KDIS_RAT
ID KDIS_RAT Reviewed; 1762 AA.
AC Q9EQG6; Q9ERD4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Kinase D-interacting substrate of 220 kDa;
DE AltName: Full=Ankyrin repeat-rich membrane-spanning protein;
GN Name=Kidins220; Synonyms=Arms;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PHOSPHORYLATION
RP AT SER-918, MUTAGENESIS OF SER-918, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH PRKD1.
RX PubMed=10998417; DOI=10.1074/jbc.m005261200;
RA Iglesias T., Cabrera-Poch N., Mitchell M.P., Naven T.J.P., Rozengurt E.,
RA Schiavo G.;
RT "Identification and cloning of Kidins220, a novel neuronal substrate of
RT protein kinase D.";
RL J. Biol. Chem. 275:40048-40056(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH NGFR AND
RP NTRK1, PHOSPHORYLATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=11150334; DOI=10.1523/jneurosci.21-01-00176.2001;
RA Kong H., Boulter J., Weber J.L., Lai C., Chao M.V.;
RT "An evolutionarily conserved transmembrane protein that is a novel
RT downstream target of neurotrophin and ephrin receptors.";
RL J. Neurosci. 21:176-185(2001).
RN [3]
RP FUNCTION, PHOSPHORYLATION, DOMAIN, AND INTERACTION WITH NTRK1; NTRK2; NTRK3
RP AND CRKL.
RX PubMed=15167895; DOI=10.1038/sj.emboj.7600253;
RA Arevalo J.C., Yano H., Teng K.K., Chao M.V.;
RT "A unique pathway for sustained neurotrophin signaling through an ankyrin-
RT rich membrane-spanning protein.";
RL EMBO J. 23:2358-2368(2004).
RN [4]
RP INTERACTION WITH NTRK1 AND NGFR.
RX PubMed=15378608; DOI=10.1002/jnr.20262;
RA Chang M.-S., Arevalo J.C., Chao M.V.;
RT "Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning
RT protein.";
RL J. Neurosci. Res. 78:186-192(2004).
RN [5]
RP FUNCTION, INTERACTION WITH SNTA1; SNTB2 AND EPHA4, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, PHOSPHORYLATION, MOTIF, AND MUTAGENESIS OF SER-1760.
RX PubMed=15939763; DOI=10.1083/jcb.200412008;
RA Luo S., Chen Y., Lai K.-O., Arevalo J.C., Froehner S.C., Adams M.E.,
RA Chao M.V., Ip N.Y.;
RT "Alpha-syntrophin regulates ARMS localization at the neuromuscular junction
RT and enhances EphA4 signaling in an ARMS-dependent manner.";
RL J. Cell Biol. 169:813-824(2005).
RN [6]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MAGI2; RAPGEF2 AND NTRK1,
RP INTERACTION WITH RAPGEF2 AND MAGI2, AND SUBCELLULAR LOCATION.
RX PubMed=17724123; DOI=10.1083/jcb.200610073;
RA Hisata S., Sakisaka T., Baba T., Yamada T., Aoki K., Matsuda M., Takai Y.;
RT "Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late endosomes,
RT leading to sustained activation of Rap1 and ERK and neurite outgrowth.";
RL J. Cell Biol. 178:843-860(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918; SER-1513 AND SER-1518,
RP AND 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).
CC -!- FUNCTION: Promotes a prolonged MAP-kinase signaling by neurotrophins
CC through activation of a Rap1-dependent mechanism. Provides a docking
CC site for the CRKL-C3G complex, resulting in Rap1-dependent sustained
CC ERK activation. May play an important role in regulating postsynaptic
CC signal transduction through the syntrophin-mediated localization of
CC receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can
CC enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth
CC factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and
CC neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated
CC neuronal outgrowth and in axon guidance during neural development and
CC in neuronal regeneration. {ECO:0000269|PubMed:11150334,
CC ECO:0000269|PubMed:15167895, ECO:0000269|PubMed:15939763,
CC ECO:0000269|PubMed:17724123}.
CC -!- SUBUNIT: Found in a complex, at least composed of KIDINS220, MAGI2,
CC NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a
CC nerve growth factor (NGF)-dependent manner (PubMed:17724123). Interacts
CC with RAPGEF2; the interaction is strengthened after NGF stimulation
CC (PubMed:17724123). Isoform 2 interacts (via C-terminal domain) with
CC MAGI2 isoform 1 (via PDZ domain) (PubMed:17724123). Interacts with
CC NTRK1, NTRK2, NTRK3, ERKL and NGFR (PubMed:11150334, PubMed:15167895,
CC PubMed:15378608). Can form a ternary complex with NGFR and NTRK1 and
CC this complex is affected by the expression levels of KIDINS220/ARMS
CC (PubMed:15378608). An increase in KIDINS220/ARMS expression leads to a
CC decreased association of NGFR and NTRK1 (PubMed:15378608). Interacts
CC (via PDZ-binding motif) with SNTA1 and SNTB2 (via PDZ domains)
CC (PubMed:15939763). Interacts with EPHA4 and PRKD1 (PubMed:10998417,
CC PubMed:15939763). {ECO:0000269|PubMed:10998417,
CC ECO:0000269|PubMed:11150334, ECO:0000269|PubMed:15167895,
CC ECO:0000269|PubMed:15378608, ECO:0000269|PubMed:15939763,
CC ECO:0000269|PubMed:17724123}.
CC -!- INTERACTION:
CC Q9EQG6; P46109: CRKL; Xeno; NbExp=2; IntAct=EBI-976654, EBI-910;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Late endosome {ECO:0000269|PubMed:10998417,
CC ECO:0000269|PubMed:17724123}. Note=Localized at late endosome before or
CC after nerve growth factor (NGF) stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EQG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQG6-2; Sequence=VSP_031868, VSP_031869;
CC -!- TISSUE SPECIFICITY: Expressed in developing nervous system and in
CC highly plastic areas of the adult brain. Also expressed in
CC neuroendocrine cells, where it concentrates at the tip of neurites.
CC Expressed in developing muscle and is concentrated at the neuromuscular
CC junction (NMS). SNTA1 can regulate its localization in the NMS.
CC {ECO:0000269|PubMed:10998417, ECO:0000269|PubMed:11150334,
CC ECO:0000269|PubMed:15939763}.
CC -!- DEVELOPMENTAL STAGE: Expressed in postmitotic neurons during the stage
CC of development in which extensive axon pathfinding is occurring. At
CC embryonic day 14 (E14), expressed in both spinal cord and dorsal root
CC ganglia. Present on the sarcolemma in postnstal day 1 (P1)
CC gastrocnemius muscle. By P8, becomes more concentrated at the
CC junctional sites and by P21, colocalizes with acetylcholine receptor
CC clusters. {ECO:0000269|PubMed:11150334, ECO:0000269|PubMed:15939763}.
CC -!- DOMAIN: The transmembrane domain mediates interaction with NTRK1.
CC {ECO:0000269|PubMed:15167895}.
CC -!- PTM: Tyrosine phosphorylated by NTRK1, NTRK2, EPHB2 and EPHA4.
CC Phosphorylation at Ser-918 is induced by phorbol ester treatment.
CC Phosphorylation by NTRK2 is induced by brain-derived neurotrophic
CC factor (BDNF) and neurotrophin-4/5. Phosphorylation by NTRK1 is induced
CC by nerve growth factor (NGF). {ECO:0000269|PubMed:10998417,
CC ECO:0000269|PubMed:11150334, ECO:0000269|PubMed:15167895,
CC ECO:0000269|PubMed:15939763}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG34167.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF239045; AAG35185.2; -; mRNA.
DR EMBL; AF313464; AAG34167.1; ALT_FRAME; mRNA.
DR RefSeq; NP_446247.1; NM_053795.1. [Q9EQG6-1]
DR PDB; 7D6F; X-ray; 2.70 A; B=1748-1762.
DR PDBsum; 7D6F; -.
DR AlphaFoldDB; Q9EQG6; -.
DR SMR; Q9EQG6; -.
DR CORUM; Q9EQG6; -.
DR IntAct; Q9EQG6; 5.
DR STRING; 10116.ENSRNOP00000063889; -.
DR iPTMnet; Q9EQG6; -.
DR PhosphoSitePlus; Q9EQG6; -.
DR SwissPalm; Q9EQG6; -.
DR jPOST; Q9EQG6; -.
DR PaxDb; Q9EQG6; -.
DR PRIDE; Q9EQG6; -.
DR GeneID; 116478; -.
DR KEGG; rno:116478; -.
DR CTD; 57498; -.
DR RGD; 619949; Kidins220.
DR eggNOG; KOG0502; Eukaryota.
DR InParanoid; Q9EQG6; -.
DR OrthoDB; 58543at2759; -.
DR PhylomeDB; Q9EQG6; -.
DR Reactome; R-RNO-170984; ARMS-mediated activation.
DR Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:Q9EQG6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:RGD.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011646; KAP_P-loop.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07693; KAP_NTPase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 10.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Endosome; Membrane;
KW Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1762
FT /note="Kinase D-interacting substrate of 220 kDa"
FT /id="PRO_0000322120"
FT TOPO_DOM 1..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..533
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..696
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..1680
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 45..74
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 78..107
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 111..140
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 145..174
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 178..207
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 211..240
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 244..273
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 277..306
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 310..339
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT REPEAT 343..372
FT /note="ANK 10"
FT /evidence="ECO:0000255"
FT REPEAT 376..405
FT /note="ANK 11"
FT /evidence="ECO:0000255"
FT DOMAIN 440..953
FT /note="KAP NTPase"
FT REGION 1089..1092
FT /note="Mediates interaction with CRKL"
FT /evidence="ECO:0000269|PubMed:15167895"
FT REGION 1279..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1757..1762
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:15939763"
FT COMPBIAS 1337..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1705..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 914
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 918
FT /note="Phosphoserine; by PKD"
FT /evidence="ECO:0000269|PubMed:10998417,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1671
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT MOD_RES 1676
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH0"
FT VAR_SEQ 135
FT /note="L -> LQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11150334"
FT /id="VSP_031868"
FT VAR_SEQ 1139..1187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11150334"
FT /id="VSP_031869"
FT MUTAGEN 918
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:10998417"
FT MUTAGEN 1760
FT /note="S->D: Loss of binding to PDZ domain of SNTA1 and
FT SNTB2."
FT /evidence="ECO:0000269|PubMed:15939763"
FT CONFLICT 519
FT /note="T -> P (in Ref. 2; AAG34167)"
FT /evidence="ECO:0000305"
FT CONFLICT 1001
FT /note="I -> M (in Ref. 2; AAG34167)"
FT /evidence="ECO:0000305"
FT CONFLICT 1220
FT /note="S -> N (in Ref. 2; AAG34167)"
FT /evidence="ECO:0000305"
FT STRAND 1758..1761
FT /evidence="ECO:0007829|PDB:7D6F"
SQ SEQUENCE 1762 AA; 195716 MW; 0CB2689A571F8AE4 CRC64;
MSVLISQSVI NYVEEENIPA LKALLEKCKD VDERNECGQT PLMLAAEQGN VEIVKELLKN
GANCNLEDLD NWTALISASK EGHIHIVEEL LKSGASLEHR DMGGWTALMW ACYKGRTDVV
ELLLSHGANP SVTGLYSVYP IIWAAGRGHA DIVHLLLQNG AKVNCSDKYG TTPLVWAARK
GHLECVKHLL AMGADVDQEG ANSMTALIVA VKGGYTQSVK EILKRNPNVN LTDKDGNTAL
MIASKEGHIE IVQDLLDAGT YVNIPDRSGD TVLIGAVRGG HVEIVRALLQ KYADIDIRGQ
DNKTALYWAV EKGNATMVRD ILQCNPDTEI CTKDGETPLI KATKMRNIEV VELLLDKGAK
VSAVDKKGDT PLHVAIRGRS RRLAELLLRN PKDGRLLYRP NKAGETPYNI DCSHQKSILT
QIFGARHLSP TETDGDMLGY DLYSSALADI LSEPTMQPPI CVGLYAQWGS GKSFLLKKLE
DEMKTFAGQQ TEPLFQFSWL IVFLTLLLCG GLGLVFAFTV DTNLAIAISL SFLALIYIFF
IVIYFGGRRE GESWNWAWAL STRLARHIGY LELLFKLMFV NPPELPEQTT KALPVRFLFT
DYNRLSSVGG ETSLAEMIAT LSDACEREFG FLATRLFRVF RTEESQGKKK WKKTCCLPSF
VIFLFIVGCI IAGITLLAIF RVDPKHLTVN AILISIASVV GLAFVLNCRT WWQVLDSLLN
SQRKRLHSAA SKLHKLKSEG FMKVLKCEVE LMARMAKTID SFTQNQTRLV VIIDGLDACE
QDKVLQMLDT VRVLFSKGPF IAIFASDPHI IIKAINQNLN SVLRDSNING HDYMRNIVHL
PVFLNSRGLS NARKFLVTSA TNGDITCSDT TGTQEDTDRR VSQNSLGEMT KLGSKTALNR
RDTYRRRQMQ RTITRQMSFD LTKLLVTEDW FSDISPQTMR RLLNIVSVTG RLLRANQITF
NWDRLASWIN LTEQWPYRTS WLILYLEETE GLPDQMTLKT IYERISKNIP TTKDVEPLLE
IDGDIRNFEV FLSSRTPVLV ARDVKTFLPC TVNLDPKLRE IIADVRAARE QINIGGLAYP
PLPLHEGPPR PPSGYSQPAS VCSSASFNGP FPGGVVSPQP HSSYYSGLSG PQHPFYNRPF
FAPYLYTPRY YPGGSQHLIS RSSVKTSLPR DQNNGLPCDS GFNKQRQAAV PATGSSLLLS
SMTVDVVCEK LRQIEGLDQS MMPQYCTTIK KANINGRVLS QCNIDELKKE MAMNFGDWHL
FRSMVLEMRS VESQVVPEDP RFLNENSSAP VPHGESARRS SHTELPLTEL SSQTPYTLNF
SFEELNTLGL DEGAPRHSNL SWQSQTRRTP SLSSLNSQDS SIEISKLTDK VQAEYRDAYR
EYIAQMSQLE GGTGSSTISG RSSPHSTYYI GQSSSGGSIH STLEQERGKE GELKQEDGRK
SFLMKRGDVI DYSSSGVSTN EASPLDPITE EDEKSDQSGS KLLPGKKSSE RPSLFQTDLK
LKGGGLRYQK LPSDEDESGT EESDNTPLLK DDKDKKAEGK AERVCKSPEH SAEPIRTFIK
AKEYLSDALL DKKDSSDSGV RSNESSPNHS LHNEAADDSQ LEKANLIELE DEGHSGKRGM
PHSLSGLQDP IIARMSICSE DKKSPSECSL IASSPEESWP ACQKAYNLNR TPSTVTLNNN
TAPTNRANQN FDEIEGIRET SQVILRPGPS PNPTAVQNEN LKSMAHKRSQ RSSYTRLSKD
ASELHAASSE STGFGEERES IL
