SYNP2_RAT
ID SYNP2_RAT Reviewed; 1262 AA.
AC D4A702;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Synaptopodin-2;
DE AltName: Full=Myopodin;
GN Name=Synpo2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11673475; DOI=10.1083/jcb.200012039;
RA Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., Mundel P.;
RT "Differentiation and stress-dependent nuclear-cytoplasmic redistribution of
RT myopodin, a novel actin bundling protein.";
RL J. Cell Biol. 155:393-404(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-323; SER-324;
RP THR-327; SER-518; SER-543; SER-544; SER-546; SER-606; SER-621; SER-700;
RP THR-749; SER-772; SER-900; SER-904; SER-908; SER-1014 AND SER-1090, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION, ASSOCIATION WITH THE CASA COMPLEX, AND ALTERNATIVE SPLICING.
RX PubMed=23434281; DOI=10.1016/j.cub.2013.01.064;
RA Ulbricht A., Eppler F.J., Tapia V.E., van der Ven P.F., Hampe N.,
RA Hersch N., Vakeel P., Stadel D., Haas A., Saftig P., Behrends C.,
RA Fuerst D.O., Volkmer R., Hoffmann B., Kolanus W., Hoehfeld J.;
RT "Cellular mechanotransduction relies on tension-induced and chaperone-
RT assisted autophagy.";
RL Curr. Biol. 23:430-435(2013).
CC -!- FUNCTION: Has an actin-binding and actin-bundling activity. Can induce
CC the formation of F-actin networks. At the sarcomeric Z lines is
CC proposed to act as adapter protein that links nascent myofibers to the
CC sarcolemma via ZYX and may play a role in early assembly and
CC stabilization of the Z lines (By similarity). Involved in autophagosome
CC formation. May play a role in chaperone-assisted selective autophagy
CC (CASA) involved in Z lines maintenance in striated muscle under
CC mechanical tension; may link the client-processing CASA chaperone
CC machinery to a membrane-tethering and fusion complex providing
CC autophagosome membranes (PubMed:23434281). Involved in regulation of
CC cell migration. May be a tumor suppressor (By similarity).
CC {ECO:0000250|UniProtKB:Q91YE8, ECO:0000250|UniProtKB:Q9UMS6,
CC ECO:0000269|PubMed:23434281}.
CC -!- SUBUNIT: May self-associate in muscle cells under oxidative stress.
CC Binds F-actin. Interacts with ACTN2; ACTN2 is proposed to anchor SYOP2
CC at Z lines in mature myocytes. Interacts with AKAP6, PPP3CA and CAMK2A.
CC Interacts (phosphorylated form) with YWHAB; YWHAB competes with ACTN2
CC for interaction with SYNPO2. Interacts with KPNA2; mediating nuclear
CC import of SYNOP2; dependent on interaction with YWHAB. Interacts with
CC IPO13; may be implicated in SYNOP2 nuclear import. Interacts with ZYX,
CC FLNC, ILK (By similarity). Interacts with BAG3 (via WW 1 domain) (By
CC similarity). May associate with the CASA complex consisting of HSPA8,
CC HSPB8 and BAG3 (PubMed:23434281). Interacts with VPS18 (By similarity).
CC {ECO:0000250|UniProtKB:Q91YE8, ECO:0000250|UniProtKB:Q9UMS6,
CC ECO:0000305|PubMed:23434281}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UMS6}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:11673475}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q9UMS6}. Note=Shuttles between the nucleus and
CC the cytoplasm in a differentiation-dependent and stress-induced
CC fashion. In undifferentiated myoblasts strongly expressed in the
CC nucleus, after induction of myotube differentiation is located to both
CC nucleus and cytoplasm along acting filaments, and in differentiated
CC myotubes is located at the Z lines. Upon stress redistributes from
CC cytoplasm of myoblasts and myotubes to the nucleus. Nuclear import is
CC KPNA2-dependent and promoted by phosphorylation by PKA and/or CaMK2,
CC and inhibition of calcineurin. The nuclear export is XPO1-dependent.
CC Localized in a fiber-like pattern, partly overlapping with filamentous
CC actin (By similarity). {ECO:0000250|UniProtKB:Q91YE8,
CC ECO:0000250|UniProtKB:Q9UMS6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment==Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=D4A702-1; Sequence=Displayed;
CC -!- DOMAIN: The PPPY motif interacts with the WW domain 1 of BAG3.
CC {ECO:0000250|UniProtKB:Q9UMS6}.
CC -!- PTM: Phosphorylated by PKA, and by CaMK2 at multiple sites.
CC Dephosphorylated by calcineurin at Ser-558 and Thr-605; abrogating
CC interaction with YWHAB and impairing nuclear import.
CC {ECO:0000250|UniProtKB:Q91YE8}.
CC -!- SIMILARITY: Belongs to the synaptopodin family. {ECO:0000305}.
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DR EMBL; AABR07013204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07013205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001178892.1; NM_001191963.1. [D4A702-1]
DR AlphaFoldDB; D4A702; -.
DR SMR; D4A702; -.
DR IntAct; D4A702; 1.
DR STRING; 10116.ENSRNOP00000019931; -.
DR iPTMnet; D4A702; -.
DR PaxDb; D4A702; -.
DR PeptideAtlas; D4A702; -.
DR PRIDE; D4A702; -.
DR GeneID; 499702; -.
DR KEGG; rno:499702; -.
DR UCSC; RGD:1564779; rat. [D4A702-1]
DR CTD; 171024; -.
DR RGD; 1564779; Synpo2.
DR VEuPathDB; HostDB:ENSRNOG00000014867; -.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_007120_0_0_1; -.
DR InParanoid; D4A702; -.
DR OMA; LDCSDRE; -.
DR OrthoDB; 109454at2759; -.
DR TreeFam; TF330867; -.
DR PRO; PR:D4A702; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014867; Expressed in skeletal muscle tissue and 18 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:RGD.
DR GO; GO:0031005; F:filamin binding; ISO:RGD.
DR GO; GO:0051371; F:muscle alpha-actinin binding; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:ARUK-UCL.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0061684; P:chaperone-mediated autophagy; IMP:ARUK-UCL.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1262
FT /note="Synaptopodin-2"
FT /id="PRO_0000439584"
FT DOMAIN 6..88
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..174
FT /note="Interaction with VPS18"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 89..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..658
FT /note="Interaction with ACTN2"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 503..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..658
FT /note="F-actin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 554..560
FT /note="Interaction with YWHAB"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT REGION 592..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..809
FT /note="Interaction with YWHAB"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT REGION 610..621
FT /note="Interaction with BAG3"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 659..922
FT /note="Interaction with ACTN2"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 659..914
FT /note="F-actin bundling activity"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 659..801
FT /note="F-actin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 741..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..898
FT /note="Actin binding"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT REGION 808..1153
FT /note="Interaction with FLNC"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 833..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..1153
FT /note="Interaction with ACTN2"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 933..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1018
FT /note="Interaction with ZYX"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT MOTIF 392..400
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOTIF 614..617
FT /note="PPPY motif"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT COMPBIAS 242..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 558
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 605
FT /note="Phosphothreonine; by PKA and CaMK2"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 617
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT MOD_RES 749
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YE8"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1262 AA; 136025 MW; 874C4D6928803FCD CRC64;
MGTGDFICIS MTGGAPWGFR LQGGKEEKQP LQVAKIRSQS KASDSGLCVG DEVVSINGNP
CADLTYPEVI KLMESITDSL HLLIKRPTSG TSEALDSETE NTNHQHLPHG GPMESTTLQI
QHAAKTQGKD FLLASVQTSA PRTEDQGNAW GYAECTTEDQ VSQMPGSQEG HLVEEVILRK
KPEAGQPGHV VELQLSLSKE RQRCTSDPIV TLLGNEKFKS PDPDWGTQHG RTVHINSIPA
PEKADTSLTS GTTVQTSSGR ELTVIQGRDP GGTGLPQVEV ILDCSDRLKA EECRLQAGRG
CVASPVEGGR SEAPPSLVSF AVSSEGTEQG EDQRSGKDQG RPHKHRARHA RLRRSESLSE
KQVKEAKSKC KSIALLLTDA PNPNSKGVLM FKKRRRRARK YTLVSYGTGE LEREEEEEDQ
EAGDKDEISD LAFLGTSESE VDEELLSDVD DNTQVVNFDW DSGLVDIEKR LNRGDKMEML
PDTTGKGALM FAKRRERMEQ FTAQNEEEKT GGLAGGGSDA LQTDGLRTMT SYQRKEESVR
MQSSVSESSF QMGRSLGSVP QQNGFSGVSE TAGPQRMIPM NRTAKPFLGS VNQTAAPFSP
TQSVTSPIPD FPAPPPYSAV SPPPEAFSRG ISSPVAGPAQ PPPWPQPAPW SQPAFYDSSE
QIASRDERIA VPAKRTGILQ EAKRRGTTKP MFTFKETKVS PNPELLSLLQ NAEGKRGTGA
GGDSGPEEDY LSLGAEACNF MQSSAKQKTP PPVAPKPAVK TSSSSQPVAP VSPVWSPGVA
PAQGPAFSTT NPPNPPQVTA VSSIKIAQPT CPPARPASAL NLAGPFKGPQ AAVVSHNYTP
KPSAPTPLVN AAPAGAGGPS NELPGMSGKG AQLFAKRQSR MEKYVVDSDT VQAHTVRAQS
PTPSLPASWK YSSNVRAPPP VAYNPIHSPS YPLAAIKSQP PGAQASKTSK KKGKKPLNTL
DVMKHQPYQL NASLFTFQPP DSKDGLPQKS TVKVSSVAPA MKQALPPRQA DIGSPTNAKA
SSVYSVPAYT SQPNFFAEAT SPVSASPVPV SVPTSPKQET TSTSYFVAPR PKFSAKKSGV
TVQENWRSLS LPGRAAPPIM SAPPWLCQPA YSYSSKPTLE QEKANKRPTP WEAAAKSPLG
LVDEAFRPRN IEESIVANVV SAARRKVFAG SQEDWKERLS FVPQTQKTSM SFSERREYNV
PSPVNSHVSS HSLYSSQLPY VCYRKESRND LKAMSMDTRS EYCLPLGGYD YNPHPRGWRH
QP
