SH3G2_MOUSE
ID SH3G2_MOUSE Reviewed; 352 AA.
AC Q62420; Q3UTL7; Q3UY49; Q8BXS6; Q8VBV1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Endophilin-A1 {ECO:0000303|PubMed:21849472};
DE AltName: Full=Endophilin-1;
DE AltName: Full=SH3 domain protein 2A;
DE AltName: Full=SH3 domain-containing GRB2-like protein 2;
DE AltName: Full=SH3p4;
GN Name=Sh3gl2; Synonyms=Een1 {ECO:0000303|PubMed:21849472}, Sh3d2a;
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].
RC TISSUE=Embryo;
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX PubMed=11978849; DOI=10.1523/jneurosci.22-09-03730.2002;
RA Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
RT "Congenic mapping of alcohol and pentobarbital withdrawal liability loci to
RT a <1 centimorgan interval of murine chromosome 4: identification of Mpdz as
RT a candidate gene.";
RL J. Neurosci. 22:3730-3738(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Olfactory bulb, and Retina;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [6]
RP PROTEIN SEQUENCE OF 54-65; 228-239 AND 297-312, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP INTERACTION WITH ADAM9 AND ADAM15.
RX PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
RA Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
RT "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two
RT SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL J. Biol. Chem. 274:31693-31699(1999).
RN [8]
RP FUNCTION, AND INTERACTION WITH DNM1.
RX PubMed=10490020; DOI=10.1038/43613;
RA Schmidt A., Wolde M., Thiele C., Fest W., Kratzin H., Podtelejnikov A.V.,
RA Witke W., Huttner W.B., Soeling H.-D.;
RT "Endophilin I mediates synaptic vesicle formation by transfer of
RT arachidonate to lysophosphatidic acid.";
RL Nature 401:133-141(1999).
RN [9]
RP INTERACTION WITH ATXN2.
RX PubMed=18602463; DOI=10.1016/j.cellsig.2008.05.018;
RA Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J.,
RA Auburger G.;
RT "Ataxin-2 associates with the endocytosis complex and affects EGF receptor
RT trafficking.";
RL Cell. Signal. 20:1725-1739(2008).
RN [10]
RP INTERACTION WITH OPHN1.
RX PubMed=19481455; DOI=10.1016/j.cub.2009.05.022;
RA Nakano-Kobayashi A., Kasri N.N., Newey S.E., Van Aelst L.;
RT "The Rho-linked mental retardation protein OPHN1 controls synaptic vesicle
RT endocytosis via endophilin A1.";
RL Curr. Biol. 19:1133-1139(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 [12]
RP FUNCTION, INTERACTION WITH TMEM108, AND SUBCELLULAR LOCATION.
RX PubMed=21849472; DOI=10.1091/mbc.e11-04-0308;
RA Fu X., Yang Y., Xu C., Niu Y., Chen T., Zhou Q., Liu J.J.;
RT "Retrolinkin cooperates with endophilin A1 to mediate BDNF-TrkB early
RT endocytic trafficking and signaling from early endosomes.";
RL Mol. Biol. Cell 22:3684-3698(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-256, AND DOMAIN.
RX PubMed=16023669; DOI=10.1016/j.jmb.2005.06.013;
RA Weissenhorn W.;
RT "Crystal structure of the endophilin-A1 BAR domain.";
RL J. Mol. Biol. 351:653-661(2005).
RN [14]
RP INTERACTION WITH ADGRB2.
RX PubMed=28891236; DOI=10.1002/humu.23336;
RA Purcell R.H., Toro C., Gahl W.A., Hall R.A.;
RT "A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2) increases
RT receptor signaling activity.";
RL Hum. Mutat. 38:1751-1760(2017).
CC -!- FUNCTION: Implicated in synaptic vesicle endocytosis. May recruit other
CC proteins to membranes with high curvature. Required for BDNF-dependent
CC dendrite outgrowth (PubMed:21849472). Cooperates with SH3GL2 to mediate
CC BDNF-NTRK2 early endocytic trafficking and signaling from early
CC endosomes (PubMed:21849472). {ECO:0000269|PubMed:10490020,
CC ECO:0000269|PubMed:21849472}.
CC -!- SUBUNIT: Monomer; in cytoplasm. Homodimer; when associated with
CC membranes (By similarity). Interacts with SYNJ1 (By similarity).
CC Interacts with DNM1 (PubMed:10490020). Interacts with MAP4K3; the
CC interaction appears to regulate MAP4K3-mediated JNK activation (By
CC similarity). Interacts with OPHN1 (PubMed:19481455). Interacts with
CC PDCD6IP (By similarity). Interacts with BIN2 (By similarity). Interacts
CC with ATXN2 (PubMed:18602463). Interacts with ADAM9 and ADAM15
CC cytoplasmic tails (PubMed:10531379). Interacts with TMEM108
CC (PubMed:21849472). Interacts with ADGRB2 (PubMed:28891236).
CC {ECO:0000250|UniProtKB:O35179, ECO:0000250|UniProtKB:Q99962,
CC ECO:0000269|PubMed:10490020, ECO:0000269|PubMed:10531379,
CC ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:19481455,
CC ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:28891236}.
CC -!- INTERACTION:
CC Q62420; Q8K382: Dennd1a; NbExp=2; IntAct=EBI-77971, EBI-7186684;
CC Q62420; Q62420: Sh3gl2; NbExp=2; IntAct=EBI-77971, EBI-77971;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35179}.
CC Membrane {ECO:0000250|UniProtKB:O35179}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O35179}. Early endosome
CC {ECO:0000269|PubMed:21849472}. Presynapse
CC {ECO:0000250|UniProtKB:O35179}.
CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second
CC amphipathic helix inserted into helix 1 of the BAR domain (N-BAR
CC domain) induce membrane curvature and bind curved membranes (By
CC similarity). The BAR domain dimer forms a rigid crescent shaped bundle
CC of helices with the pair of second amphipathic helices protruding
CC towards the membrane-binding surface. {ECO:0000250,
CC ECO:0000269|PubMed:16023669}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have lysophosphatidic acid
CC acyltransferase activity, but has since been experimentally shown not
CC to have this activity. {ECO:0000305|PubMed:11978849}.
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DR EMBL; U58886; AAC71774.1; -; mRNA.
DR EMBL; AF326561; AAL37407.1; -; mRNA.
DR EMBL; AF326562; AAL37408.1; -; mRNA.
DR EMBL; AK044370; BAC31888.1; -; mRNA.
DR EMBL; AK134970; BAE22364.1; -; mRNA.
DR EMBL; AK139337; BAE23963.1; -; mRNA.
DR EMBL; AL805970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL806524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018385; AAH18385.1; -; mRNA.
DR CCDS; CCDS18303.1; -.
DR RefSeq; NP_062408.2; NM_019535.2.
DR PDB; 1ZWW; X-ray; 2.30 A; A/B=1-256.
DR PDBsum; 1ZWW; -.
DR AlphaFoldDB; Q62420; -.
DR BMRB; Q62420; -.
DR SMR; Q62420; -.
DR BioGRID; 203206; 24.
DR DIP; DIP-30992N; -.
DR IntAct; Q62420; 16.
DR MINT; Q62420; -.
DR STRING; 10090.ENSMUSP00000030212; -.
DR TCDB; 8.A.34.1.1; the endophilin (endophilin) family.
DR iPTMnet; Q62420; -.
DR PhosphoSitePlus; Q62420; -.
DR SwissPalm; Q62420; -.
DR jPOST; Q62420; -.
DR MaxQB; Q62420; -.
DR PaxDb; Q62420; -.
DR PRIDE; Q62420; -.
DR ProteomicsDB; 257220; -.
DR Antibodypedia; 4106; 345 antibodies from 37 providers.
DR DNASU; 20404; -.
DR Ensembl; ENSMUST00000030212; ENSMUSP00000030212; ENSMUSG00000028488.
DR GeneID; 20404; -.
DR KEGG; mmu:20404; -.
DR UCSC; uc008tlo.1; mouse.
DR CTD; 6456; -.
DR MGI; MGI:700009; Sh3gl2.
DR VEuPathDB; HostDB:ENSMUSG00000028488; -.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000160529; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q62420; -.
DR OMA; XIRQASS; -.
DR OrthoDB; 788657at2759; -.
DR TreeFam; TF313281; -.
DR Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-6807004; Negative regulation of MET activity.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 20404; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Sh3gl2; mouse.
DR EvolutionaryTrace; Q62420; -.
DR PRO; PR:Q62420; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q62420; protein.
DR Bgee; ENSMUSG00000028488; Expressed in urinary bladder urothelium and 203 other tissues.
DR ExpressionAtlas; Q62420; baseline and differential.
DR Genevisible; Q62420; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097441; C:basal dendrite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IMP:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; IMP:UniProtKB.
DR GO; GO:0060988; P:lipid tube assembly; ISO:MGI.
DR GO; GO:0097753; P:membrane bending; ISO:MGI.
DR GO; GO:0097749; P:membrane tubulation; ISO:MGI.
DR GO; GO:1905604; P:negative regulation of blood-brain barrier permeability; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; ISO:MGI.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; ISO:MGI.
DR GO; GO:0002090; P:regulation of receptor internalization; IDA:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IGI:MGI.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IGI:SynGO.
DR GO; GO:0099050; P:vesicle scission; ISO:MGI.
DR CDD; cd11803; SH3_Endophilin_A; 1.
DR DisProt; DP02819; -.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Endocytosis; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..352
FT /note="Endophilin-A1"
FT /id="PRO_0000146748"
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 290..349
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..125
FT /note="Binds and tubulates liposomes"
FT /evidence="ECO:0000250"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..21
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250"
FT REGION 60..87
FT /note="Required for dimerization upon membrane association"
FT /evidence="ECO:0000250"
FT REGION 264..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..248
FT /evidence="ECO:0000255"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62419"
FT CONFLICT 28
FT /note="K -> N (in Ref. 3; BAC31888)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="T -> K (in Ref. 3; BAE23963)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="S -> G (in Ref. 3; BAE23963)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="D -> G (in Ref. 1; AAC71774)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="F -> L (in Ref. 1; AAC71774)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="G -> A (in Ref. 1; AAC71774)"
FT /evidence="ECO:0000305"
FT HELIX 31..58
FT /evidence="ECO:0007829|PDB:1ZWW"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1ZWW"
FT HELIX 89..104
FT /evidence="ECO:0007829|PDB:1ZWW"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1ZWW"
FT HELIX 110..138
FT /evidence="ECO:0007829|PDB:1ZWW"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:1ZWW"
FT HELIX 150..173
FT /evidence="ECO:0007829|PDB:1ZWW"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:1ZWW"
FT HELIX 180..206
FT /evidence="ECO:0007829|PDB:1ZWW"
FT HELIX 209..245
FT /evidence="ECO:0007829|PDB:1ZWW"
SQ SEQUENCE 352 AA; 39955 MW; 8C2B6F0FB245DCD3 CRC64;
MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI MTKTIEYLQP
NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLAEAMLKF GRELGDDCNF GPALGEVGEA
MRELSEVKDS LDMEVKQNFI DPLQNLHDKD LREIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQALEKF DESKEIAESS MFNLLEMDIE QVSQLSALVQ AQLEYHKQAV QILQQVTVRL
EERIRQASSQ PRREYQPKPR MSLEFATGDS TQPNGGLSHT GTPKPPGVQM DQPCCRALYD
FEPENEGELG FKEGDIITLT NQIDENWYEG MLHGQSGFFP INYVEILVAL PH
