JIP2_HUMAN
ID JIP2_HUMAN Reviewed; 824 AA.
AC Q13387; Q96G62; Q99771; Q9NZ59; Q9UKQ4;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 2;
DE Short=JIP-2;
DE Short=JNK-interacting protein 2;
DE AltName: Full=Islet-brain-2;
DE Short=IB-2;
DE AltName: Full=JNK MAP kinase scaffold protein 2;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 2;
GN Name=MAPK8IP2; Synonyms=IB2, JIP2, PRKM8IPL;
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] (ISOFORM 1), INTERACTION WITH JNK1; JNK2; JNK3;
RP MAP2K7; MAP3K10; MAP3K11 AND MAP3K12, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=10490659; DOI=10.1128/mcb.19.10.7245;
RA Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.;
RT "The JIP group of mitogen-activated protein kinase scaffold proteins.";
RL Mol. Cell. Biol. 19:7245-7254(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain, and Insulinoma;
RX PubMed=10756100; DOI=10.1006/geno.2000.6129;
RA Negri S., Oberson A., Steinmann M., Sauser C., Nicod P., Waeber G.,
RA Schorderet D.F., Bonny C.;
RT "cDNA cloning and mapping of a novel islet-brain/JNK interacting protein.";
RL Genomics 64:324-330(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RA Adams M.D.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-824.
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 599-824 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [8]
RP INTERACTION WITH FGF13 AND MAPK13.
RX PubMed=11378392; DOI=10.1016/s0960-9822(01)00232-9;
RA Schoorlemmer J., Goldfarb M.;
RT "Fibroblast growth factor homologous factors are intracellular signaling
RT proteins.";
RL Curr. Biol. 11:793-797(2001).
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. JIP2
CC inhibits IL1 beta-induced apoptosis in insulin-secreting cells. May
CC function as a regulator of vesicle transport, through interactions with
CC the JNK-signaling components and motor proteins (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms homo- or heterooligomeric complexes. Binds specific
CC components of the JNK signaling pathway namely JNK1, JNK2, JNK3,
CC MAP2K7, MAP3K10, MAP3K11, MAP3K12 and MAPK13. Also binds the proline-
CC rich domain-containing splice variant of apolipoprotein E receptor 2
CC (ApoER2). Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds
CC the TPR motif-containing C-terminal of kinesin light chain, Klc1, pre-
CC assembled MAPK8IP1 scaffolding complexes are then transported as a
CC cargo of kinesin, to the required subcellular location (By similarity).
CC Interacts with the cytoplasmic domain of APP (By similarity). Interacts
CC with DCLK2. Interacts with TIAM1 and TIAM2 (By similarity). Interacts
CC with FGF13; enables the interaction with MAPK13 and may regulate the
CC MAPK8IP2 scaffolding activity. Interacts with SH3RF2 (By similarity).
CC {ECO:0000250|UniProtKB:G3V9M2, ECO:0000250|UniProtKB:Q9ERE9,
CC ECO:0000269|PubMed:10490659, ECO:0000269|PubMed:11378392}.
CC -!- INTERACTION:
CC Q13387; Q15389-2: ANGPT1; NbExp=3; IntAct=EBI-722813, EBI-10692491;
CC Q13387; P00533: EGFR; NbExp=5; IntAct=EBI-722813, EBI-297353;
CC Q13387; P04626: ERBB2; NbExp=3; IntAct=EBI-722813, EBI-641062;
CC Q13387; O15205: UBD; NbExp=3; IntAct=EBI-722813, EBI-6657186;
CC Q13387; Q53HF2; NbExp=2; IntAct=EBI-722813, EBI-877761;
CC Q13387-4; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-12345753, EBI-1383687;
CC Q13387-4; P29466-3: CASP1; NbExp=3; IntAct=EBI-12345753, EBI-12248206;
CC Q13387-4; P14136: GFAP; NbExp=3; IntAct=EBI-12345753, EBI-744302;
CC Q13387-4; P31273: HOXC8; NbExp=3; IntAct=EBI-12345753, EBI-1752118;
CC Q13387-4; P05556: ITGB1; NbExp=3; IntAct=EBI-12345753, EBI-703066;
CC Q13387-4; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-12345753, EBI-9090282;
CC Q13387-4; P17612: PRKACA; NbExp=3; IntAct=EBI-12345753, EBI-476586;
CC Q13387-4; P63000: RAC1; NbExp=3; IntAct=EBI-12345753, EBI-413628;
CC Q13387-4; P34741: SDC2; NbExp=3; IntAct=EBI-12345753, EBI-1172957;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10490659}.
CC Note=Accumulates in cell surface projections.
CC {ECO:0000269|PubMed:10490659}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q13387-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13387-2; Sequence=VSP_002770;
CC Name=3;
CC IsoId=Q13387-3; Sequence=VSP_002770, VSP_002772, VSP_002773,
CC VSP_002774;
CC Name=4;
CC IsoId=Q13387-4; Sequence=VSP_002771;
CC -!- TISSUE SPECIFICITY: Expressed mainly in the brain and pancreas,
CC including insulin-secreting cells. In the nervous system, more
CC abundantly expressed in the cerebellum, pituitary gland, occipital lobe
CC and the amygdala. Also expressed in fetal brain. Very low levels found
CC in uterus, ovary, prostate, colon, testis, adrenal gland, thyroid gland
CC and salivary gland.
CC -!- MISCELLANEOUS: [Isoform 3]: Might be artifactual as it is only
CC predicted from a genomic sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16714.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF136382; AAF00980.1; -; mRNA.
DR EMBL; AF218778; AAF32323.1; -; mRNA.
DR EMBL; U62317; AAB03340.1; -; Genomic_DNA.
DR EMBL; BC009940; AAH09940.2; -; mRNA.
DR EMBL; AL021708; CAA16714.1; ALT_INIT; mRNA.
DR EMBL; U79261; AAB50207.1; -; mRNA.
DR CCDS; CCDS74886.1; -. [Q13387-1]
DR RefSeq; NP_036456.1; NM_012324.4. [Q13387-1]
DR AlphaFoldDB; Q13387; -.
DR SMR; Q13387; -.
DR BioGRID; 117086; 109.
DR CORUM; Q13387; -.
DR IntAct; Q13387; 84.
DR MINT; Q13387; -.
DR STRING; 9606.ENSP00000330572; -.
DR MoonDB; Q13387; Predicted.
DR iPTMnet; Q13387; -.
DR PhosphoSitePlus; Q13387; -.
DR BioMuta; MAPK8IP2; -.
DR DMDM; 17433017; -.
DR MassIVE; Q13387; -.
DR PaxDb; Q13387; -.
DR PeptideAtlas; Q13387; -.
DR PRIDE; Q13387; -.
DR ProteomicsDB; 59356; -. [Q13387-1]
DR ProteomicsDB; 59357; -. [Q13387-2]
DR ProteomicsDB; 59358; -. [Q13387-3]
DR ProteomicsDB; 59359; -. [Q13387-4]
DR Antibodypedia; 28835; 254 antibodies from 28 providers.
DR DNASU; 23542; -.
DR Ensembl; ENST00000329492.6; ENSP00000330572.4; ENSG00000008735.14. [Q13387-1]
DR GeneID; 23542; -.
DR KEGG; hsa:23542; -.
DR MANE-Select; ENST00000329492.6; ENSP00000330572.4; NM_012324.6; NP_036456.1.
DR UCSC; uc032qrw.2; human. [Q13387-1]
DR CTD; 23542; -.
DR DisGeNET; 23542; -.
DR GeneCards; MAPK8IP2; -.
DR HGNC; HGNC:6883; MAPK8IP2.
DR HPA; ENSG00000008735; Group enriched (brain, pituitary gland).
DR MIM; 607755; gene.
DR neXtProt; NX_Q13387; -.
DR OpenTargets; ENSG00000008735; -.
DR PharmGKB; PA30627; -.
DR VEuPathDB; HostDB:ENSG00000008735; -.
DR eggNOG; KOG3775; Eukaryota.
DR GeneTree; ENSGT00940000160461; -.
DR HOGENOM; CLU_006711_0_0_1; -.
DR InParanoid; Q13387; -.
DR OMA; HLAFACP; -.
DR OrthoDB; 372907at2759; -.
DR PhylomeDB; Q13387; -.
DR PathwayCommons; Q13387; -.
DR SignaLink; Q13387; -.
DR SIGNOR; Q13387; -.
DR BioGRID-ORCS; 23542; 8 hits in 289 CRISPR screens.
DR ChiTaRS; MAPK8IP2; human.
DR GeneWiki; MAPK8IP2; -.
DR GenomeRNAi; 23542; -.
DR Pharos; Q13387; Tbio.
DR PRO; PR:Q13387; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q13387; protein.
DR Bgee; ENSG00000008735; Expressed in Brodmann (1909) area 10 and 162 other tissues.
DR Genevisible; Q13387; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; ISS:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; NAS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISS:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0001662; P:behavioral fear response; ISS:BHF-UCL.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IDA:MGI.
DR GO; GO:0007617; P:mating behavior; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0046958; P:nonassociative learning; ISS:BHF-UCL.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IEA:Ensembl.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:BHF-UCL.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISS:BHF-UCL.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:0007172; P:signal complex assembly; TAS:ProtInc.
DR GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
DR CDD; cd11942; SH3_JIP2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035637; JIP2_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00326; SH3; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..824
FT /note="C-Jun-amino-terminal kinase-interacting protein 2"
FT /id="PRO_0000220631"
FT DOMAIN 604..665
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 677..813
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..275
FT /note="JNK-binding domain (JBD)"
FT REGION 172..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..498
FT /note="Necessary for interaction with FGF13"
FT /evidence="ECO:0000269|PubMed:11378392"
FT REGION 361..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..434
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..484
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE9"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE9"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE9"
FT VAR_SEQ 1..57
FT /note="MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDS
FT DHCEK -> MLPDFPSPSTWAPGLLLPSGPALLSPSVLQ (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10756100"
FT /id="VSP_002770"
FT VAR_SEQ 88..468
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_002771"
FT VAR_SEQ 152..394
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002772"
FT VAR_SEQ 415..439
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002773"
FT VAR_SEQ 768
FT /note="C -> CEAPQGAAFQWERGVDRKRVLQTRGNVQPHLGAGQGAALNRATEGSS
FT TGSEKGEWTPLVIMELTQSVNSC (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002774"
FT VARIANT 743
FT /note="P -> L (in dbSNP:rs1140555)"
FT /id="VAR_049666"
SQ SEQUENCE 824 AA; 87975 MW; 7EFC8F3BC58E37BB CRC64;
MADRAEMFSL STFHSLSPPG CRPPQDISLE EFDDEDLSEI TDDCGLGLSY DSDHCEKDSL
SLGRSEQPHP ICSFQDDFQE FEMIDDNEEE DDEDEEEEEE EEEGDGEGQE GGDPGSEAPA
PGPLIPSPSV EEPHKHRPTT LRLTTLGAQD SLNNNGGFDL VRPASWQETA LCSPAPEALR
ELPGPLPATD TGPGGAQSPV RPGCDCEGNR PAEPPAPGGT SPSSDPGIEA DLRSRSSGGR
GGRRSSQELS SPGSDSEDAG GARLGRMISS ISETELELSS DGGSSSSGRS SHLTNSIEEA
SSPASEPEPP REPPRRPAFL PVGPDDTNSE YESGSESEPD LSEDADSPWL LSNLVSRMIS
EGSSPIRCPG QCLSPAPRPP GEPVSPAGGA AQDSQDPEAA AGPGGVELVD METLCAPPPP
APAAPRPGPA QPGPCLFLSN PTRDTITPLW AAPGRAARPG RACSAACSEE EDEEDDEEEE
DAEDSAGSPG GRGTGPSAPR DASLVYDAVK YTLVVDEHTQ LELVSLRRCA GLGHDSEEDS
GGEASEEEAG AALLGGGQVS GDTSPDSPDL TFSKKFLNVF VNSTSRSSST ESFGLFSCLV
NGEEREQTHR AVFRFIPRHP DELELDVDDP VLVEAEEDDF WFRGFNMRTG ERGVFPAFYA
HAVPGPAKDL LGSKRSPCWV ERFDVQFLGS VEVPCHQGNG ILCAAMQKIA TARKLTVHLR
PPASCDLEIS LRGVKLSLSG GGPEFQRCSH FFQMKNISFC GCHPRNSCYF GFITKHPLLS
RFACHVFVSQ ESMRPVAQSV GRAFLEYYQE HLAYACPTED IYLE
