ID PACN2_MOUSE Reviewed; 486 AA. AC Q9WVE8; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 172. DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 2; DE AltName: Full=Syndapin-2; DE AltName: Full=Syndapin-II; DE Short=SdpII; GN Name=Pacsin2; 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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6 X DBA; RX PubMed=10431838; DOI=10.1016/s0014-5793(99)00830-3; RA Ritter B., Modregger J., Paulsson M., Plomann M.; RT "PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter RT proteins."; RL FEBS Lett. 454:356-362(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; 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 FUNCTION, INTERACTION WITH DNM1; SYNJ1 AND WASL, HOMOOLIGOMERIZATION, RP HETEROOLIGOMERIZATION WITH PACSIN1 AND PACSIN3, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND MUTAGENESIS OF PRO-478. RX PubMed=11082044; DOI=10.1242/jcs.113.24.4511; RA Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.; RT "All three PACSIN isoforms bind to endocytic proteins and inhibit RT endocytosis."; RL J. Cell Sci. 113:4511-4521(2000). RN [4] RP FUNCTION, INTERACTION WITH EHD1 AND EHD3, AND SUBCELLULAR LOCATION. RX PubMed=15930129; DOI=10.1091/mbc.e05-01-0076; RA Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D., RA Kessels M.M., Qualmann B.; RT "EHD proteins associate with syndapin I and II and such interactions play a RT crucial role in endosomal recycling."; RL Mol. Biol. Cell 16:3642-3658(2005). RN [5] RP INTERACTION WITH TRPV4. RX PubMed=16627472; DOI=10.1074/jbc.m602452200; RA Cuajungco M.P., Grimm C., Oshima K., D'hoedt D., Nilius B., RA Mensenkamp A.R., Bindels R.J., Plomann M., Heller S.; RT "PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the RT subcellular localization of TRPV4."; RL J. Biol. Chem. 281:18753-18762(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; 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 [7] RP FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-40; ARG-50; RP 124-MET-MET-125 AND LYS-189. RX PubMed=20188097; DOI=10.1016/j.febslet.2010.02.058; RA Shimada A., Takano K., Shirouzu M., Hanawa-Suetsugu K., Terada T., RA Toyooka K., Umehara T., Yamamoto M., Yokoyama S., Suetsugu S.; RT "Mapping of the basic amino-acid residues responsible for tubulation and RT cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II."; RL FEBS Lett. 584:1111-1118(2010). RN [8] RP FUNCTION, DOMAIN, SUBCELLULAR LOCATION, INTERACTION WITH CAV1, AND RP DISRUPTION PHENOTYPE. RX PubMed=21610094; DOI=10.1242/jcs.086264; RA Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.; RT "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting."; RL J. Cell Sci. 124:2032-2040(2011). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAC1. RX PubMed=21693584; DOI=10.1242/jcs.080630; RA de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C., Hensbergen P.J., RA Deelder A.M., Plomann M., Hordijk P.L.; RT "The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell RT spreading and migration."; RL J. Cell Sci. 124:2375-2388(2011). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=21807942; DOI=10.1242/jcs.084319; RA Hansen C.G., Howard G., Nichols B.J.; RT "Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis."; RL J. Cell Sci. 124:2777-2785(2011). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23129763; DOI=10.1074/jbc.m112.391078; RA de Kreuk B.J., Anthony E.C., Geerts D., Hordijk P.L.; RT "The F-BAR protein PACSIN2 regulates epidermal growth factor receptor RT internalization."; RL J. Biol. Chem. 287:43438-43453(2012). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [13] RP PHOSPHORYLATION AT SER-313, PHOSPHORYLATION AT SER-373, MUTAGENESIS OF RP SER-313 AND SER-373, AND SUBCELLULAR LOCATION. RX PubMed=26092940; DOI=10.1242/jcs.167775; RA Senju Y., Rosenbaum E., Shah C., Hamada-Nakahara S., Itoh Y., Yamamoto K., RA Hanawa-Suetsugu K., Daumke O., Suetsugu S.; RT "Phosphorylation of PACSIN2 by protein kinase C triggers the removal of RT caveolae from the plasma membrane."; RL J. Cell Sci. 128:2766-2780(2015). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 16-302, SUBUNIT, AND DOMAIN. RX PubMed=20471395; DOI=10.1016/j.jmb.2010.05.008; RA Plomann M., Wittmann J.G., Rudolph M.G.; RT "A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to RT membrane-curvature sensing."; RL J. Mol. Biol. 400:129-136(2010). CC -!- FUNCTION: Regulates the morphogenesis and endocytosis of caveolae CC (PubMed:21807942). Lipid-binding protein that is able to promote the CC tubulation of the phosphatidic acid-containing membranes it CC preferentially binds. Plays a role in intracellular vesicle-mediated CC transport. Involved in the endocytosis of cell-surface receptors like CC the EGF receptor, contributing to its internalization in the absence of CC EGF stimulus. {ECO:0000269|PubMed:11082044, CC ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:20188097, CC ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:21693584, CC ECO:0000269|PubMed:21807942, ECO:0000269|PubMed:23129763}. CC -!- SUBUNIT: Homodimer (PubMed:20471395). May form heterooligomers with CC other PACSINs (PubMed:11082044). Interacts (via NPF motifs) with EHD1 CC (via EH domain) (PubMed:15930129). Interacts (via NPF motifs) with EHD2 CC (via EH domain); this interaction probably stabilizes the caveolae (By CC similarity). Interacts with EHD3 (PubMed:15930129). Interacts (via the CC SH3 domain) with MICALL1 (By similarity). Interacts with RAC1 CC (PubMed:21693584). Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 CC and WASL (PubMed:11082044). Interacts (via F-BAR domain) with CAV1; CC this interaction induces membrane tubulation (PubMed:21610094). CC Interacts with TRPV4 (PubMed:16627472). {ECO:0000250|UniProtKB:Q9UNF0, CC ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:15930129, CC ECO:0000269|PubMed:16627472, ECO:0000269|PubMed:20471395, CC ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:21693584}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic CC vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell CC projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic CC side. Early endosome. Recycling endosome membrane {ECO:0000250}. Cell CC membrane; Peripheral membrane protein; Cytoplasmic side. Cell CC projection {ECO:0000250|UniProtKB:Q9UNF0}. Membrane, caveola CC {ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:21807942, CC ECO:0000269|PubMed:26092940}. Note=Detected at the neck of flask-shaped CC caveolae. Localization to tubular recycling endosomes probably requires CC interaction with MICALL1 and EHD1. CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). CC {ECO:0000269|PubMed:10431838, ECO:0000269|PubMed:11082044}. CC -!- DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane- CC binding and membrane tubulation (PubMed:20188097, PubMed:20471395). CC Autoinhibition of these functions is mediated by an interaction between CC the SH3 and F-BAR domains (By similarity). The F-Bar domain also CC mediates the binding to the cell actin cytoskeleton through the CC interaction with CAV-1 (PubMed:21610094). CC {ECO:0000250|UniProtKB:Q9UNF0, ECO:0000269|PubMed:20188097, CC ECO:0000269|PubMed:20471395, ECO:0000269|PubMed:21610094}. CC -!- PTM: Phosphorylated by casein kinase 2 (CK2). Phosphorylation by PKC CC probably decreases the membrane binding and tubulation capacities of CC PACSIN2, thereby modulating the lifetime of caveolae (PubMed:26092940). CC {ECO:0000269|PubMed:26092940}. CC -!- DISRUPTION PHENOTYPE: Results in loss of morphologically defined CC caveolae. {ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:21807942}. CC -!- SIMILARITY: Belongs to the PACSIN 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; AF128535; AAD41780.1; -; mRNA. DR EMBL; BC023502; AAH23502.1; -; mRNA. DR CCDS; CCDS27701.1; -. DR RefSeq; NP_001152981.1; NM_001159509.1. DR RefSeq; NP_001152982.1; NM_001159510.1. DR RefSeq; NP_035992.1; NM_011862.3. DR PDB; 3LLL; X-ray; 3.30 A; A/B=16-302. DR PDBsum; 3LLL; -. DR AlphaFoldDB; Q9WVE8; -. DR SMR; Q9WVE8; -. DR BioGRID; 204831; 16. DR IntAct; Q9WVE8; 2. DR MINT; Q9WVE8; -. DR STRING; 10090.ENSMUSP00000131504; -. DR ChEMBL; CHEMBL2176817; -. DR GlyGen; Q9WVE8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9WVE8; -. DR PhosphoSitePlus; Q9WVE8; -. DR SwissPalm; Q9WVE8; -. DR EPD; Q9WVE8; -. DR jPOST; Q9WVE8; -. DR MaxQB; Q9WVE8; -. DR PaxDb; 10090-ENSMUSP00000130098; -. DR ProteomicsDB; 294099; -. DR Pumba; Q9WVE8; -. DR Antibodypedia; 34964; 265 antibodies from 31 providers. DR DNASU; 23970; -. DR Ensembl; ENSMUST00000056177.7; ENSMUSP00000058320.7; ENSMUSG00000016664.17. DR Ensembl; ENSMUST00000165095.9; ENSMUSP00000130098.2; ENSMUSG00000016664.17. DR Ensembl; ENSMUST00000171436.8; ENSMUSP00000131504.2; ENSMUSG00000016664.17. DR Ensembl; ENSMUST00000230679.2; ENSMUSP00000155481.2; ENSMUSG00000016664.17. DR Ensembl; ENSMUST00000231184.2; ENSMUSP00000155334.2; ENSMUSG00000016664.17. DR GeneID; 23970; -. DR KEGG; mmu:23970; -. DR UCSC; uc007xba.2; mouse. DR AGR; MGI:1345153; -. DR CTD; 11252; -. DR MGI; MGI:1345153; Pacsin2. DR VEuPathDB; HostDB:ENSMUSG00000016664; -. DR eggNOG; KOG2856; Eukaryota. DR GeneTree; ENSGT00950000182973; -. DR HOGENOM; CLU_030752_0_0_1; -. DR InParanoid; Q9WVE8; -. DR OMA; PDSLGWC; -. DR OrthoDB; 9421at2759; -. DR PhylomeDB; Q9WVE8; -. DR TreeFam; TF313677; -. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR BioGRID-ORCS; 23970; 2 hits in 76 CRISPR screens. DR ChiTaRS; Pacsin2; mouse. DR EvolutionaryTrace; Q9WVE8; -. DR PRO; PR:Q9WVE8; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q9WVE8; Protein. DR Bgee; ENSMUSG00000016664; Expressed in interventricular septum and 251 other cell types or tissues. DR ExpressionAtlas; Q9WVE8; baseline and differential. DR GO; GO:0005901; C:caveola; IDA:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; IDA:MGI. DR GO; GO:0034451; C:centriolar satellite; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0016607; C:nuclear speck; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; ISO:MGI. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB. DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro. DR GO; GO:0070836; P:caveola assembly; ISS:UniProtKB. DR GO; GO:0072584; P:caveolin-mediated endocytosis; ISS:UniProtKB. DR GO; GO:0048858; P:cell projection morphogenesis; IMP:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:0045806; P:negative regulation of endocytosis; IDA:MGI. DR GO; GO:0097320; P:plasma membrane tubulation; IMP:UniProtKB. DR GO; GO:0036010; P:protein localization to endosome; ISO:MGI. DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:MGI. DR CDD; cd07679; F-BAR_PACSIN2; 1. DR CDD; cd11998; SH3_PACSIN1-2; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR031160; F_BAR. DR InterPro; IPR001060; FCH_dom. DR InterPro; IPR035743; PACSIN1/PACSIN2_SH3. DR InterPro; IPR037453; PACSIN2_F-BAR. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1. DR PANTHER; PTHR23065:SF14; PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 2; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00055; FCH; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51741; F_BAR; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9WVE8; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell membrane; Cell projection; Coiled coil; KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Endosome; KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; SH3 domain. FT CHAIN 1..486 FT /note="Protein kinase C and casein kinase substrate in FT neurons protein 2" FT /id="PRO_0000161796" FT DOMAIN 11..282 FT /note="F-BAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077" FT DOMAIN 426..486 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 315..426 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 25..274 FT MOTIF 362..364 FT /note="NPF1" FT MOTIF 405..407 FT /note="NPF2" FT MOTIF 417..419 FT /note="NPF3" FT COMPBIAS 325..368 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 386..424 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 53 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 273 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UNF0" FT MOD_RES 313 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:26092940" FT MOD_RES 373 FT /note="Phosphoserine; by IKKB" FT /evidence="ECO:0000269|PubMed:26092940" FT MOD_RES 399 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 446 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UNF0" FT MUTAGEN 40 FT /note="D->K: Slight increase in affinity for membranes. FT Increases membrane tubulation activity." FT /evidence="ECO:0000269|PubMed:20188097" FT MUTAGEN 50 FT /note="R->D: Slight decrease in affinity for membranes. FT Nearly abolishes membrane tubulation activity." FT /evidence="ECO:0000269|PubMed:20188097" FT MUTAGEN 124..125 FT /note="MM->TT: Nearly abolishes membrane tubulation FT activity." FT /evidence="ECO:0000269|PubMed:20188097" FT MUTAGEN 189 FT /note="K->E: Decreases affinity for membranes." FT /evidence="ECO:0000269|PubMed:20188097" FT MUTAGEN 313 FT /note="S->E: Reduced membrane-binding affinity." FT /evidence="ECO:0000269|PubMed:26092940" FT MUTAGEN 373 FT /note="S->D: Reduced membrane-binding affinity." FT /evidence="ECO:0000269|PubMed:26092940" FT MUTAGEN 478 FT /note="P->L: Loss of DNM1-, SYNJ1- and WASL-binding." FT /evidence="ECO:0000269|PubMed:11082044" FT TURN 21..24 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 25..71 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 77..106 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 108..117 FT /evidence="ECO:0007829|PDB:3LLL" FT STRAND 124..128 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 131..174 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 184..192 FT /evidence="ECO:0007829|PDB:3LLL" FT TURN 193..198 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 199..202 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 204..216 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 220..255 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 261..275 FT /evidence="ECO:0007829|PDB:3LLL" FT HELIX 279..289 FT /evidence="ECO:0007829|PDB:3LLL" SQ SEQUENCE 486 AA; 55833 MW; 66C17ECCC767E0E7 CRC64; MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCGD LMNCLHERAR IEKAYAQQLT EWARRWRQLV EKGPQYGTVE KAWIAVMSEA ERVSELHLEV KASLMNEDFE KIKNWQKEAF HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK EVEAAKKAHH TACKEEKLAI SREANSKADP SLNPEQLKKL QDKIEKCKQD VLKTKDKYEK SLKELDQTTP QYMENMEQVF EQCQQFEEKR LRFFREVLLE VQKHLDLSNV ASYKTIYREL EQSIKAADAV EDLRWFRANH GPGMAMNWPQ FEEWSADLNR TLSRREKKKA VDGVTLTGIN QTGDQSGQNK PGSNLSVPSN PAQSTQLQSS YNPFEDEDDT GSSISEKEDI KAKNVSSYEK TQTYPTDWSD DESNNPFSST DANGDSNPFD EDTTSGTEVR VRALYDYEGQ EHDELSFKAG DELTKIEDED EQGWCKGRLD SGQVGLYPAN YVEAIQ //