PACN1_MOUSE
ID PACN1_MOUSE Reviewed; 441 AA.
AC Q61644;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 1;
DE AltName: Full=Syndapin-1;
GN Name=Pacsin1; Synonyms=Pacsin;
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], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=9746365; DOI=10.1046/j.1432-1327.1998.2560201.x;
RA Plomann M., Lange R., Vopper G., Cremer H., Heinlein U.A.O., Scheff S.,
RA Baldwin S.A., Leitges M., Cramer M., Paulsson M., Barthels D.;
RT "PACSIN, a brain protein that is upregulated upon differentiation into
RT neuronal cells.";
RL Eur. J. Biochem. 256:201-211(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 PROTEIN SEQUENCE OF 52-62; 71-79; 319-341 AND 425-441, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION, INTERACTION WITH DNM1; SYNJ1 AND WASL, HOMOOLIGOMERIZATION,
RP HETEROOLIGOMERIZATION WITH PACSIN2 AND PACSIN3, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF PRO-434.
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 [5]
RP INTERACTION WITH EHD1.
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-345; SER-358;
RP SER-402 AND SER-427, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH DNM1; DNM2 AND DNM3,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21926968; DOI=10.1038/emboj.2011.339;
RA Koch D., Spiwoks-Becker I., Sabanov V., Sinning A., Dugladze T.,
RA Stellmacher A., Ahuja R., Grimm J., Schuler S., Muller A., Angenstein F.,
RA Ahmed T., Diesler A., Moser M., Tom Dieck S., Spessert R., Boeckers T.M.,
RA Fassler R., Hubner C.A., Balschun D., Gloveli T., Kessels M.M.,
RA Qualmann B.;
RT "Proper synaptic vesicle formation and neuronal network activity critically
RT rely on syndapin I.";
RL EMBO J. 30:4955-4969(2011).
RN [10]
RP FUNCTION, INTERACTION WITH MAPT, MUTAGENESIS OF PRO-434, AND TISSUE
RP SPECIFICITY.
RX PubMed=23035120; DOI=10.1074/jbc.m112.403451;
RA Liu Y., Lv K., Li Z., Yu A.C., Chen J., Teng J.;
RT "PACSIN1, a Tau-interacting protein, regulates axonal elongation and
RT branching by facilitating microtubule instability.";
RL J. Biol. Chem. 287:39911-39924(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-337, SUBCELLULAR LOCATION,
RP FUNCTION, SUBUNIT, INTERACTION WITH DNM1, MUTAGENESIS OF 122-ILE-MET-123;
RP LYS-127; LYS-130; 145-LYS--LYS-148 AND PRO-434, DOMAIN, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=20404169; DOI=10.1073/pnas.1003478107;
RA Rao Y., Ma Q., Vahedi-Faridi A., Sundborger A., Pechstein A., Puchkov D.,
RA Luo L., Shupliakov O., Saenger W., Haucke V.;
RT "Molecular basis for SH3 domain regulation of F-BAR-mediated membrane
RT deformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8213-8218(2010).
CC -!- FUNCTION: Binds to membranes via its F-BAR domain and mediates membrane
CC tubulation. Plays a role in the reorganization of the microtubule
CC cytoskeleton via its interaction with MAPT; this decreases microtubule
CC stability and inhibits MAPT-induced microtubule polymerization. Plays a
CC role in cellular transport processes by recruiting DNM1, DNM2 and DNM3
CC to membranes. Plays a role in the reorganization of the actin
CC cytoskeleton and in neuron morphogenesis via its interaction with COBL
CC and WASL, and by recruiting COBL to the cell cortex. Plays a role in
CC the regulation of neurite formation, neurite branching and the
CC regulation of neurite length. Required for normal synaptic vesicle
CC endocytosis; this process retrieves previously released
CC neurotransmitters to accommodate multiple cycles of neurotransmission.
CC Required for normal excitatory and inhibitory synaptic transmission.
CC {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:20404169,
CC ECO:0000269|PubMed:21926968, ECO:0000269|PubMed:23035120}.
CC -!- SUBUNIT: Homodimer. May form heterooligomers with other PACSINs.
CC Interacts with both COBL and DBNL. Identified in a complex composed of
CC COBL, PACSIN1 and WASL. Interacts with EHD3 (By similarity). Interacts
CC (via SH3 domain) with SYNJ1 and WASL. Interacts (via SH3 domain) with
CC DNM1; the interaction is reduced by DNM1 phosphorylation. Interacts
CC with DNM2 and DNM3. Interacts with MAPT. Interacts with EHD1. Interacts
CC with TRPV4. {ECO:0000250, ECO:0000269|PubMed:11082044,
CC ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:16627472,
CC ECO:0000269|PubMed:20404169, ECO:0000269|PubMed:21926968,
CC ECO:0000269|PubMed:23035120}.
CC -!- INTERACTION:
CC Q61644; P10637: Mapt; NbExp=5; IntAct=EBI-2255561, EBI-774043;
CC Q61644; Q61644: Pacsin1; NbExp=3; IntAct=EBI-2255561, EBI-2255561;
CC Q61644; P19332-5: Mapt; Xeno; NbExp=6; IntAct=EBI-2255561, EBI-8758676;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection {ECO:0000250}.
CC Synapse, synaptosome {ECO:0000250}. Cell projection, ruffle membrane.
CC Membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane;
CC Peripheral membrane protein. Synapse. Cytoplasm, cytosol. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=In primary neuronal cultures, present at a
CC high level in presynaptic nerve terminals and in the cell body.
CC Colocalizes with DNM1 at vesicular structures in the cell body and
CC neurites (By similarity). Colocalizes with MAPT in axons.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Detected in hippocampus
CC and dorsal root ganglion neurons. Detected in rod photoreceptor
CC terminals in the outer plexiform layer of the retina (at protein
CC level). In CNS neurons, high levels in the pyramidal cells of the
CC hippocampus, Purkinje cells of the cerebellum and large neurons of the
CC cortex and brain stem. {ECO:0000269|PubMed:11082044,
CC ECO:0000269|PubMed:21926968, ECO:0000269|PubMed:23035120,
CC ECO:0000269|PubMed:9746365}.
CC -!- DEVELOPMENTAL STAGE: Expression is seen at embryonic day 17 and is up-
CC regulated developmentally with a correlation to neuronal
CC differentiation.
CC -!- DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-
CC binding and membrane tubulation. In the autoinhibited conformation,
CC interaction with the SH3 domain inhibits membrane tubulation mediated
CC by the F-BAR domain. DNM1 binding abolishes autoinhibition.
CC {ECO:0000269|PubMed:20404169}.
CC -!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
CC (PKC).
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate, but
CC display a slightly reduced body weight and reduced fertility. Mice
CC display increased synaptic vesicle diameter and impaired compensatory
CC synaptic vesicle endocytosis after high synapse activity. Rod
CC photoreceptor ribbon synapses display an abnormally high number of
CC endosome-like structures and tubular elements after light exposure.
CC Mice display defects in excitatory and inhibitory synaptic transmission
CC in the hippocampus, and display a tendency to seizures when confronted
CC with novelty. {ECO:0000269|PubMed:21926968}.
CC -!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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DR EMBL; X85124; CAA59437.1; -; mRNA.
DR EMBL; BC014698; AAH14698.1; -; mRNA.
DR CCDS; CCDS28567.1; -.
DR RefSeq; NP_001273672.1; NM_001286743.1.
DR RefSeq; NP_001273673.1; NM_001286744.1.
DR RefSeq; NP_035991.1; NM_011861.3.
DR RefSeq; NP_848142.1; NM_178365.4.
DR RefSeq; XP_006524289.1; XM_006524226.3.
DR RefSeq; XP_011244733.1; XM_011246431.2.
DR PDB; 2X3V; X-ray; 2.45 A; A/B/C=1-337.
DR PDB; 2X3W; X-ray; 2.64 A; A/B/C=1-337, D=382-441.
DR PDB; 2X3X; X-ray; 3.35 A; A/B/C=1-337, D/E=382-441.
DR PDBsum; 2X3V; -.
DR PDBsum; 2X3W; -.
DR PDBsum; 2X3X; -.
DR AlphaFoldDB; Q61644; -.
DR SMR; Q61644; -.
DR BioGRID; 204830; 16.
DR DIP; DIP-53108N; -.
DR IntAct; Q61644; 12.
DR MINT; Q61644; -.
DR STRING; 10090.ENSMUSP00000044168; -.
DR iPTMnet; Q61644; -.
DR PhosphoSitePlus; Q61644; -.
DR UCD-2DPAGE; Q61644; -.
DR MaxQB; Q61644; -.
DR PaxDb; Q61644; -.
DR PRIDE; Q61644; -.
DR ProteomicsDB; 294098; -.
DR Antibodypedia; 4091; 264 antibodies from 34 providers.
DR DNASU; 23969; -.
DR Ensembl; ENSMUST00000045896; ENSMUSP00000044168; ENSMUSG00000040276.
DR Ensembl; ENSMUST00000097360; ENSMUSP00000094973; ENSMUSG00000040276.
DR Ensembl; ENSMUST00000114873; ENSMUSP00000110523; ENSMUSG00000040276.
DR Ensembl; ENSMUST00000231669; ENSMUSP00000156003; ENSMUSG00000040276.
DR Ensembl; ENSMUST00000232437; ENSMUSP00000155999; ENSMUSG00000040276.
DR GeneID; 23969; -.
DR KEGG; mmu:23969; -.
DR UCSC; uc008bpj.2; mouse.
DR CTD; 29993; -.
DR MGI; MGI:1345181; Pacsin1.
DR VEuPathDB; HostDB:ENSMUSG00000040276; -.
DR eggNOG; KOG2856; Eukaryota.
DR GeneTree; ENSGT00950000182973; -.
DR HOGENOM; CLU_030752_0_0_1; -.
DR InParanoid; Q61644; -.
DR OMA; WAAIMTE; -.
DR OrthoDB; 727724at2759; -.
DR PhylomeDB; Q61644; -.
DR TreeFam; TF313677; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 23969; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pacsin1; mouse.
DR EvolutionaryTrace; Q61644; -.
DR PRO; PR:Q61644; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q61644; protein.
DR Bgee; ENSMUSG00000040276; Expressed in pontine nuclear group and 143 other tissues.
DR ExpressionAtlas; Q61644; baseline and differential.
DR Genevisible; Q61644; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR GO; GO:0098833; C:presynaptic endocytic zone; IDA:SynGO.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0045806; P:negative regulation of endocytosis; IDA:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; IMP:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0072657; P:protein localization to membrane; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR CDD; cd07680; F-BAR_PACSIN1; 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; IPR028518; PACSIN1.
DR InterPro; IPR035743; PACSIN1/PACSIN2_SH3.
DR InterPro; IPR037454; PACSIN1_F-BAR.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF16; PTHR23065:SF16; 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; 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; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Endocytosis; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; SH3 domain; Synapse;
KW Synaptosome.
FT CHAIN 1..441
FT /note="Protein kinase C and casein kinase substrate in
FT neurons protein 1"
FT /id="PRO_0000161793"
FT DOMAIN 10..280
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 382..441
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 297..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..272
FT COMPBIAS 306..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0W5"
FT MOD_RES 391
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 122..123
FT /note="IM->FF: Increases membrane tubulation."
FT /evidence="ECO:0000269|PubMed:20404169"
FT MUTAGEN 122..123
FT /note="IM->QQ: Abolishes membrane tubulation. No effect on
FT phospholipid binding."
FT /evidence="ECO:0000269|PubMed:20404169"
FT MUTAGEN 127
FT /note="K->E: Abolishes membrane tubulation; when associated
FT with E-130."
FT /evidence="ECO:0000269|PubMed:20404169"
FT MUTAGEN 130
FT /note="K->E: Abolishes membrane tubulation; when associated
FT with E-127."
FT /evidence="ECO:0000269|PubMed:20404169"
FT MUTAGEN 145..148
FT /note="KKMK->EEME: Abolishes membrane tubulation."
FT /evidence="ECO:0000269|PubMed:20404169"
FT MUTAGEN 400
FT /note="E->R: Impairs interaction with DNM1."
FT MUTAGEN 434
FT /note="P->L: Abolishes interaction with DNM1, MAPT, SYNJ1
FT and WASL."
FT /evidence="ECO:0000269|PubMed:11082044,
FT ECO:0000269|PubMed:20404169, ECO:0000269|PubMed:23035120"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:2X3V"
FT HELIX 23..70
FT /evidence="ECO:0007829|PDB:2X3V"
FT HELIX 75..104
FT /evidence="ECO:0007829|PDB:2X3V"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:2X3V"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2X3W"
FT HELIX 127..175
FT /evidence="ECO:0007829|PDB:2X3V"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2X3V"
FT HELIX 182..253
FT /evidence="ECO:0007829|PDB:2X3V"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2X3V"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:2X3V"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:2X3V"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:2X3W"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:2X3W"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2X3W"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:2X3W"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:2X3W"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:2X3W"
SQ SEQUENCE 441 AA; 50575 MW; 21BEB339A14A41F9 CRC64;
MSGSYDEASE EITDSFWEVG NYKRTVKRID DGHRLCNDLM SCVQERAKIE KAYAQQLTDW
AKRWRQLIEK GPQYGSLERA WGAMMTEADK VSELHQEVKN SLLNEDLEKV KNWQKDAYHK
QIMGGFKETK EAEDGFRKAQ KPWAKKMKEL EAAKKAYHLA CKEERLAMTR EMNSKTEQSV
TPEQQKKLVD KVDKCRQDVQ KTQEKYEKVL EDVGKTTPQY MEGMEQVFEQ CQQFEEKRLV
FLKEVLLDIK RHLNLAENSS YMHVYRELEQ AIRGADAQED LRWFRSTSGP GMPMNWPQFE
EWNPDLPHTT AKKEKQPKKA EGATLSNATG AVESTSQAGD RGSVSSYDRG QTYATEWSDD
ESGNPFGGNE ANGGANPFED DAKGVRVRAL YDYDGQEQDE LSFKAGDELT KLGEEDEQGW
CRGRLDSGQL GLYPANYVEA I
