JIP3_RAT
ID JIP3_RAT Reviewed; 1322 AA.
AC E9PSK7; B0VXR4;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 3;
DE Short=JIP-3;
DE Short=JNK-interacting protein 3;
DE AltName: Full=JNK MAP kinase scaffold protein 3;
GN Name=Mapk8ip3; Synonyms=Jip3;
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], FUNCTION, AND INTERACTION WITH MAPK10.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=21076496; DOI=10.1139/y10-088;
RA Xu B., Zhou Y., Karmin O., Choy P.C., Pierce G.N., Siow Y.L.;
RT "Regulation of stress-associated scaffold proteins JIP1 and JIP3 on the c-
RT Jun NH2-terminal kinase in ischemia-reperfusion.";
RL Can. J. Physiol. Pharmacol. 88:1084-1092(2010).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NTRK2 AND KLC1.
RX PubMed=21775604; DOI=10.1523/jneurosci.0436-11.2011;
RA Huang S.H., Duan S., Sun T., Wang J., Zhao L., Geng Z., Yan J., Sun H.J.,
RA Chen Z.Y.;
RT "JIP3 mediates TrkB axonal anterograde transport and enhances BDNF
RT signaling by directly bridging TrkB with kinesin-1.";
RL J. Neurosci. 31:10602-10614(2011).
RN [4]
RP INTERACTION WITH SH3RF2.
RX PubMed=22128169; DOI=10.1074/jbc.m111.269431;
RA Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A., Gire S.,
RA Maes M.E., Xu Z., Greene L.A.;
RT "Sh3rf2/POSHER protein promotes cell survival by RING-mediated proteasomal
RT degradation of the c-Jun N-terminal kinase scaffold POSH (Plenty of SH3s)
RT protein.";
RL J. Biol. Chem. 287:2247-2256(2012).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23576431; DOI=10.1074/jbc.m113.464453;
RA Sun T., Yu N., Zhai L.K., Li N., Zhang C., Zhou L., Huang Z., Jiang X.Y.,
RA Shen Y., Chen Z.Y.;
RT "c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3) regulates
RT neuronal axon elongation in a kinesin- and JNK-dependent manner.";
RL J. Biol. Chem. 288:14531-14543(2013).
RN [7]
RP FUNCTION.
RX PubMed=25944905; DOI=10.1074/jbc.m115.651885;
RA Watt D., Dixit R., Cavalli V.;
RT "JIP3 activates kinesin-1 motility to promote axon elongation.";
RL J. Biol. Chem. 290:15512-15525(2015).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins
CC selectively mediates JNK signaling by aggregating specific components
CC of the MAPK cascade to form a functional JNK signaling module. May
CC function as a regulator of vesicle transport, through interactions with
CC the JNK-signaling components and motor proteins (By similarity).
CC Promotes neuronal axon elongation in a kinesin- and JNK-dependent
CC manner. Activates cofilin at axon tips via local activation of JNK,
CC thereby regulating filopodial dynamics and enhancing axon elongation.
CC Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility
CC along microtubules and is essential for axon elongation and
CC regeneration. Regulates cortical neuronal migration by mediating
CC NTRK2/TRKB anterograde axonal transport during brain development. Acts
CC as an adapter that bridges the interaction between NTRK2/TRKB and KLC1
CC and drives NTRK2/TRKB axonal but not dendritic anterograde transport,
CC which is essential for subsequent BDNF-triggered signaling and
CC filopodia formation. {ECO:0000250|UniProtKB:Q9ESN9,
CC ECO:0000269|PubMed:21076496, ECO:0000269|PubMed:21775604,
CC ECO:0000269|PubMed:23576431, ECO:0000269|PubMed:25944905}.
CC -!- SUBUNIT: Forms homo- or heterooligomeric complexes. The central region
CC of MAPK8IP3 interacts with the C-terminal of MAPK8IP2 but not MAPK8IP1.
CC Binds specific components of the JNK signaling pathway namely
CC MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 to the N-terminal region,
CC MAP2K4/MKK4 and MAP2K7/MKK7 to the central region and MAP3K11 to the C-
CC terminal region. Binds the TPR motif-containing C-terminal of kinesin
CC light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding complexes are
CC then transported as a cargo of kinesin, to the required subcellular
CC location. Interacts with ROCK1 and this interaction is enhanced by
CC ultraviolet-B (UVB) radiation (By similarity). Interacts with SH3RF2
CC (PubMed:22128169). Interacts with NTRK3/TRKC (By similarity). Interacts
CC with NTRK2/TRKB (PubMed:21775604). {ECO:0000250|UniProtKB:Q9ESN9,
CC ECO:0000250|UniProtKB:Q9UPT6, ECO:0000269|PubMed:21076496,
CC ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:22128169}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN9}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q9ESN9}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, axon
CC {ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:23576431}. Cell
CC projection, dendrite {ECO:0000269|PubMed:21775604}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:21775604}. Note=Localized in the
CC soma and growth cones of differentiated neurites and the Golgi and
CC vesicles of the early secretory compartment of epithelial cells.
CC KIF5A/B/C-mediated transportation to axon tips is essential for its
CC function in enhancing neuronal axon elongation.
CC {ECO:0000250|UniProtKB:Q9ESN9, ECO:0000269|PubMed:23576431}.
CC -!- PTM: Phosphorylation by ROCK1 is crucial for the recruitment of JNK.
CC {ECO:0000250|UniProtKB:Q9UPT6}.
CC -!- SIMILARITY: Belongs to the JIP scaffold 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; DQ377222; ABD24061.1; -; mRNA.
DR EMBL; AC130925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001094143.1; NM_001100673.1.
DR AlphaFoldDB; E9PSK7; -.
DR SMR; E9PSK7; -.
DR STRING; 10116.ENSRNOP00000039682; -.
DR PaxDb; E9PSK7; -.
DR PeptideAtlas; E9PSK7; -.
DR PRIDE; E9PSK7; -.
DR GeneID; 302983; -.
DR KEGG; rno:302983; -.
DR CTD; 23162; -.
DR RGD; 1563691; Mapk8ip3.
DR VEuPathDB; HostDB:ENSRNOG00000033568; -.
DR eggNOG; KOG2077; Eukaryota.
DR HOGENOM; CLU_003841_0_0_1; -.
DR InParanoid; E9PSK7; -.
DR OMA; YCSVNIH; -.
DR OrthoDB; 324912at2759; -.
DR PRO; PR:E9PSK7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000033568; Expressed in frontal cortex and 20 other tissues.
DR GO; GO:0030673; C:axolemma; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:RGD.
DR GO; GO:0008432; F:JUN kinase binding; ISO:RGD.
DR GO; GO:0019894; F:kinesin binding; ISS:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISO:RGD.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:RGD.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0099641; P:anterograde axonal protein transport; IMP:UniProtKB.
DR GO; GO:0061564; P:axon development; IMP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0031103; P:axon regeneration; IMP:UniProtKB.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007254; P:JNK cascade; ISO:RGD.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IEP:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0046328; P:regulation of JNK cascade; ISO:RGD.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR039911; JIP3/JIP4.
DR InterPro; IPR032486; JIP_LZII.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13886; PTHR13886; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1322
FT /note="C-Jun-amino-terminal kinase-interacting protein 3"
FT /id="PRO_0000444893"
FT DOMAIN 12..100
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 506..580
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 50..80
FT /note="Kinesin-binding domain (KBD); essential for its
FT function in axon elongation"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN9"
FT REGION 183..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..226
FT /note="JNK-binding domain (JBD); essential for its function
FT in axon elongation"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN9"
FT REGION 245..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..459
FT /note="Leucine zipper-like domain (LZ); essential for its
FT function in axon elongation"
FT /evidence="ECO:0000269|PubMed:21775604"
FT REGION 459..515
FT /note="Interaction with NTRK2"
FT /evidence="ECO:0000269|PubMed:21775604"
FT REGION 704..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..167
FT /evidence="ECO:0000255"
FT COILED 443..534
FT /evidence="ECO:0000255"
FT COMPBIAS 245..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN9"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN9"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN9"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPT6"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPT6"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN9"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN9"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN9"
FT CONFLICT 440
FT /note="I -> V (in Ref. 1; ABD24061)"
FT /evidence="ECO:0000305"
FT CONFLICT 940
FT /note="V -> M (in Ref. 1; ABD24061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1208
FT /note="Y -> N (in Ref. 1; ABD24061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1322 AA; 145650 MW; 01C4DAF1DFEDAA35 CRC64;
MMEIQMDEGG GVVVYQDDYC SGSVMSERVS GLAGSIYREF ERLIHCYDEE VVKELMPLVV
NVLENLDSVL SENQEHEVEL ELLREDNEQL LTQYEREKAL RKQAEEKFIE FEDALEQEKK
ELQIQVEHYE FQTRQLELKA KNYADQISRL EERESEMKKE YNALHQRHTE MIQTYVEHIE
RSKMQQVGGG GQTESSLPGR SRKERPTSLN VFPLADGMVR AQMGGKLVPA GDHWHLSDLG
QLQSSSSYQC PNDEMSESGQ SSAAATPSTT GTKSNTPTSS VPSAAVTPLN ESLQPLGDYG
SVTKNNKRAR EKRNSRNMEV QVTQEMRNVS IGMGSSDEWS DVQDIIDSTP ELDVCPETRL
DRTGSSPTQG IVNKAFGINT DSLYHELSTA GSEVIGDVDE GADLLGEFSG MGKEVGNLLL
ENSQLLETKN ALNVVKNDLI AKVDQLSGEQ EVLKGELEAA KQAKVKLENR IKELEEELKR
VKSEAVTARR EPREEVEDDK IPMAQRRRFT RVEMARVLME RNQYKERLME LQEAVRWTEM
IRASREHPSV QEKKKSTIWQ FFSRLFSSSS SPPPAKRSYP SVNIHYKSPT TAGFSQRRNH
ALCQISAGSR PLEFFPDDDC TSSARREQKR EQYRQVREHV RNDDGRLQAC GWSLPAKYKQ
LSPNGGQEDT RMKNVPVPVY CRPLVEKDPS TKLWCAAGVN LSGWKPNEED SSNGPKPAPG
RDPLTCDREG EGEPKSTHPS PEKKKAKEVP EADATSSRVW ILTSTLTTSK VVIIDANQPG
TVVDQFTVCN AHVLCISSIP AASDSDYPPG DMFLDSDVNP EDSGADGVLA GITLVGCATR
CNVPRSNCSS RGDTPVLDKG QGDVAATANG KVNPSQSTEE ATEATEVPDP GPSESEATTV
RPGPLTEHVF TDPAPTQSSS TQPASENGSE SDGSIVQPQV EPSGESSATT SSAAPTMWLG
AQNGWLYVHS AVANWKKCLH SIKLKDSVLS LVHVKGRVLV ALADGTLAIF HRGEDGQWDL
SNYHLMDLGH PHHSIRCMAV VDDRVWCGYK NKVHVIQPKT MQIEKSFDAH PRRESQVRQL
AWIGDGVWVS IRLDSTLRLY HAHTHQHLQD VDIEPYVSKM LGTGKLGFSF VRITALLIAG
NRLWVGTGNG VVISIPLTET VVLHRGQLLG LRANKTSPTS GEGTRPGGII HVYGDDSSDK
TASSFIPYCS MAQAQLCFHG HRDAVKFFVS VPGNVLATLN GSVLDSPSEG PGPAAPAADA
EGQKLKNALV LSGGEGYIDF RIGDGEDDET EEGTGDVNQT KPSLSKAERS HIIVWQVSYT
PE
