AP2M1_MOUSE
ID AP2M1_MOUSE Reviewed; 435 AA.
AC P84091; P20172; P53679;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=AP-2 complex subunit mu;
DE AltName: Full=AP-2 mu chain;
DE AltName: Full=Adaptor protein complex AP-2 subunit mu;
DE AltName: Full=Adaptor-related protein complex 2 subunit mu;
DE AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
DE AltName: Full=Clathrin coat assembly protein AP50;
DE AltName: Full=Clathrin coat-associated protein AP50;
DE AltName: Full=Mu2-adaptin;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN Name=Ap2m1; Synonyms=Clapm1;
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 STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=7569928; DOI=10.1126/science.7569928;
RA Ohno H., Stewart J., Fournier M.C., Bosshart H., Rhee I.R., Miyatake S.,
RA Saito T., Gallusser A., Kirchhausen T., Bonifacino J.S.;
RT "Interaction of tyrosine-based sorting signals with clathrin-associated
RT proteins.";
RL Science 269:1872-1875(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=9573360; DOI=10.1016/s0378-1119(97)00649-5;
RA Ohno H., Poy G., Bonifacino J.S.;
RT "Cloning of the gene encoding the murine clathrin-associated adaptor medium
RT chain mu 2: gene organization, alternative splicing and chromosomal
RT assignment.";
RL Gene 210:187-193(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PROTEIN SEQUENCE OF 61-70; 131-139 AND 282-288, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH RALBP1.
RX PubMed=10910768; DOI=10.1242/jcs.113.16.2837;
RA Jullien-Flores V., Mahe Y., Mirey G., Leprince C., Meunier-Bisceuil B.,
RA Sorkin A., Camonis J.H.;
RT "RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex:
RT involvement of the Ral pathway in receptor endocytosis.";
RL J. Cell Sci. 113:2837-2844(2000).
RN [6]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in the
RT post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [7]
RP SUBCELLULAR LOCATION OF THE AP-2 COMPLEX.
RX PubMed=14530274; DOI=10.1074/jbc.c300390200;
RA Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M.;
RT "The AP-2 complex is excluded from the dynamic population of plasma
RT membrane-associated clathrin.";
RL J. Biol. Chem. 278:47357-47360(2003).
RN [8]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=16227583; DOI=10.1128/mcb.25.21.9318-9323.2005;
RA Mitsunari T., Nakatsu F., Shioda N., Love P.E., Grinberg A.,
RA Bonifacino J.S., Ohno H.;
RT "Clathrin adaptor AP-2 is essential for early embryonal development.";
RL Mol. Cell. Biol. 25:9318-9323(2005).
RN [10]
RP INTERACTION WITH PIP5K1C.
RX PubMed=16707488; DOI=10.1074/jbc.m601465200;
RA Bairstow S.F., Ling K., Su X., Firestone A.J., Carbonara C., Anderson R.A.;
RT "Type Igamma661 phosphatidylinositol phosphate kinase directly interacts
RT with AP2 and regulates endocytosis.";
RL J. Biol. Chem. 281:20632-20642(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156, 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 [12]
RP FUNCTION, INTERACTION WITH ADAM10, AND TISSUE SPECIFICITY.
RX PubMed=23676497; DOI=10.1172/jci65401;
RA Marcello E., Saraceno C., Musardo S., Vara H., de la Fuente A.G.,
RA Pelucchi S., Di Marino D., Borroni B., Tramontano A., Perez-Otano I.,
RA Padovani A., Giustetto M., Gardoni F., Di Luca M.;
RT "Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's
RT disease.";
RL J. Clin. Invest. 123:2523-2538(2013).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2)
CC (PubMed:14745134, PubMed:15473838). Adaptor protein complexes function
CC in protein transport via transport vesicles in different membrane
CC traffic pathways (PubMed:14745134, PubMed:15473838). Adaptor protein
CC complexes are vesicle coat components and appear to be involved in
CC cargo selection and vesicle formation (PubMed:14745134,
CC PubMed:15473838). AP-2 is involved in clathrin-dependent endocytosis in
CC which cargo proteins are incorporated into vesicles surrounded by
CC clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion
CC with the early endosome (PubMed:14745134, PubMed:15473838). The
CC clathrin lattice serves as a mechanical scaffold but is itself unable
CC to bind directly to membrane components (PubMed:14745134,
CC PubMed:15473838). Clathrin-associated adaptor protein (AP) complexes
CC which can bind directly to both the clathrin lattice and to the lipid
CC and protein components of membranes are considered to be the major
CC clathrin adaptors contributing the CCV formation (By similarity). AP-2
CC also serves as a cargo receptor to selectively sort the membrane
CC proteins involved in receptor-mediated endocytosis (By similarity). AP-
CC 2 seems to play a role in the recycling of synaptic vesicle membranes
CC from the presynaptic surface (By similarity). AP-2 recognizes Y-X-X-
CC [FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs
CC within the cytosolic tails of transmembrane cargo molecules (By
CC similarity). AP-2 may also play a role in maintaining normal post-
CC endocytic trafficking through the ARF6-regulated, non-clathrin pathway
CC (By similarity). During long-term potentiation in hippocampal neurons,
CC AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497).
CC The AP-2 mu subunit binds to transmembrane cargo proteins; it
CC recognizes the Y-X-X-Phi motifs (By similarity). The surface region
CC interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic
CC AP-2, but becomes accessible through a conformational change following
CC phosphorylation of AP-2 mu subunit at Thr-156 in membrane-associated
CC AP-2 (By similarity). The membrane-specific phosphorylation event
CC appears to involve assembled clathrin which activates the AP-2 mu
CC kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled
CC family members upon Wnt signaling (By similarity).
CC {ECO:0000250|UniProtKB:P84092, ECO:0000250|UniProtKB:Q96CW1,
CC ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838,
CC ECO:0000269|PubMed:23676497}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type
CC subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC adaptin (sigma-type subunit AP2S1) (By similarity). Interacts with
CC ATP6V1H and MEGF10 (By similarity). Interacts with EGFR and TTGN1 (By
CC similarity). Interacts with F2R (By similarity). Interacts with PIP5K1C
CC isoform 1; tyrosine phosphorylation of PIP5K1C weakens the interaction.
CC Does not interact with PIP5K1C isoform 3 (PubMed:16707488). Interacts
CC with KIAA0319; required for clathrin-mediated endocytosis of KIAA0319
CC (By similarity). Interacts with DVL2 (via DEP domain) (By similarity).
CC Interacts with KCNQ1; mediates estrogen-induced internalization via
CC clathrin-coated vesicles (By similarity). Interacts with P2RX4 (via
CC internalization motif) (By similarity). Together with AP2A1 or AP2A2
CC and AP2B1, it interacts with ADAM10; this interaction facilitates
CC ADAM10 endocytosis from the plasma membrane during long-term
CC potentiation in hippocampal neurons (PubMed:23676497). Probably
CC interacts with ACE2 (via endocytic sorting signal motif); the
CC interaction is inhibited by ACE2 phosphorylation (By similarity).
CC Interacts with RALBP1; the interaction is direct (PubMed:10910768).
CC {ECO:0000250|UniProtKB:P84092, ECO:0000250|UniProtKB:Q96CW1,
CC ECO:0000269|PubMed:10910768, ECO:0000269|PubMed:16707488,
CC ECO:0000269|PubMed:23676497}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96CW1}.
CC Membrane, coated pit {ECO:0000250|UniProtKB:Q96CW1}; Peripheral
CC membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded
CC from internalizing CCVs and to disengage from sites of endocytosis
CC seconds before internalization of the nascent CCV.
CC {ECO:0000305|PubMed:14530274}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:23676497). Detected in spleen. {ECO:0000269|PubMed:23676497}.
CC -!- PTM: Phosphorylation at Thr-156 increases the affinity of the AP-2
CC complex for cargo membrane proteins during the initial stages of
CC endocytosis. {ECO:0000250|UniProtKB:Q96CW1}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal before day 3.5 postcoitus
CC (E3.5). {ECO:0000269|PubMed:16227583}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; U27106; AAC53158.1; -; mRNA.
DR EMBL; AF001923; AAC53583.1; -; Genomic_DNA.
DR EMBL; AF001913; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001914; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001915; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001916; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001917; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001918; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001919; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001920; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001921; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; AF001922; AAC53583.1; JOINED; Genomic_DNA.
DR EMBL; BC056352; AAH56352.1; -; mRNA.
DR CCDS; CCDS28048.1; -.
DR PIR; I49327; I49327.
DR PIR; JC6563; JC6563.
DR RefSeq; NP_033809.1; NM_009679.3.
DR PDB; 6OWO; EM; 3.20 A; M=1-435.
DR PDB; 6OWT; EM; 3.80 A; M=1-141.
DR PDB; 6OXL; EM; 3.50 A; M=1-435.
DR PDB; 7RW8; EM; 3.50 A; M=1-435.
DR PDB; 7RW9; EM; 3.90 A; M=1-435.
DR PDB; 7RWA; EM; 4.70 A; M/m=1-435.
DR PDB; 7RWB; EM; 3.90 A; M/m=1-435.
DR PDB; 7RWC; EM; 3.80 A; M=1-435.
DR PDBsum; 6OWO; -.
DR PDBsum; 6OWT; -.
DR PDBsum; 6OXL; -.
DR PDBsum; 7RW8; -.
DR PDBsum; 7RW9; -.
DR PDBsum; 7RWA; -.
DR PDBsum; 7RWB; -.
DR PDBsum; 7RWC; -.
DR AlphaFoldDB; P84091; -.
DR SMR; P84091; -.
DR BioGRID; 198131; 35.
DR ComplexPortal; CPX-5152; AP-2 Adaptor complex, alpha1 variant.
DR ComplexPortal; CPX-5153; AP-2 Adaptor complex, alpha2 variant.
DR IntAct; P84091; 5.
DR STRING; 10090.ENSMUSP00000007216; -.
DR iPTMnet; P84091; -.
DR PhosphoSitePlus; P84091; -.
DR SwissPalm; P84091; -.
DR EPD; P84091; -.
DR jPOST; P84091; -.
DR PaxDb; P84091; -.
DR PeptideAtlas; P84091; -.
DR PRIDE; P84091; -.
DR ProteomicsDB; 281786; -.
DR Antibodypedia; 33793; 569 antibodies from 35 providers.
DR DNASU; 11773; -.
DR Ensembl; ENSMUST00000007216; ENSMUSP00000007216; ENSMUSG00000022841.
DR GeneID; 11773; -.
DR KEGG; mmu:11773; -.
DR UCSC; uc007ypy.2; mouse.
DR CTD; 1173; -.
DR MGI; MGI:1298405; Ap2m1.
DR VEuPathDB; HostDB:ENSMUSG00000022841; -.
DR eggNOG; KOG0938; Eukaryota.
DR GeneTree; ENSGT00940000159223; -.
DR InParanoid; P84091; -.
DR OMA; VWKIPRI; -.
DR OrthoDB; 725236at2759; -.
DR PhylomeDB; P84091; -.
DR TreeFam; TF300722; -.
DR Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
DR Reactome; R-MMU-8964038; LDL clearance.
DR BioGRID-ORCS; 11773; 23 hits in 78 CRISPR screens.
DR ChiTaRS; Ap2m1; mouse.
DR PRO; PR:P84091; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P84091; protein.
DR Bgee; ENSMUSG00000022841; Expressed in primary visual cortex and 124 other tissues.
DR ExpressionAtlas; P84091; baseline and differential.
DR Genevisible; P84091; MM.
DR GO; GO:0030122; C:AP-2 adaptor complex; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030141; C:secretory granule; TAS:MGI.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0097718; F:disordered domain specific binding; IDA:CAFA.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0005048; F:signal sequence binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:MGI.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0097494; P:regulation of vesicle size; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0006900; P:vesicle budding from membrane; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd09251; AP-2_Mu2_Cterm; 1.
DR CDD; cd14836; AP2_Mu_N; 1.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR043532; AP2_Mu_N.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR043512; Mu2_C.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coated pit; Direct protein sequencing;
KW Endocytosis; Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..435
FT /note="AP-2 complex subunit mu"
FT /id="PRO_0000193775"
FT DOMAIN 170..434
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT BINDING 341
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250|UniProtKB:P84092"
FT BINDING 345
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250|UniProtKB:P84092"
FT BINDING 354
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250|UniProtKB:P84092"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CW1"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 75..93
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 172..185
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 191..205
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 269..279
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 315..325
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 330..345
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 350..361
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 418..433
FT /evidence="ECO:0007829|PDB:6OWO"
SQ SEQUENCE 435 AA; 49655 MW; 82803219BA279954 CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMA AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKS QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETSKSGKQS
IAIDDCTFHQ CVRLSKFDSE RSISFIPPDG EFELMRYRTT KDIILPFRVI PLVREVGRTK
LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA IVWKIKRMAG
MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK
WVRYIGRSGI YETRC
