JIP1_RAT
ID JIP1_RAT Reviewed; 708 AA.
AC Q9R237; B0VXR5; O88979; Q9R1H8; Q9WVI5; Q9WVI6;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 1;
DE Short=JIP-1;
DE Short=JNK-interacting protein 1;
DE AltName: Full=Islet-brain-1;
DE Short=IB-1;
DE AltName: Full=JIP-1-related protein;
DE Short=JRP;
DE AltName: Full=JNK MAP kinase scaffold protein 1;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 1;
GN Name=Mapk8ip1; Synonyms=Ib1, Jip1, Mapk8ip;
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).
RC TISSUE=Pancreas;
RX PubMed=9442013; DOI=10.1074/jbc.273.4.1843;
RA Bonny C., Nicod P., Waeber G.;
RT "IB1, a JIP-1-related nuclear protein present in insulin-secreting cells.";
RL J. Biol. Chem. 273:1843-1846(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=Fischer; TISSUE=Fibroblast;
RA Chen Y., Talmage D.;
RT "JIP-1 related protein (JRP).";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10098834; DOI=10.1046/j.1471-4159.1999.721335.x;
RA Kim I.-J., Lee K.-W., Park B.Y., Lee J.-K., Park J., Choi I.Y., Eom S.-J.,
RA Chang T.-S., Kim M.J., Yeom Y.I., Chang S.K., Lee Y.-D., Choi E.-J.,
RA Han P.-L.;
RT "Molecular cloning of multiple splicing variants of JIP-1 preferentially
RT expressed in brain.";
RL J. Neurochem. 72:1335-1343(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-28, 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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 487-546, SH3 DOMAIN, AND SUBUNIT.
RX PubMed=16456539; DOI=10.1038/sj.emboj.7600982;
RA Kristensen O., Guenat S., Dar I., Allaman-Pillet N., Abderrahmani A.,
RA Ferdaoussi M., Roduit R., Maurer F., Beckmann J.S., Kastrup J.S.,
RA Gajhede M., Bonny C.;
RT "A unique set of SH3-SH3 interactions controls IB1 homodimerization.";
RL EMBO J. 25:785-797(2006).
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. Required
CC for JNK activation in response to excitotoxic stress. Cytoplasmic
CC MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK
CC in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun.
CC May also participate in ApoER2-specific reelin signaling. Directly, or
CC indirectly, regulates GLUT2 gene expression and beta-cell function.
CC Appears to have a role in cell signaling in mature and developing nerve
CC terminals. May function as a regulator of vesicle transport, through
CC interactions with the JNK-signaling components and motor proteins.
CC Functions as an anti-apoptotic protein and whose level seems to
CC influence the beta-cell death or survival response. Acts as a scaffold
CC protein that coordinates with SH3RF1 in organizing different components
CC of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or
CC MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a
CC functional multiprotein complex to ensure the effective activation of
CC the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and
CC differentiation of CD8(+) T-cells. {ECO:0000250|UniProtKB:Q9WVI9,
CC ECO:0000269|PubMed:21076496}.
CC -!- SUBUNIT: Forms homo- or heterooligomeric complexes (PubMed:16456539).
CC Binds specific components of the JNK signaling pathway namely
CC MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAP2K7/MKK7, MAP3K11/MLK3 and
CC DLK1. Also binds the proline-rich domain-containing splice variant of
CC apolipoprotein E receptor 2 (ApoER2). Interacts, via the PID domain,
CC with ARHGEF28 (By similarity). Binds the cytoplasmic tails of LRP1 and
CC LRP2 (Megalin). 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 the cytoplasmic domain of APP (By similarity).
CC Interacts with DCLK2, VRK2 and MAP3K7/TAK1. Found in a complex with
CC SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1. Found in a
CC complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and
CC MAPK9/JNK2 (By similarity). Interacts with SH3RF2 (PubMed:22128169).
CC {ECO:0000250|UniProtKB:Q9UQF2, ECO:0000250|UniProtKB:Q9WVI9,
CC ECO:0000269|PubMed:16456539, ECO:0000269|PubMed:21076496,
CC ECO:0000269|PubMed:22128169}.
CC -!- INTERACTION:
CC Q9R237-3; Q9R237-3: Mapk8ip1; NbExp=8; IntAct=EBI-8051913, EBI-8051913;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Nucleus. Endoplasmic reticulum membrane
CC {ECO:0000250}. Mitochondrion membrane {ECO:0000250}. Note=Accumulates
CC in cell surface projections. Under certain stress conditions,
CC translocates to the perinuclear region of neurons. In insulin-secreting
CC cells, detected in both the cytoplasm and nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=JIP-1a, JIP-1b;
CC IsoId=Q9R237-1; Sequence=Displayed;
CC Name=2; Synonyms=JIP-1c, 2A;
CC IsoId=Q9R237-2; Sequence=VSP_002767;
CC Name=3; Synonyms=JIP-1d;
CC IsoId=Q9R237-3; Sequence=VSP_002768, VSP_002769;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and pancreatic beta-
CC cells. Weaker expression found in kidney.
CC -!- DOMAIN: The SH3 domain mediates homodimerization.
CC -!- PTM: Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr-
CC 103 is also necessary for the dissociation and activation of MAP3K12.
CC Phosphorylated by VRK2. Hyperphosphorylated during mitosis following
CC activation of stress-activated and MAP kinases (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Two preliminary events are required to prime for
CC ubiquitination; phosphorylation and an increased in intracellular
CC calcium concentration. Then, the calcium influx initiates
CC ubiquitination and degradation by the ubiquitin-proteasome pathway (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22543.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAD38351.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF108959; AAD22543.1; ALT_INIT; mRNA.
DR EMBL; AF092450; AAC62110.1; -; mRNA.
DR EMBL; AF109772; AAD38350.1; -; mRNA.
DR EMBL; AF109773; AAD38351.1; ALT_INIT; mRNA.
DR EMBL; AF109774; AAD38352.1; -; mRNA.
DR EMBL; DQ377223; ABD24062.1; -; mRNA.
DR RefSeq; NP_446229.1; NM_053777.1. [Q9R237-2]
DR PDB; 2FPD; X-ray; 2.05 A; A/B/C/D=487-546.
DR PDB; 2FPE; X-ray; 1.75 A; A/B/C/D/E/F/G/H=487-546.
DR PDB; 2FPF; X-ray; 3.00 A; A/B/C/D=482-552.
DR PDBsum; 2FPD; -.
DR PDBsum; 2FPE; -.
DR PDBsum; 2FPF; -.
DR AlphaFoldDB; Q9R237; -.
DR SMR; Q9R237; -.
DR BioGRID; 250437; 2.
DR IntAct; Q9R237; 6.
DR MINT; Q9R237; -.
DR STRING; 10116.ENSRNOP00000065176; -.
DR iPTMnet; Q9R237; -.
DR PhosphoSitePlus; Q9R237; -.
DR jPOST; Q9R237; -.
DR PaxDb; Q9R237; -.
DR PRIDE; Q9R237; -.
DR Ensembl; ENSRNOT00000079746; ENSRNOP00000074684; ENSRNOG00000058478. [Q9R237-2]
DR Ensembl; ENSRNOT00000117436; ENSRNOP00000090670; ENSRNOG00000058478. [Q9R237-1]
DR GeneID; 116457; -.
DR KEGG; rno:116457; -.
DR UCSC; RGD:70937; rat. [Q9R237-1]
DR CTD; 9479; -.
DR RGD; 70937; Mapk8ip1.
DR eggNOG; KOG3775; Eukaryota.
DR GeneTree; ENSGT00940000157089; -.
DR InParanoid; Q9R237; -.
DR OMA; GHHRERI; -.
DR OrthoDB; 372907at2759; -.
DR PhylomeDB; Q9R237; -.
DR TreeFam; TF325073; -.
DR EvolutionaryTrace; Q9R237; -.
DR PRO; PR:Q9R237; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000058478; Expressed in frontal cortex and 19 other tissues.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044295; C:axonal growth cone; IDA:MGI.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0044294; C:dendritic growth cone; IDA:MGI.
DR GO; GO:0044302; C:dentate gyrus mossy fiber; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008432; F:JUN kinase binding; IPI:RGD.
DR GO; GO:0019894; F:kinesin binding; ISS:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IMP: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; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0007258; P:JUN phosphorylation; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:RGD.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
DR CDD; cd11943; SH3_JIP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035638; JIP1_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
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 SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW Membrane; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Ubl conjugation.
FT CHAIN 1..708
FT /note="C-Jun-amino-terminal kinase-interacting protein 1"
FT /id="PRO_0000220630"
FT DOMAIN 485..546
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 558..697
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..282
FT /note="JNK-binding domain (JBD)"
FT REGION 154..173
FT /note="Minimal inhibitory domain (MID)"
FT REGION 280..468
FT /note="Interaction with MAP3K7"
FT /evidence="ECO:0000250"
FT REGION 426..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..657
FT /note="Interaction with VRK2"
FT /evidence="ECO:0000250"
FT MOTIF 350..357
FT /note="D-box 1"
FT MOTIF 361..369
FT /note="D-box 2"
FT COMPBIAS 102..116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 103
FT /note="Phosphothreonine; by MAPK8, MAPK9 and MAPK10"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 202
FT /note="Phosphothreonine; by MAPK8, MAPK9 and MAPK10"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT VAR_SEQ 1..33
FT /note="MAERESGLSGGAASPPAASPFLGLHIASPPNFR -> MQLVLKMDSSPDNDS
FT WLEDQWERW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10098834"
FT /id="VSP_002767"
FT VAR_SEQ 69..93
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_002768"
FT VAR_SEQ 708
FT /note="E -> EPMAQVQLQVDLEIKRAAAEQKLISEEDLNGAA (in isoform
FT 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_002769"
FT CONFLICT 38
FT /note="I -> V (in Ref. 2; AAC62110)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="S -> C (in Ref. 1; AAD22543)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="E -> D (in Ref. 4; ABD24062)"
FT /evidence="ECO:0000305"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:2FPE"
FT STRAND 511..517
FT /evidence="ECO:0007829|PDB:2FPE"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:2FPE"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:2FPE"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:2FPE"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:2FPE"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:2FPE"
SQ SEQUENCE 708 AA; 77318 MW; 4923FD55F1C511F4 CRC64;
MAERESGLSG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE ITDECGISLQ
CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA SDTPGAEDDE EDDDELAAQR
PGVGPSKAES GQEPASRSQG QGQGPGTGSG DTYRPKRPTT LNLFPQVPRS QDTLNNNSLG
KKHSWQDRVS RSSSPLKTGE QTPPHEHICL SDELPPQGSP VPTQDRGTST DSPCRRTAAT
QMAPPSGPPA TAPGGRGHSH RDRIHYQADV RLEATEEIYL TPVQRPPDPA EPTSTFLPPT
ESRMSVSSDP DPAAYSVTAG RPHPSISEED EGFDCLSSPE QAEPPGGGWR GSLGEPPPPP
RASLSSDTSA LSYDSVKYTL VVDEHAQLEL VSLRPCFGDY SDESDSATVY DNCASASSPY
ESAIGEEYEE APQPRPPTCL SEDSTPDEPD VHFSKKFLNV FMSGRSRSSS AESFGLFSCV
INGEEHEQTH RAIFRFVPRH EDELELEVDD PLLVELQAED YWYEAYNMRT GARGVFPAYY
AIEVTKEPEH MAALAKNSDW IDQFRVKFLG SVQVPYHKGN DVLCAAMQKI ATTRRLTVHF
NPPSSCVLEI SVRGVKIGVK ADEAQEAKGN KCSHFFQLKN ISFCGYHPKN NKYFGFITKH
PADHRFACHV FVSEDSTKAL AESVGRAFQQ FYKQFVEYTC PTEDIYLE
