ID DLGP1_MOUSE Reviewed; 992 AA. AC Q9D415; Q52KF6; Q5DTK5; Q6P6N4; Q6XBF4; Q8BZL7; Q8BZQ1; Q8C0G0; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 3. DT 27-MAR-2024, entry version 172. DE RecName: Full=Disks large-associated protein 1; DE Short=DAP-1; DE AltName: Full=Guanylate kinase-associated protein; DE AltName: Full=PSD-95/SAP90-binding protein 1; DE AltName: Full=SAP90/PSD-95-associated protein 1; DE Short=SAPAP1; GN Name=Dlgap1; Synonyms=Gkap, Kiaa4162; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY. RC STRAIN=ICR; RX PubMed=15024750; DOI=10.1002/cne.20060; RA Welch J.M., Wang D., Feng G.; RT "Differential mRNA expression and protein localization of the SAP90/PSD-95- RT associated proteins (SAPAPs) in the nervous system of the mouse."; RL J. Comp. Neurol. 472:24-39(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 660-992 (ISOFORM 4). RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Fetal brain; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by RT screening of terminal sequences of cDNA clones randomly sampled from size- RT fractionated libraries."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 210-992 (ISOFORM 4). RC STRAIN=C57BL/6J; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-509; SER-516 AND RP SER-947, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-362; SER-365; RP SER-368; SER-372; SER-418; SER-421; SER-425; SER-437; SER-509; SER-516; RP SER-578; THR-579; SER-581; SER-605; THR-606 AND SER-608, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP INTERACTION WITH SHANK3, AND SUBCELLULAR LOCATION. RX PubMed=24153177; DOI=10.1038/nature12630; RA Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J., RA Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C., RA Zoghbi H.Y.; RT "SHANK3 overexpression causes manic-like behaviour with unique RT pharmacogenetic properties."; RL Nature 503:72-77(2013). CC -!- FUNCTION: Part of the postsynaptic scaffold in neuronal cells. CC -!- SUBUNIT: Interacts with the guanylate kinase-like domain of DLG1, DLG2, CC DLG3, DLG4 and AIP1. Interacts with the PDZ domain of SHANK1, SHANK2 CC and SHANK3. Found in a complex with DLG4 and SHANK1, SHANK2 or SHANK3. CC Found in a complex with DLG4 and BEGAIN. Interacts with DYL2 and LRFN1. CC Interacts with MPP2 (via the SH3-Guanylate kinase-like sub-module) (By CC similarity). {ECO:0000250|UniProtKB:P97836, CC ECO:0000269|PubMed:24153177}. CC -!- INTERACTION: CC Q9D415; Q80YA9: Cnksr2; NbExp=3; IntAct=EBI-400152, EBI-771429; CC Q9D415; P35436: Grin2a; NbExp=2; IntAct=EBI-400152, EBI-400115; CC Q9D415; Q9Z2Y3: Homer1; NbExp=4; IntAct=EBI-400152, EBI-396980; CC Q9D415; Q4ACU6: Shank3; NbExp=4; IntAct=EBI-400152, EBI-771450; CC Q9D415; F6SEU4: Syngap1; NbExp=3; IntAct=EBI-400152, EBI-5797569; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse CC {ECO:0000269|PubMed:24153177}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=SAPAP1; CC IsoId=Q9D415-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9D415-2; Sequence=VSP_015409; CC Name=3; Synonyms=GKAP1a; CC IsoId=Q9D415-3; Sequence=VSP_015412; CC Name=4; Synonyms=GKAP1b; CC IsoId=Q9D415-4; Sequence=VSP_015409, VSP_015413, VSP_015414; CC Name=5; CC IsoId=Q9D415-5; Sequence=VSP_015410, VSP_015411; CC Name=6; CC IsoId=Q9D415-6; Sequence=VSP_015408; CC -!- TISSUE SPECIFICITY: Highest levels in the neocortex, part of the CC hippocampus, the granule cell layer of the cerebellum, the glomerular CC layer of the olfactory bulb, the inner plexiform layer of the retina, CC the ventral and dorsal horn of the spinal chord, the neuromuscular CC junction and the submandibular ganglion. {ECO:0000269|PubMed:15024750}. CC -!- PTM: Ubiquitinated by TRIM3; leading to proteasomal degradation. CC {ECO:0000250|UniProtKB:P97836}. CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD90519.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AY243846; AAP70755.2; -; mRNA. DR EMBL; AK031410; BAC27391.1; -; mRNA. DR EMBL; AK033901; BAC28508.1; -; mRNA. DR EMBL; AK034182; BAC28619.1; -; mRNA. DR EMBL; AK220515; BAD90519.1; ALT_INIT; mRNA. DR EMBL; BC062120; AAH62120.1; -; mRNA. DR EMBL; BC094369; AAH94369.1; -; mRNA. DR CCDS; CCDS28953.1; -. [Q9D415-1] DR CCDS; CCDS84331.1; -. [Q9D415-3] DR CCDS; CCDS84332.1; -. [Q9D415-2] DR RefSeq; NP_001334340.1; NM_001347411.1. [Q9D415-3] DR RefSeq; NP_081988.3; NM_027712.3. [Q9D415-4] DR RefSeq; NP_808307.2; NM_177639.6. [Q9D415-1] DR RefSeq; XP_006524236.1; XM_006524173.2. [Q9D415-1] DR RefSeq; XP_011244709.1; XM_011246407.2. [Q9D415-1] DR PDB; 7YKI; X-ray; 2.00 A; B/D=408-421. DR PDBsum; 7YKI; -. DR AlphaFoldDB; Q9D415; -. DR SMR; Q9D415; -. DR BioGRID; 230347; 166. DR IntAct; Q9D415; 158. DR MINT; Q9D415; -. DR STRING; 10090.ENSMUSP00000122896; -. DR GlyGen; Q9D415; 14 sites, 1 O-linked glycan (14 sites). DR iPTMnet; Q9D415; -. DR MetOSite; Q9D415; -. DR PhosphoSitePlus; Q9D415; -. DR SwissPalm; Q9D415; -. DR MaxQB; Q9D415; -. DR PaxDb; 10090-ENSMUSP00000122896; -. DR PeptideAtlas; Q9D415; -. DR ProteomicsDB; 279780; -. [Q9D415-1] DR ProteomicsDB; 279781; -. [Q9D415-2] DR ProteomicsDB; 279782; -. [Q9D415-3] DR ProteomicsDB; 279783; -. [Q9D415-4] DR ProteomicsDB; 279784; -. [Q9D415-5] DR ProteomicsDB; 279785; -. [Q9D415-6] DR ABCD; Q9D415; 3 sequenced antibodies. DR Antibodypedia; 21914; 282 antibodies from 37 providers. DR DNASU; 224997; -. DR Ensembl; ENSMUST00000060072.12; ENSMUSP00000052858.6; ENSMUSG00000003279.18. [Q9D415-2] DR Ensembl; ENSMUST00000133983.8; ENSMUSP00000116716.2; ENSMUSG00000003279.18. [Q9D415-2] DR Ensembl; ENSMUST00000135938.8; ENSMUSP00000118497.2; ENSMUSG00000003279.18. [Q9D415-3] DR Ensembl; ENSMUST00000155016.8; ENSMUSP00000122896.2; ENSMUSG00000003279.18. [Q9D415-1] DR GeneID; 224997; -. DR KEGG; mmu:224997; -. DR UCSC; uc008dky.1; mouse. [Q9D415-6] DR UCSC; uc008dla.1; mouse. [Q9D415-5] DR UCSC; uc008dle.2; mouse. [Q9D415-1] DR UCSC; uc008dlf.2; mouse. [Q9D415-4] DR AGR; MGI:1346065; -. DR CTD; 9229; -. DR MGI; MGI:1346065; Dlgap1. DR VEuPathDB; HostDB:ENSMUSG00000003279; -. DR eggNOG; KOG3971; Eukaryota. DR GeneTree; ENSGT00940000156220; -. DR HOGENOM; CLU_010880_0_0_1; -. DR InParanoid; Q9D415; -. DR OMA; NSGDAHP; -. DR PhylomeDB; Q9D415; -. DR TreeFam; TF321382; -. DR Reactome; R-MMU-6794361; Neurexins and neuroligins. DR BioGRID-ORCS; 224997; 2 hits in 76 CRISPR screens. DR ChiTaRS; Dlgap1; mouse. DR PRO; PR:Q9D415; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q9D415; Protein. DR Bgee; ENSMUSG00000003279; Expressed in piriform cortex and 161 other cell types or tissues. DR ExpressionAtlas; Q9D415; baseline and differential. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL. DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI. DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI. DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB. DR GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:MGI. DR GO; GO:0070842; P:aggresome assembly; ISO:MGI. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:MGI. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI. DR GO; GO:0035418; P:protein localization to synapse; ISO:MGI. DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:MGI. DR InterPro; IPR005026; SAPAP. DR PANTHER; PTHR12353:SF7; DISKS LARGE-ASSOCIATED PROTEIN 1; 1. DR PANTHER; PTHR12353; DISKS LARGE-ASSOCIATED PROTEIN DAP SAP90/PSD-95-ASSOCIATED PROTEIN; 1. DR Pfam; PF03359; GKAP; 1. DR Genevisible; Q9D415; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Membrane; KW Phosphoprotein; Reference proteome; Synapse; Ubl conjugation. FT CHAIN 1..992 FT /note="Disks large-associated protein 1" FT /id="PRO_0000174289" FT REGION 150..209 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 355..376 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 665..676 FT /note="Interaction with DYL2" FT /evidence="ECO:0000250" FT REGION 687..698 FT /note="Interaction with DYL2" FT /evidence="ECO:0000250" FT REGION 914..980 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 990..992 FT /note="PDZ-binding" FT /evidence="ECO:0000250" FT COMPBIAS 174..193 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..209 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 914..931 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 948..962 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 169 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 368 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 372 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 389 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97836" FT MOD_RES 418 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 425 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 428 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97836" FT MOD_RES 437 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 578 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 579 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 581 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 605 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 606 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 608 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 611 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97836" FT MOD_RES 947 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087" FT VAR_SEQ 398..992 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_015408" FT VAR_SEQ 537..546 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3" FT /id="VSP_015409" FT VAR_SEQ 538 FT /note="V -> E (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_015410" FT VAR_SEQ 539..992 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_015411" FT VAR_SEQ 547..574 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15024750" FT /id="VSP_015412" FT VAR_SEQ 924..944 FT /note="ERRAPPPVPKKPAKGPAPLIR -> VEQCRFCMVHLKPCTNAGQSK (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_015413" FT VAR_SEQ 945..992 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_015414" FT CONFLICT 383 FT /note="L -> P (in Ref. 3; BAD90519)" FT /evidence="ECO:0000305" FT CONFLICT 397 FT /note="K -> R (in Ref. 1; AAP70755)" FT /evidence="ECO:0000305" FT CONFLICT 431 FT /note="P -> H (in Ref. 2; BAC27391)" FT /evidence="ECO:0000305" FT CONFLICT 752 FT /note="S -> F (in Ref. 2; BAC28619)" FT /evidence="ECO:0000305" SQ SEQUENCE 992 AA; 110374 MW; 9962C8B56A33EE13 CRC64; MKGLSGSRSH HHGITCEAAC DSLSHHSDHK PYLLSPVDHH PADHPYYTQR NSFQAECVGP FSDPLASSTF PRRHYTSQQE LKDESALVPR TLATKANRLP TNLLDQFERQ LPLSRDGYHT LQYKRTAVEH RSDSPGRIRH LVHSVQKLFT KSHSLEGPSK GSVNGGKASP DESQTLRYGK RSKSKERRSE SKARSNASNA SPTSPSWWSS DDNLDGDMCL YHTPSGVMTM GRCPDRSASQ YFMEAYNTIS EQAVKASRSN NDIKCSTCAN LPVTLDAPLL KKSAWSSTLT VSRAREVYQK ASVNMDQAMV KSEACQQERS CQYLQVPQDE WSGYTPRGKD DEIPCRRMRS GSYIKAMGDE DSGDSDTSPK PSPKVAARRE SYLKATQPSL TELTTLKISN EHSPKLQIRS HSYLRAVSEV SINRSLDSLD PAGLLTSPKF RSRNESYMRA MSTISQVSEM EVNGQFESVC ESVFSELESQ AVEALDLPLP GCFRMRSHSY VRAIEKGCSQ DDECVSLRSS SPPRTTTTVR TIQSSTGVIK LSSAVEVSSC ITTYKKTPPP VPPRTTTKPF ISITAQSSTE SAQDAYMDGQ GQRGDMISQS GLSNSTESLD SMKALTAAIE AANAQIHGPA SQHMGSNAAA VTTTTTIATV TTEDRKKDFK KNRCLSIGIQ VDDAEEPEKM AESKTSNKFQ SVGVQVEEEK CFRRFTRSNS VTTAVQADLD FHDNLENSLE SIEDNSCPGP MARQFSRDAS TSTVSIQGSG NHYHACAADD DFDTDFDPSI LPPPDPWIDS ITEDPLEAVQ RSVCHRDGHW FLKLLQAERD RMEGWCKLME REERENNLPE DILGKIRTAV GSAQLLMAQK FYQFRELCEE NLNPNAHPRP TSQDLAGFWD MLQLSIENIS MKFDELHQLK ANNWKQMDPL DKKERRAPPP VPKKPAKGPA PLIRERSLES SQRQEARKRL MAAKRAASVR QNSATESAES IEIYIPEAQT RL //