PACN2_MOUSE
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 03-AUG-2022, entry version 163.
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, Pancreas,
RC 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}.
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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; 14.
DR IntAct; Q9WVE8; 2.
DR MINT; Q9WVE8; -.
DR STRING; 10090.ENSMUSP00000130098; -.
DR ChEMBL; CHEMBL2176817; -.
DR iPTMnet; Q9WVE8; -.
DR PhosphoSitePlus; Q9WVE8; -.
DR EPD; Q9WVE8; -.
DR jPOST; Q9WVE8; -.
DR MaxQB; Q9WVE8; -.
DR PaxDb; Q9WVE8; -.
DR PRIDE; Q9WVE8; -.
DR ProteomicsDB; 294099; -.
DR Antibodypedia; 34964; 232 antibodies from 31 providers.
DR DNASU; 23970; -.
DR Ensembl; ENSMUST00000056177; ENSMUSP00000058320; ENSMUSG00000016664.
DR Ensembl; ENSMUST00000165095; ENSMUSP00000130098; ENSMUSG00000016664.
DR Ensembl; ENSMUST00000171436; ENSMUSP00000131504; ENSMUSG00000016664.
DR Ensembl; ENSMUST00000230679; ENSMUSP00000155481; ENSMUSG00000016664.
DR Ensembl; ENSMUST00000231184; ENSMUSP00000155334; ENSMUSG00000016664.
DR GeneID; 23970; -.
DR KEGG; mmu:23970; -.
DR UCSC; uc007xba.2; mouse.
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; MEAMAHV; -.
DR OrthoDB; 727724at2759; -.
DR PhylomeDB; Q9WVE8; -.
DR TreeFam; TF313677; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 23970; 2 hits in 71 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 248 other tissues.
DR ExpressionAtlas; Q9WVE8; baseline and differential.
DR Genevisible; Q9WVE8; MM.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
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; ISO:MGI.
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; -; 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; IPR028521; PACSIN2.
DR InterPro; IPR037453; PACSIN2_F-BAR.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF14; PTHR23065:SF14; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
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
