PIB2_YEAST
ID PIB2_YEAST Reviewed; 635 AA.
AC P53191; D6VUB4; E9P8Z2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glutamine sensor PIB2 {ECO:0000303|PubMed:34535752};
DE AltName: Full=Phosphatidylinositol 3-phosphate-binding protein 2 {ECO:0000305};
GN Name=PIB2 {ECO:0000312|SGD:S000002991};
GN OrderedLocusNames=YGL023C {ECO:0000312|SGD:S000002991};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-124; SER-165;
RP SER-174 AND SER-300, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-53; THR-56; SER-73;
RP SER-113; SER-165; SER-300; SER-309 AND SER-381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN FYVE-TYPE, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 621-SER--PHE-635.
RX PubMed=26510498; DOI=10.1091/mbc.e15-08-0581;
RA Kim A., Cunningham K.W.;
RT "A LAPF/phafin1-like protein regulates TORC1 and lysosomal membrane
RT permeabilization in response to endoplasmic reticulum membrane stress.";
RL Mol. Biol. Cell 26:4631-4645(2015).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH TOR1, AND DISRUPTION PHENOTYPE.
RX PubMed=28483912; DOI=10.1128/mcb.00075-17;
RA Tanigawa M., Maeda T.;
RT "An In Vitro TORC1 Kinase Assay That Recapitulates the Gtr-Independent
RT Glutamine-Responsive TORC1 Activation Mechanism on Yeast Vacuoles.";
RL Mol. Cell. Biol. 37:e00075-e00075(2017).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH TOR1; KOG1; TCO89;
RP LST8 AND TOR2, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP DOMAIN FYVE-TYPE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-337;
RP ARG-475; CYS-522 AND 621-SER--PHE-635.
RX PubMed=29698392; DOI=10.1371/journal.pgen.1007334;
RA Ukai H., Araki Y., Kira S., Oikawa Y., May A.I., Noda T.;
RT "Gtr/Ego-independent TORC1 activation is achieved through a glutamine-
RT sensitive interaction with Pib2 on the vacuolar membrane.";
RL PLoS Genet. 14:e1007334-e1007334(2018).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32801125; DOI=10.1242/jcs.245555;
RA Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA Ishikawa Y., Izawa S., Abe F.;
RT "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT high hydrostatic pressure.";
RL J. Cell Sci. 133:jcs245555-jcs245555(2020).
RN [12]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH TOR1, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF PRO-337; LEU-340; ARG-341 AND VAL-626.
RX PubMed=34535752; DOI=10.1038/s42003-021-02625-w;
RA Tanigawa M., Yamamoto K., Nagatoishi S., Nagata K., Noshiro D., Noda N.N.,
RA Tsumoto K., Maeda T.;
RT "A glutamine sensor that directly activates TORC1.";
RL Commun. Biol. 4:1093-1093(2021).
CC -!- FUNCTION: Functions as an intracellular glutamine sensor that directly
CC activates the TORC1 signaling pathway, to promote cell growth when
CC glutamine is available (PubMed:34535752, PubMed:29698392,
CC PubMed:28483912, PubMed:26510498, PubMed:32801125). May play a role in
CC repressing NPR1 activity independently of TORC1 signaling (By
CC similarity). {ECO:0000250|UniProtKB:A0A8H4C2S2,
CC ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:28483912,
CC ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:32801125,
CC ECO:0000269|PubMed:34535752}.
CC -!- ACTIVITY REGULATION: Activated by glutamine (PubMed:34535752,
CC PubMed:29698392). May also be activated by cysteine (PubMed:34535752).
CC {ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:34535752}.
CC -!- SUBUNIT: Interacts with the TORC1 complex when activated by glutamine
CC or cysteine (PubMed:34535752, PubMed:29698392, PubMed:28483912).
CC Interacts with TOR1; glutamine enhances the interaction
CC (PubMed:34535752, PubMed:29698392, PubMed:28483912). Interacts with
CC KOG1; glutamine enhances the interaction (PubMed:29698392). Interacts
CC with TCO89 (PubMed:29698392). Interacts with LST8; glutamine enhances
CC the interaction (PubMed:29698392). Interacts with TOR2; glutamine
CC enhances the interaction (PubMed:29698392).
CC {ECO:0000269|PubMed:28483912, ECO:0000269|PubMed:29698392,
CC ECO:0000269|PubMed:34535752}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:29698392}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The FYVE-type zinc finger domain contributes to vacuolar
CC localization. {ECO:0000269|PubMed:26510498,
CC ECO:0000269|PubMed:29698392}.
CC -!- DISRUPTION PHENOTYPE: Abnormal activation of TORC1 signaling in
CC nitrogen-replete conditions (glutamine nitrogen source), and during
CC high hydrostatic pressure (mechanical stress) (PubMed:29698392,
CC PubMed:28483912, PubMed:32801125). Increases cellular levels of
CC glutamine and alanine during high hydrostatic pressure (mechanical
CC stress) (PubMed:32801125). Sensitive to rapamycin (TORC1 signaling-
CC inhibitor), caffeine, and high hydrostatic pressure (mechanical stress)
CC (PubMed:29698392, PubMed:34535752, PubMed:26510498, PubMed:32801125).
CC Resistance to tunicamycin (endoplasmic reticulum stressor) administered
CC together with FK506 (calcineurin inhibitor) (PubMed:26510498).
CC Localization of TORC1 to vacuoles is normal (PubMed:28483912).
CC Simultaneous disruption of GTR1 results in TOR1 mislocalization and
CC loss of TORC1 activity and viability (PubMed:29698392). Simultaneous
CC disruption of EGO1 results in loss of viability (PubMed:29698392).
CC {ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:28483912,
CC ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:32801125,
CC ECO:0000269|PubMed:34535752}.
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DR EMBL; Z72545; CAA96724.1; -; Genomic_DNA.
DR EMBL; Z72544; CAA96723.1; -; Genomic_DNA.
DR EMBL; AY692918; AAT92937.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08075.1; -; Genomic_DNA.
DR PIR; S64025; S64025.
DR RefSeq; NP_011492.3; NM_001180888.3.
DR AlphaFoldDB; P53191; -.
DR SMR; P53191; -.
DR BioGRID; 33223; 315.
DR DIP; DIP-6378N; -.
DR IntAct; P53191; 8.
DR MINT; P53191; -.
DR STRING; 4932.YGL023C; -.
DR iPTMnet; P53191; -.
DR MaxQB; P53191; -.
DR PaxDb; P53191; -.
DR PRIDE; P53191; -.
DR EnsemblFungi; YGL023C_mRNA; YGL023C; YGL023C.
DR GeneID; 852861; -.
DR KEGG; sce:YGL023C; -.
DR SGD; S000002991; PIB2.
DR VEuPathDB; FungiDB:YGL023C; -.
DR eggNOG; KOG1729; Eukaryota.
DR HOGENOM; CLU_020649_0_0_1; -.
DR InParanoid; P53191; -.
DR OMA; RHWLYLD; -.
DR BioCyc; YEAST:G3O-30542-MON; -.
DR PRO; PR:P53191; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53191; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transducer;
KW Vacuole; Zinc; Zinc-finger.
FT CHAIN 1..635
FT /note="Glutamine sensor PIB2"
FT /id="PRO_0000058425"
FT ZN_FING 452..527
FT /note="FYVE-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..164
FT /note="May play a role in attenuating TORC1 signaling"
FT /evidence="ECO:0000250|UniProtKB:A0A8H4C2S2"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..440
FT /note="Required for interaction with TORC1"
FT /evidence="ECO:0000269|PubMed:34535752"
FT REGION 534..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..635
FT /note="May be required for TORC1 activation"
FT /evidence="ECO:0000269|PubMed:34535752"
FT COMPBIAS 10..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 337
FT /note="P->A: Mildly decreases interaction with and
FT activation of TOR1 in response to glutamine. Sensitive to
FT rapamycin."
FT /evidence="ECO:0000269|PubMed:34535752"
FT MUTAGEN 337
FT /note="P->S: Decreases interaction with and activation of
FT TOR1."
FT /evidence="ECO:0000269|PubMed:29698392"
FT MUTAGEN 340
FT /note="L->A: Decreases interaction with and activation of
FT TOR1 in response to glutamine. Sensitive to rapamycin."
FT /evidence="ECO:0000269|PubMed:34535752"
FT MUTAGEN 341
FT /note="R->A: Abolishes interaction with and activation of
FT TOR1 in response to glutamine. Sensitive to rapamycin."
FT /evidence="ECO:0000269|PubMed:34535752"
FT MUTAGEN 475
FT /note="R->A: Decreases localization to the vacuolar
FT membrane and results in rapamycin sensitivity; when
FT associated with S-522."
FT /evidence="ECO:0000269|PubMed:29698392"
FT MUTAGEN 522
FT /note="C->S: Decreases localization to the vacuolar
FT membrane and results in rapamycin sensitivity; when
FT associated with A-475."
FT /evidence="ECO:0000269|PubMed:29698392"
FT MUTAGEN 621..635
FT /note="Missing: Abnormal TORC1 activation in glutamine-
FT replete conditions. Sensitive to caffeine. Resistance to
FT tunicamycin (endoplasmic reticulum stressor) administered
FT together with FK506 (calcineurin inhibitor)."
FT /evidence="ECO:0000269|PubMed:26510498,
FT ECO:0000269|PubMed:29698392"
FT MUTAGEN 626
FT /note="V->A: Increases activity in presence of glutamine."
FT /evidence="ECO:0000269|PubMed:34535752"
FT CONFLICT 152
FT /note="E -> G (in Ref. 3; AAT92937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 635 AA; 70617 MW; 512E9B873E6E0164 CRC64;
MTALHSVSKT PAIKEEEEDG DERDGRGVPL GPRNHDYRGR KGDEESGADT VTSPITFEKK
KIAPRASTHS EQSILSSISL KSMVNQHRQQ QLQQESSTGA GTGFVDRKQQ IQSPAMVSIL
RKNSAEENVR SSHSSKLGEG QIDGRKASAS KEIGKTLPFT DDQRSNPELD PTNSVVDVSR
GKNTKSKTVF NELEDDADDD DEVRQKNLTT QALRKLSSFK MNASSNLRLS KENKAKESSS
SSTSSVSSSS TSKVENIVDK LTTTNSSSMS QLRFGNTNVI IDSVNHAAKP PHQQMLRKPS
LEFLPQPASS TNLNFNSNKH KSNVRQISNP KKPLYIPAVL RKVSETNITN DDLLNATLSS
YYKKASNLEH GFNPSKSQSA SVQNANNLRI ISSQSSVQSN TSSILESYKN KISSYLFPNS
IPNSDRINLI PTISNRNSAR VNPPTKDHWI PDSKRNSCRY CHKPFTLWER KHHCRHCGDI
FCQDHLRHWL YLDSQANFIM INELNNGGIN GGGTLCKICD DCLVEYENLS TTNHNANTNE
DNINVEEGED DDNDNRKKLR NYYKNRQMNA LFRPKKGGSS QEHATVDRDT TTPIQVKSND
EEADNENTGG EQEEGNDVLG SVIGSVPANW NWSSF