GRIP1_HUMAN
ID GRIP1_HUMAN Reviewed; 1128 AA.
AC Q9Y3R0; C9JT59; Q1RLM0;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Glutamate receptor-interacting protein 1;
DE Short=GRIP-1;
GN Name=GRIP1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 265-1128 (ISOFORM 2), FUNCTION, INTERACTION
RP WITH EFNB1 AND EFNB3, AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=10197531; DOI=10.1016/s0896-6273(00)80706-0;
RA Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H.,
RA Klein R.;
RT "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft
RT membrane microdomains.";
RL Neuron 22:511-524(1999).
RN [4]
RP INTERACTION WITH PRLHR.
RX PubMed=11641419; DOI=10.1124/mol.60.5.916;
RA Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.;
RT "The carboxyl terminus of the prolactin-releasing peptide receptor
RT interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-5-
RT methylisoxazole-4-propionic acid receptor clustering.";
RL Mol. Pharmacol. 60:916-923(2001).
RN [5]
RP INVOLVEMENT IN FRASRS3.
RX PubMed=22510445; DOI=10.1136/jmedgenet-2011-100590;
RA Vogel M.J., van Zon P., Brueton L., Gijzen M., van Tuil M.C., Cox P.,
RA Schanze D., Kariminejad A., Ghaderi-Sohi S., Blair E., Zenker M.,
RA Scambler P.J., Ploos van Amstel H.K., van Haelst M.M.;
RT "Mutations in GRIP1 cause Fraser syndrome.";
RL J. Med. Genet. 49:303-306(2012).
RN [6]
RP INTERACTION WITH BUD23.
RX PubMed=24488492; DOI=10.1074/jbc.m113.540906;
RA Jangani M., Poolman T.M., Matthews L., Yang N., Farrow S.N., Berry A.,
RA Hanley N., Williamson A.J., Whetton A.D., Donn R., Ray D.W.;
RT "The methyltransferase WBSCR22/Merm1 enhances glucocorticoid receptor
RT function and is regulated in lung inflammation and cancer.";
RL J. Biol. Chem. 289:8931-8946(2014).
CC -!- FUNCTION: May play a role as a localized scaffold for the assembly of a
CC multiprotein signaling complex and as mediator of the trafficking of
CC its binding partners at specific subcellular location in neurons
CC (PubMed:10197531). Through complex formation with NSG1, GRIA2 and STX12
CC controls the intracellular fate of AMPAR and the endosomal sorting of
CC the GRIA2 subunit toward recycling and membrane targeting (By
CC similarity). {ECO:0000250|UniProtKB:P97879,
CC ECO:0000269|PubMed:10197531}.
CC -!- SUBUNIT: Interacts with EPHA7, EPHB2, KIF5A, KIF5B, KIF5C, GRIA2,
CC GRIA3, GRIPAP1/GRASP1, PPFIA1, PPFIA4, FRAS1, PLCD4, PTPRF and liprins-
CC alpha. Can form homomultimers or heteromultimers with GRIP2. Forms a
CC ternary complex with GRIA2 and CSPG4 (By similarity). Interacts with
CC ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis
CC disrupts binding to ATAD1 and to GRIA2 and leads to AMPAR complex
CC disassembly (By similarity). Interacts with EFNB1, EFNB3 and the C-
CC terminal tail of PRLHR. Interacts with SLC30A9 (By similarity).
CC Interacts with BUD23. Forms a complex with NSG1, GRIA2 and STX12;
CC controls the intracellular fate of AMPAR and the endosomal sorting of
CC the GRIA2 subunit toward recycling and membrane targeting. Interacts
CC with NSG1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P97879,
CC ECO:0000269|PubMed:10197531, ECO:0000269|PubMed:11641419,
CC ECO:0000269|PubMed:24488492}.
CC -!- INTERACTION:
CC Q9Y3R0; P03372: ESR1; NbExp=2; IntAct=EBI-5349621, EBI-78473;
CC Q9Y3R0; Q14653: IRF3; NbExp=2; IntAct=EBI-5349621, EBI-2650369;
CC Q9Y3R0; P49683: PRLHR; NbExp=2; IntAct=EBI-5349621, EBI-8009236;
CC Q9Y3R0; P28065: PSMB9; NbExp=3; IntAct=EBI-5349621, EBI-603300;
CC Q9Y3R0-3; Q7L9B9: EEPD1; NbExp=3; IntAct=EBI-12193965, EBI-12262046;
CC Q9Y3R0-3; P61328-2: FGF12; NbExp=3; IntAct=EBI-12193965, EBI-10699759;
CC Q9Y3R0-3; O60921: HUS1; NbExp=3; IntAct=EBI-12193965, EBI-1056174;
CC Q9Y3R0-3; P55082: MFAP3; NbExp=3; IntAct=EBI-12193965, EBI-11287173;
CC Q9Y3R0-3; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-12193965, EBI-11750983;
CC Q9Y3R0-3; Q9NNW5: WDR6; NbExp=3; IntAct=EBI-12193965, EBI-1568315;
CC Q9Y3R0-3; P47989: XDH; NbExp=3; IntAct=EBI-12193965, EBI-2557331;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:10197531}. Perikaryon
CC {ECO:0000250|UniProtKB:P97879}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P97879}. Cytoplasm
CC {ECO:0000250|UniProtKB:P97879}. Endomembrane system
CC {ECO:0000250|UniProtKB:P97879}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P97879}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P97879}. Postsynaptic density
CC {ECO:0000250|UniProtKB:P97879}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10197531}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P97879}. Note=Membrane-associated with vesicles,
CC peri-Golgi complexes and endoplasmic reticulum. Enriched in
CC postsynaptic plasma membrane and postsynaptic densities.
CC {ECO:0000250|UniProtKB:P97879}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y3R0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3R0-2; Sequence=VSP_009743;
CC Name=3;
CC IsoId=Q9Y3R0-3; Sequence=VSP_040281;
CC -!- DOMAIN: PDZ 6 mediates interaction with the PDZ recognition motif of
CC EFNB1 and EPHB2 and with the C-terminus of PPFIA1 and PPFIA4. PDZ 4 and
CC PDZ 5 mediate interaction with the C-terminus of GRIA2 and GRIA3. PDZ
CC 4, PDZ 5 and PDZ 6 mediate homomultimers. PDZ 7 mediates interaction
CC with PDZ domain of GRASP1. PDZ 7 domain binds CSPG4. PDZ 6 mediates
CC interaction with the C-terminus of liprins-alpha. PDZ 1, PDZ 2 and PDZ
CC 3 mediate interaction with the PDZ-binding motif of FRAS1 (By
CC similarity). PDZ 4 and PDZ 5 mediate interaction with PRLHR.
CC {ECO:0000250}.
CC -!- DISEASE: Fraser syndrome 3 (FRASRS3) [MIM:617667]: A form of Fraser
CC syndrome, an autosomal recessive disorder characterized by
CC cryptophthalmos, cutaneous syndactyly, and urogenital abnormalities
CC including renal agenesis or hypoplasia. Additional features include
CC abnormalities of the larynx, ear malformations, and facial
CC abnormalities. {ECO:0000269|PubMed:22510445}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
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DR EMBL; AC078889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115393; AAI15394.1; -; mRNA.
DR EMBL; BC115394; AAI15395.1; -; mRNA.
DR EMBL; AJ133439; CAB39895.1; -; mRNA.
DR CCDS; CCDS41807.1; -. [Q9Y3R0-3]
DR RefSeq; NP_001171545.1; NM_001178074.1.
DR RefSeq; NP_066973.2; NM_021150.3. [Q9Y3R0-3]
DR RefSeq; XP_011536395.1; XM_011538093.2.
DR PDB; 2JIL; X-ray; 1.50 A; A/B=149-239.
DR PDBsum; 2JIL; -.
DR AlphaFoldDB; Q9Y3R0; -.
DR SMR; Q9Y3R0; -.
DR BioGRID; 116995; 75.
DR CORUM; Q9Y3R0; -.
DR IntAct; Q9Y3R0; 28.
DR MINT; Q9Y3R0; -.
DR STRING; 9606.ENSP00000381098; -.
DR TCDB; 8.A.24.1.12; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.
DR GlyGen; Q9Y3R0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3R0; -.
DR PhosphoSitePlus; Q9Y3R0; -.
DR BioMuta; GRIP1; -.
DR DMDM; 313104231; -.
DR EPD; Q9Y3R0; -.
DR jPOST; Q9Y3R0; -.
DR MassIVE; Q9Y3R0; -.
DR MaxQB; Q9Y3R0; -.
DR PaxDb; Q9Y3R0; -.
DR PeptideAtlas; Q9Y3R0; -.
DR PRIDE; Q9Y3R0; -.
DR ProteomicsDB; 86065; -. [Q9Y3R0-1]
DR ProteomicsDB; 86066; -. [Q9Y3R0-2]
DR ProteomicsDB; 86067; -. [Q9Y3R0-3]
DR Antibodypedia; 8598; 242 antibodies from 36 providers.
DR DNASU; 23426; -.
DR Ensembl; ENST00000359742.9; ENSP00000352780.4; ENSG00000155974.13. [Q9Y3R0-1]
DR Ensembl; ENST00000398016.7; ENSP00000381098.3; ENSG00000155974.13. [Q9Y3R0-3]
DR GeneID; 23426; -.
DR KEGG; hsa:23426; -.
DR MANE-Select; ENST00000359742.9; ENSP00000352780.4; NM_001366722.1; NP_001353651.1.
DR UCSC; uc001stk.4; human. [Q9Y3R0-1]
DR CTD; 23426; -.
DR DisGeNET; 23426; -.
DR GeneCards; GRIP1; -.
DR HGNC; HGNC:18708; GRIP1.
DR HPA; ENSG00000155974; Tissue enhanced (parathyroid).
DR MalaCards; GRIP1; -.
DR MIM; 604597; gene.
DR MIM; 617667; phenotype.
DR neXtProt; NX_Q9Y3R0; -.
DR OpenTargets; ENSG00000155974; -.
DR Orphanet; 2052; Fraser syndrome.
DR VEuPathDB; HostDB:ENSG00000155974; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000158692; -.
DR InParanoid; Q9Y3R0; -.
DR OMA; QLYPGYE; -.
DR OrthoDB; 65191at2759; -.
DR PhylomeDB; Q9Y3R0; -.
DR TreeFam; TF326909; -.
DR PathwayCommons; Q9Y3R0; -.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
DR SignaLink; Q9Y3R0; -.
DR SIGNOR; Q9Y3R0; -.
DR BioGRID-ORCS; 23426; 10 hits in 1062 CRISPR screens.
DR ChiTaRS; GRIP1; human.
DR EvolutionaryTrace; Q9Y3R0; -.
DR GeneWiki; GRIP1_(gene); -.
DR GenomeRNAi; 23426; -.
DR Pharos; Q9Y3R0; Tbio.
DR PRO; PR:Q9Y3R0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y3R0; protein.
DR Bgee; ENSG00000155974; Expressed in cortical plate and 133 other tissues.
DR ExpressionAtlas; Q9Y3R0; baseline and differential.
DR Genevisible; Q9Y3R0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; TAS:AgBase.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; NAS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; ISS:ARUK-UCL.
DR Gene3D; 2.30.42.10; -; 7.
DR InterPro; IPR030026; GRIP1.
DR InterPro; IPR043545; GRIP1/2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR46227; PTHR46227; 1.
DR PANTHER; PTHR46227:SF3; PTHR46227:SF3; 1.
DR Pfam; PF00595; PDZ; 6.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 7.
DR SUPFAM; SSF50156; SSF50156; 7.
DR PROSITE; PS50106; PDZ; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse.
FT CHAIN 1..1128
FT /note="Glutamate receptor-interacting protein 1"
FT /id="PRO_0000083849"
FT DOMAIN 53..136
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 150..238
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 252..336
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 472..561
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 573..658
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 673..755
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1004..1086
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 754..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97879"
FT VAR_SEQ 348..400
FT /note="VKIQRSDRQLTWDSWASNHSSLHTNHHYNTYHPDHCRVPALTFPKAPPPNSP
FT P -> A (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040281"
FT VAR_SEQ 912..926
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10197531"
FT /id="VSP_009743"
FT VARIANT 322
FT /note="A -> T (in dbSNP:rs17102531)"
FT /id="VAR_056904"
FT CONFLICT 821
FT /note="Q -> E (in Ref. 2; AAI15394 and 3; CAB39895)"
FT /evidence="ECO:0000305"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:2JIL"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2JIL"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2JIL"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:2JIL"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2JIL"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:2JIL"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:2JIL"
SQ SEQUENCE 1128 AA; 122422 MW; D97B96ADF2C3796B CRC64;
MIAVSFKCRC QILRRLTKDE SPYTKSASQT KPPDGALAVR RQSIPEEFKG STVVELMKKE
GTTLGLTVSG GIDKDGKPRV SNLRQGGIAA RSDQLDVGDY IKAVNGINLA KFRHDEIISL
LKNVGERVVL EVEYELPPVS VQGSSVIFRT VEVTLHKEGN TFGFVIRGGA HDDRNKSRPV
VITCVRPGGP ADREGTIKPG DRLLSVDGIR LLGTTHAEAM SILKQCGQEA ALLIEYDVSV
MDSVATASGP LLVEVAKTPG ASLGVALTTS MCCNKQVIVI DKIKSASIAD RCGALHVGDH
ILSIDGTSME YCTLAEATQF LANTTDQVKL EILPHHQTRL ALKGPDHVKI QRSDRQLTWD
SWASNHSSLH TNHHYNTYHP DHCRVPALTF PKAPPPNSPP ALVSSSFSPT SMSAYSLSSL
NMGTLPRSLY STSPRGTMMR RRLKKKDFKS SLSLASSTVG LAGQVVHTET TEVVLTADPV
TGFGIQLQGS VFATETLSSP PLISYIEADS PAERCGVLQI GDRVMAINGI PTEDSTFEEA
SQLLRDSSIT SKVTLEIEFD VAESVIPSSG TFHVKLPKKH NVELGITISS PSSRKPGDPL
VISDIKKGSV AHRTGTLELG DKLLAIDNIR LDNCSMEDAV QILQQCEDLV KLKIRKDEDN
SDEQESSGAI IYTVELKRYG GPLGITISGT EEPFDPIIIS SLTKGGLAER TGAIHIGDRI
LAINSSSLKG KPLSEAIHLL QMAGETVTLK IKKQTDAQSA SSPKKFPISS HLSDLGDVEE
DSSPAQKPGK LSDMYPSTVP SVDSAVDSWD GSAIDTSYGT QGTSFQASGY NFNTYDWRSP
KQRGSLSPVT KPRSQTYPDV GLSYEDWDRS TASGFAGAAD SAETEQEENF WSQALEDLET
CGQSGILREL EEKADRRVSL RNMTLLATIM SGSTMSLNHE APTPRSQLGR QASFQERSSS
RPHYSQTTRS NTLPSDVGRK SVTLRKMKQE IKEIMSPTPV ELHKVTLYKD SDMEDFGFSV
ADGLLEKGVY VKNIRPAGPG DLGGLKPYDR LLQVNHVRTR DFDCCLVVPL IAESGNKLDL
VISRNPLASQ KSIDQQSLPG DWSEQNSAFF QQPSHGGNLE TREPTNTL
