AP2B1_MOUSE
ID AP2B1_MOUSE Reviewed; 937 AA.
AC Q9DBG3; Q80XJ4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=AP-2 complex subunit beta;
DE AltName: Full=AP105B;
DE AltName: Full=Adaptor protein complex AP-2 subunit beta;
DE AltName: Full=Adaptor-related protein complex 2 subunit beta;
DE AltName: Full=Beta-2-adaptin;
DE AltName: Full=Beta-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 beta large chain;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin beta subunit;
GN Name=Ap2b1; Synonyms=Clapb1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
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 [4]
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 [5]
RP IDENTIFICATION BY 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 [6]
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).
RN [7]
RP INTERACTION WITH KIAA1107.
RX PubMed=29262337; DOI=10.1016/j.celrep.2017.11.073;
RA Piccini A., Castroflorio E., Valente P., Guarnieri F.C., Aprile D.,
RA Michetti C., Bramini M., Giansante G., Pinto B., Savardi A., Cesca F.,
RA Bachi A., Cattaneo A., Wren J.D., Fassio A., Valtorta F., Benfenati F.,
RA Giovedi S.;
RT "APache is an AP2-interacting protein involved in synaptic vesicle
RT trafficking and neuronal development.";
RL Cell Rep. 21:3596-3611(2017).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC protein complexes function in protein transport via transport vesicles
CC in different membrane traffic pathways. Adaptor protein complexes are
CC vesicle coat components and appear to be involved in cargo selection
CC and vesicle formation. AP-2 is involved in clathrin-dependent
CC endocytosis in which cargo proteins are incorporated into vesicles
CC surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC destined for fusion with the early endosome. The clathrin lattice
CC serves as a mechanical scaffold but is itself unable to bind directly
CC to membrane components. Clathrin-associated adaptor protein (AP)
CC complexes which can bind directly to both the clathrin lattice and to
CC the lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane proteins
CC involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC the recycling of synaptic vesicle membranes from the presynaptic
CC surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC [LI] endocytosis signal motifs within the cytosolic tails of
CC transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC normal post-endocytic trafficking through the ARF6-regulated, non-
CC clathrin pathway. During long-term potentiation in hippocampal neurons,
CC AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497).
CC The AP-2 beta subunit acts via its C-terminal appendage domain as a
CC scaffolding platform for endocytic accessory proteins; at least some
CC clathrin-associated sorting proteins (CLASPs) are recognized by their
CC [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to
CC clathrin heavy chain, promoting clathrin lattice assembly; clathrin
CC displaces at least some CLASPs from AP2B1 which probably then can be
CC positioned for further coat assembly (By similarity). {ECO:0000250,
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 EPN1
CC (By similarity). Interacts with EPS15; clathrin competes with EPS15 (By
CC similarity). Interacts with SNAP91; clathrin competes with SNAP91 (By
CC similarity). Interacts with CLTC; clathrin competes with EPS15, SNAP91
CC and PIP5K1C (By similarity). Interacts with LDLRAP1 (By similarity).
CC Interacts with AMPH and BIN1 (By similarity). Interacts with ARF6 (GDP-
CC bound) (By similarity). Interacts (dephosphorylated at Tyr-737) with
CC ARRB1; phosphorylation of AP2B1 at Tyr-737 disrupts the interaction (By
CC similarity). Interacts with SLC2A8 (By similarity). Interacts with
CC SCYL1 and SCYL2. Interacts with TGFBR1 and TGFBR2 (By similarity).
CC Interacts with PIP5K1C; clathrin competes with PIP5K1C (By similarity).
CC Interacts with DENND1B (By similarity). Interacts with FCHO1 (By
CC similarity). Interacts with RFTN1 (By similarity). Interacts with
CC KIAA1107 (PubMed:29262337). Together with AP2A1 or AP2A2 and AP2M1, it
CC interacts with ADAM10; this interaction facilitates ADAM10 endocytosis
CC from the plasma membrane during long-term potentiation in hippocampal
CC neurons (PubMed:23676497). {ECO:0000250|UniProtKB:P62944,
CC ECO:0000250|UniProtKB:P63010, ECO:0000269|PubMed:23676497,
CC ECO:0000269|PubMed:29262337}.
CC -!- INTERACTION:
CC Q9DBG3; Q64729: Tgfbr1; NbExp=2; IntAct=EBI-775229, EBI-2899393;
CC Q9DBG3; P48023: FASLG; Xeno; NbExp=2; IntAct=EBI-775229, EBI-495538;
CC Q9DBG3-1; O70161: Pip5k1c; NbExp=3; IntAct=EBI-775239, EBI-773657;
CC Q9DBG3-2; O70161: Pip5k1c; NbExp=8; IntAct=EBI-7257021, EBI-773657;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=AP-2 appears to be excluded from internalizing
CC CCVs and to disengage from sites of endocytosis seconds before
CC internalization of the nascent CCV. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DBG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBG3-2; Sequence=VSP_011491;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:23676497}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; AK004975; BAB23711.1; -; mRNA.
DR EMBL; BC046772; AAH46772.1; -; mRNA.
DR CCDS; CCDS25161.1; -. [Q9DBG3-2]
DR CCDS; CCDS25162.1; -. [Q9DBG3-1]
DR RefSeq; NP_001030931.1; NM_001035854.2. [Q9DBG3-2]
DR RefSeq; NP_082191.1; NM_027915.3. [Q9DBG3-1]
DR RefSeq; XP_006534321.1; XM_006534258.3. [Q9DBG3-2]
DR RefSeq; XP_017170261.1; XM_017314772.1. [Q9DBG3-2]
DR PDB; 6OWO; EM; 3.20 A; B=1-591.
DR PDB; 6OXL; EM; 3.50 A; B=1-591.
DR PDB; 7RW8; EM; 3.50 A; B=1-591.
DR PDB; 7RW9; EM; 3.90 A; B=1-591.
DR PDB; 7RWA; EM; 4.70 A; B/b=1-591.
DR PDB; 7RWB; EM; 3.90 A; B/b=1-591.
DR PDB; 7RWC; EM; 3.80 A; B=1-591.
DR PDBsum; 6OWO; -.
DR PDBsum; 6OXL; -.
DR PDBsum; 7RW8; -.
DR PDBsum; 7RW9; -.
DR PDBsum; 7RWA; -.
DR PDBsum; 7RWB; -.
DR PDBsum; 7RWC; -.
DR AlphaFoldDB; Q9DBG3; -.
DR SMR; Q9DBG3; -.
DR BioGRID; 214914; 46.
DR ComplexPortal; CPX-5152; AP-2 Adaptor complex, alpha1 variant.
DR ComplexPortal; CPX-5153; AP-2 Adaptor complex, alpha2 variant.
DR DIP; DIP-32161N; -.
DR IntAct; Q9DBG3; 13.
DR MINT; Q9DBG3; -.
DR STRING; 10090.ENSMUSP00000018875; -.
DR iPTMnet; Q9DBG3; -.
DR PhosphoSitePlus; Q9DBG3; -.
DR SwissPalm; Q9DBG3; -.
DR EPD; Q9DBG3; -.
DR jPOST; Q9DBG3; -.
DR MaxQB; Q9DBG3; -.
DR PaxDb; Q9DBG3; -.
DR PRIDE; Q9DBG3; -.
DR ProteomicsDB; 296208; -. [Q9DBG3-1]
DR ProteomicsDB; 296209; -. [Q9DBG3-2]
DR Antibodypedia; 4320; 267 antibodies from 30 providers.
DR DNASU; 71770; -.
DR Ensembl; ENSMUST00000018875; ENSMUSP00000018875; ENSMUSG00000035152. [Q9DBG3-2]
DR Ensembl; ENSMUST00000065692; ENSMUSP00000070714; ENSMUSG00000035152. [Q9DBG3-1]
DR GeneID; 71770; -.
DR KEGG; mmu:71770; -.
DR UCSC; uc007kor.1; mouse. [Q9DBG3-1]
DR CTD; 163; -.
DR MGI; MGI:1919020; Ap2b1.
DR VEuPathDB; HostDB:ENSMUSG00000035152; -.
DR eggNOG; KOG1061; Eukaryota.
DR GeneTree; ENSGT00940000155206; -.
DR HOGENOM; CLU_006320_1_1_1; -.
DR InParanoid; Q9DBG3; -.
DR OMA; ASIYHKS; -.
DR TreeFam; TF300318; -.
DR Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
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; 71770; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Ap2b1; mouse.
DR PRO; PR:Q9DBG3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DBG3; protein.
DR Bgee; ENSMUSG00000035152; Expressed in spermatid and 261 other tissues.
DR ExpressionAtlas; Q9DBG3; baseline and differential.
DR Genevisible; Q9DBG3; MM.
DR GO; GO:0030122; C:AP-2 adaptor complex; IDA:UniProtKB.
DR GO; GO:0030131; C:clathrin adaptor complex; ISO:MGI.
DR GO; GO:0030118; C:clathrin coat; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0048268; P:clathrin coat assembly; ISO:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:UniProtKB.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0099590; P:neurotransmitter receptor internalization; IMP:SynGO.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; ISO:MGI.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1150; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF09066; B2-adapt-app_C; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM00185; ARM; 2.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Coated pit;
KW Endocytosis; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT CHAIN 2..937
FT /note="AP-2 complex subunit beta"
FT /id="PRO_0000193743"
FT REGION 593..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT MOD_RES 737
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT MOD_RES 928
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62944"
FT VAR_SEQ 663
FT /note="L -> LLGSDLGGGIGGSPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011491"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6OXL"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 296..312
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:6OXL"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:6OXL"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 442..453
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 454..458
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6OXL"
FT HELIX 478..494
FT /evidence="ECO:0007829|PDB:6OWO"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 517..532
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 534..541
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 557..564
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 570..574
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:6OWO"
SQ SEQUENCE 937 AA; 104583 MW; 452DF0AE91EDB0AE CRC64;
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST
DAGDSPVGTT TTTNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL
DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI GMAPGGYVAP KAVWLPAVKA
KGLEISGTFT HRQGHIYMEM NFTNKALQHM TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ
SIDVSLPLNT LGPVMKMEPL NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT
WKDIPNENEL QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN
