VPS29_MOUSE
ID VPS29_MOUSE Reviewed; 182 AA.
AC Q9QZ88; Q3UCZ0; Q9D107;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Vacuolar protein sorting-associated protein 29;
DE AltName: Full=Vesicle protein sorting 29;
GN Name=Vps29;
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] (ISOFORM 1).
RC TISSUE=Lung;
RA Edgar A.J.;
RT "Molecular cloning of mouse vacuolar sorting protein VPS29.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 1-14, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP SUBUNIT.
RX PubMed=21040701; DOI=10.1016/j.bbrc.2010.10.121;
RA Kim E., Lee Y., Lee H.J., Kim J.S., Song B.S., Huh J.W., Lee S.R.,
RA Kim S.U., Kim S.H., Hong Y., Shim I., Chang K.T.;
RT "Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin
RT trafficking.";
RL Biochem. Biophys. Res. Commun. 403:167-171(2010).
RN [6]
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 [7]
RP FUNCTION, LACK OF PHOSPHATASE ACTIVITY, AND INTERACTION WITH SNX1.
RX PubMed=21629666; DOI=10.1371/journal.pone.0020420;
RA Swarbrick J.D., Shaw D.J., Chhabra S., Ghai R., Valkov E., Norwood S.J.,
RA Seaman M.N., Collins B.M.;
RT "VPS29 is not an active metallo-phosphatase but is a rigid scaffold
RT required for retromer interaction with accessory proteins.";
RL PLoS ONE 6:E20420-E20420(2011).
RN [8]
RP SUBUNIT.
RX PubMed=20875039; DOI=10.1111/j.1600-0854.2010.01124.x;
RA Norwood S.J., Shaw D.J., Cowieson N.P., Owen D.J., Teasdale R.D.,
RA Collins B.M.;
RT "Assembly and solution structure of the core retromer protein complex.";
RL Traffic 12:56-71(2011).
RN [9]
RP SUBUNIT.
RX PubMed=21920005; DOI=10.1111/j.1600-0854.2011.01284.x;
RA Bugarcic A., Zhe Y., Kerr M.C., Griffin J., Collins B.M., Teasdale R.D.;
RT "Vps26A and Vps26B subunits define distinct retromer complexes.";
RL Traffic 12:1759-1773(2011).
RN [10]
RP INTERACTION WITH ANKRD27, AND MUTAGENESIS OF LEU-152.
RX PubMed=24856514; DOI=10.1016/j.devcel.2014.04.010;
RA Hesketh G.G., Perez-Dorado I., Jackson L.P., Wartosch L., Schafer I.B.,
RA Gray S.R., McCoy A.J., Zeldin O.B., Garman E.F., Harbour M.E., Evans P.R.,
RA Seaman M.N., Luzio J.P., Owen D.J.;
RT "VARP is recruited on to endosomes by direct interaction with retromer,
RT where together they function in export to the cell surface.";
RL Dev. Cell 29:591-606(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS,
RP ABSENCE OF CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, AND
RP MUTAGENESIS OF ASN-39; VAL-90 AND ILE-91.
RX PubMed=15965486; DOI=10.1038/nsmb954;
RA Collins B.M., Skinner C.F., Watson P.J., Seaman M.N., Owen D.J.;
RT "Vps29 has a phosphoesterase fold that acts as a protein interaction
RT scaffold for retromer assembly.";
RL Nat. Struct. Mol. Biol. 12:594-602(2005).
CC -!- FUNCTION: Acts as component of the retromer cargo-selective complex
CC (CSC). The CSC is believed to be the core functional component of
CC retromer or respective retromer complex variants acting to prevent
CC missorting of selected transmembrane cargo proteins into the lysosomal
CC degradation pathway. The recruitment of the CSC to the endosomal
CC membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates
CC retrograde transport of cargo proteins from endosomes to the trans-
CC Golgi network (TGN) and is involved in endosome-to-plasma membrane
CC transport for cargo protein recycling. The SNX3-retromer mediates the
CC retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR
CC retromer pathway. The SNX27-retromer is believed to be involved in
CC endosome-to-plasma membrane trafficking and recycling of a broad
CC spectrum of cargo proteins. The CSC seems to act as recruitment hub for
CC other proteins, such as the WASH complex and TBC1D5. Required to
CC regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-
CC pIgA) (By similarity). Acts also as component of the retriever complex.
CC The retriever complex is a heterotrimeric complex related to retromer
CC cargo-selective complex (CSC) and essential for retromer-independent
CC retrieval and recycling of numerous cargos such as integrin alpha-
CC 5/beta-1 (ITGA5:ITGB1). In the endosomes, retriever complex drives the
CC retrieval and recycling of NxxY-motif-containing cargo proteins by
CC coupling to SNX17, a cargo essential for the homeostatic maintenance of
CC numerous cell surface proteins associated with processes that include
CC cell migration, cell adhesion, nutrient supply and cell signaling. The
CC recruitment of the retriever complex to the endosomal membrane involves
CC CCC and WASH complexes. Involved in GLUT1 endosome-to-plasma membrane
CC trafficking; the function is dependent of association with ANKRD27 (By
CC similarity). Has no activity towards p-nitrophenylphosphate, p-
CC nitrophenylphosphorylcholine or phosphatidylinositlphosphates or a
CC phosphorylated peptide derived from retromer cargo (in vitro)
CC (PubMed:21629666, PubMed:15965486). {ECO:0000250|UniProtKB:Q9UBQ0,
CC ECO:0000269|PubMed:15965486, ECO:0000269|PubMed:21629666}.
CC -!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
CC complex (CSC), also described as vacuolar protein sorting subcomplex
CC (VPS) formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35
CC (PubMed:21040701, PubMed:20875039, PubMed:21920005). The CSC has a
CC highly elongated structure with VPS26 and VPS29 binding independently
CC at opposite distal ends of VPS35 as central platform (By similarity).
CC The CSC is believed to associate with variable sorting nexins to form
CC functionally distinct retromer complex variants. The originally
CC described retromer complex (also called SNX-BAR retromer) is a pentamer
CC containing the CSC and a heterodimeric membrane-deforming subcomplex
CC formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR
CC subcomplex); the respective CSC and SNX-BAR subcomplexes associate with
CC low affinity. The CSC associates with SNX3 to form a SNX3-retromer
CC complex. The CSC associates with SNX27, the WASH complex and the SNX-
CC BAR subcomplex to form the SNX27-retromer complex (By similarity).
CC Component of the heterotrimeric retriever complex formed by VPS26C,
CC VPS29 and VPS35L (By similarity). Interacts with VPS35L (By
CC similarity). Interacts with VPS26A, VPS26B, VPS35, ANKRD27
CC (PubMed:20875039, PubMed:21920005, PubMed:24856514). Interacts with
CC SNX1, SNX2, SNX27, WASHC5 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBQ0, ECO:0000269|PubMed:15965486,
CC ECO:0000269|PubMed:20875039, ECO:0000269|PubMed:21040701,
CC ECO:0000269|PubMed:21920005, ECO:0000269|PubMed:24856514}.
CC -!- INTERACTION:
CC Q9QZ88; Q9EQH3: Vps35; NbExp=5; IntAct=EBI-8334188, EBI-775825;
CC Q9QZ88; Q5T1M5: FKBP15; Xeno; NbExp=7; IntAct=EBI-8334188, EBI-5235934;
CC Q9QZ88; Q92609: TBC1D5; Xeno; NbExp=5; IntAct=EBI-8334188, EBI-742381;
CC Q9QZ88-1; Q9EQH3: Vps35; NbExp=3; IntAct=EBI-15553808, EBI-775825;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Endosome membrane
CC {ECO:0000269|PubMed:15965486}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15965486}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QZ88-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QZ88-2; Sequence=VSP_004074;
CC -!- SIMILARITY: Belongs to the VPS29 family. {ECO:0000305}.
CC -!- CAUTION: Was originally believed to be a metal-dependent phosphatase
CC but shown to lack catalytic activity; can bind metals (Zn(2+) and
CC Mn(2+)) with very low affinity suggesting that metal binding is not
CC required for its function. {ECO:0000303|PubMed:15965486,
CC ECO:0000303|PubMed:21629666}.
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DR EMBL; AF193794; AAF04595.1; -; mRNA.
DR EMBL; AK004103; BAB23170.1; -; mRNA.
DR EMBL; AK150330; BAE29472.1; -; mRNA.
DR EMBL; BC005663; AAH05663.1; -; mRNA.
DR CCDS; CCDS39256.1; -. [Q9QZ88-1]
DR CCDS; CCDS84954.1; -. [Q9QZ88-2]
DR RefSeq; NP_001334382.1; NM_001347453.1. [Q9QZ88-2]
DR RefSeq; NP_062754.1; NM_019780.1. [Q9QZ88-1]
DR PDB; 1Z2W; X-ray; 2.00 A; A/B=1-182.
DR PDB; 1Z2X; X-ray; 2.22 A; A/B=1-182.
DR PDB; 3PSN; X-ray; 2.20 A; A/B=1-182.
DR PDB; 3PSO; X-ray; 3.00 A; A/B=1-182.
DR PDB; 6TL0; NMR; -; A=1-182.
DR PDB; 6VAB; EM; 4.90 A; A/C=1-182.
DR PDB; 6VAC; EM; 5.70 A; C=1-182.
DR PDBsum; 1Z2W; -.
DR PDBsum; 1Z2X; -.
DR PDBsum; 3PSN; -.
DR PDBsum; 3PSO; -.
DR PDBsum; 6TL0; -.
DR PDBsum; 6VAB; -.
DR PDBsum; 6VAC; -.
DR AlphaFoldDB; Q9QZ88; -.
DR SMR; Q9QZ88; -.
DR BioGRID; 207976; 25.
DR CORUM; Q9QZ88; -.
DR DIP; DIP-60495N; -.
DR IntAct; Q9QZ88; 20.
DR STRING; 10090.ENSMUSP00000121020; -.
DR iPTMnet; Q9QZ88; -.
DR PhosphoSitePlus; Q9QZ88; -.
DR REPRODUCTION-2DPAGE; Q9QZ88; -.
DR EPD; Q9QZ88; -.
DR jPOST; Q9QZ88; -.
DR MaxQB; Q9QZ88; -.
DR PaxDb; Q9QZ88; -.
DR PeptideAtlas; Q9QZ88; -.
DR PRIDE; Q9QZ88; -.
DR ProteomicsDB; 297583; -. [Q9QZ88-1]
DR ProteomicsDB; 297584; -. [Q9QZ88-2]
DR TopDownProteomics; Q9QZ88-1; -. [Q9QZ88-1]
DR Antibodypedia; 31016; 212 antibodies from 32 providers.
DR DNASU; 56433; -.
DR Ensembl; ENSMUST00000118830; ENSMUSP00000113525; ENSMUSG00000029462. [Q9QZ88-2]
DR Ensembl; ENSMUST00000155671; ENSMUSP00000121020; ENSMUSG00000029462. [Q9QZ88-1]
DR GeneID; 56433; -.
DR KEGG; mmu:56433; -.
DR UCSC; uc008zlb.1; mouse. [Q9QZ88-1]
DR UCSC; uc008zlc.1; mouse. [Q9QZ88-2]
DR CTD; 51699; -.
DR MGI; MGI:1928344; Vps29.
DR VEuPathDB; HostDB:ENSMUSG00000029462; -.
DR eggNOG; KOG3325; Eukaryota.
DR GeneTree; ENSGT00390000012669; -.
DR HOGENOM; CLU_063749_0_1_1; -.
DR InParanoid; Q9QZ88; -.
DR OMA; IVVYVYE; -.
DR OrthoDB; 1233814at2759; -.
DR PhylomeDB; Q9QZ88; -.
DR TreeFam; TF300880; -.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR BioGRID-ORCS; 56433; 40 hits in 75 CRISPR screens.
DR ChiTaRS; Vps29; mouse.
DR EvolutionaryTrace; Q9QZ88; -.
DR PRO; PR:Q9QZ88; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9QZ88; protein.
DR Bgee; ENSMUSG00000029462; Expressed in otic placode and 267 other tissues.
DR ExpressionAtlas; Q9QZ88; baseline and differential.
DR Genevisible; Q9QZ88; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030904; C:retromer complex; IDA:UniProtKB.
DR GO; GO:0030906; C:retromer, cargo-selective complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006896; P:Golgi to vacuole transport; ISS:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR CDD; cd07394; MPP_Vps29; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR InterPro; IPR028661; Vps29.
DR PANTHER; PTHR11124; PTHR11124; 1.
DR PANTHER; PTHR11124:SF12; PTHR11124:SF12; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00040; yfcE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Endosome; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..182
FT /note="Vacuolar protein sorting-associated protein 29"
FT /id="PRO_0000065895"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ0"
FT VAR_SEQ 1
FT /note="M -> MAGHR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_004074"
FT MUTAGEN 39
FT /note="N->D: Decreases interaction with VPS35."
FT /evidence="ECO:0000269|PubMed:15965486"
FT MUTAGEN 90
FT /note="V->D: Decreases interaction with VPS35."
FT /evidence="ECO:0000269|PubMed:15965486"
FT MUTAGEN 91
FT /note="I->S: Disrupts interaction with VPS35."
FT /evidence="ECO:0000269|PubMed:15965486"
FT MUTAGEN 152
FT /note="L->E: Disrupts interaction with ANKRD27."
FT /evidence="ECO:0000269|PubMed:24856514"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1Z2W"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3PSN"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:1Z2W"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1Z2X"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1Z2W"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3PSN"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6TL0"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6TL0"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:1Z2W"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:1Z2W"
SQ SEQUENCE 182 AA; 20496 MW; 6CDCDE6B720C9BF8 CRC64;
MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKESYDYLK TLAGDVHIVR
GDFDENLNYP EQKVVTVGQF KIGLIHGHQV IPWGDMASLA LLQRQFDVDI LISGHTHKFE
AFEHENKFYI NPGSATGAYN ALETNIIPSF VLMDIQASTV VTYVYQLIGD DVKVERIEYK
KS
