; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
DR InterPro; IPR033269; Sit1.
DR PANTHER; PTHR15604; PTHR15604; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..196
FT /note="Signaling threshold-regulating transmembrane adapter
FT 1"
FT /id="PRO_0000045152"
FT TOPO_DOM 25..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 90..93
FT /note="Interaction with GRB2"
FT /evidence="ECO:0000269|PubMed:11433379"
FT REGION 132..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..151
FT /note="Interaction with PTPN11"
FT REGION 169..172
FT /note="Interaction with CSK"
FT /evidence="ECO:0000269|PubMed:11433379"
FT REGION 188..191
FT /note="Interaction with GRB2"
FT /evidence="ECO:0000269|PubMed:11433379"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M869"
FT MOD_RES 90
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11433379,
FT ECO:0007744|PubMed:15144186"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:11433379"
FT MOD_RES 144
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 148
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10209036,
FT ECO:0000269|PubMed:11433379, ECO:0007744|PubMed:19690332"
FT MOD_RES 169
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:11433379"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11433379,
FT ECO:0007744|PubMed:15144186, ECO:0007744|PubMed:19690332"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10209036"
FT DISULFID 27
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT MUTAGEN 26
FT /note="N->Q: Abolishes glycosylation."
FT /evidence="ECO:0000269|PubMed:10209036"
FT MUTAGEN 90
FT /note="Y->F: Reduces interaction with GRB2. Abolishes
FT interaction with GRB2; when associated with F-188."
FT /evidence="ECO:0000269|PubMed:11433379"
FT MUTAGEN 127
FT /note="Y->F: No effect on interaction with PTPN11 or GRB2."
FT /evidence="ECO:0000269|PubMed:11433379"
FT MUTAGEN 148
FT /note="Y->F: Reduces interaction with PTPN11, no effect on
FT inhibition of NF-AT activation."
FT /evidence="ECO:0000269|PubMed:10209036,
FT ECO:0000269|PubMed:11433379"
FT MUTAGEN 169
FT /note="Y->F: Abolishes interaction with CSK and impairs
FT inhibition of NF-AT activation."
FT /evidence="ECO:0000269|PubMed:11433379"
FT MUTAGEN 188
FT /note="Y->F: Reduces interaction with GRB2. Abolishes
FT interaction with GRB2; when associated with F-90."
FT /evidence="ECO:0000269|PubMed:11433379"
SQ SEQUENCE 196 AA; 21126 MW; 2A0C48C9466F7F07 CRC64;
MNQADPRLRA VCLWTLTSAA MSRGDNCTDL LALGIPSITQ AWGLWVLLGA VTLLFLISLA
AHLSQWTRGR SRSHPGQGRS GESVEEVPLY GNLHYLQTGR LSQDPEPDQQ DPTLGGPARA
AEEVMCYTSL QLRPPQGRIP GPGTPVKYSE VVLDSEPKSQ ASGPEPELYA SVCAQTRRAR
ASFPDQAYAN SQPAAS
