LAMP1_MOUSE
ID LAMP1_MOUSE Reviewed; 406 AA.
AC P11438; Q62020;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Lysosome-associated membrane glycoprotein 1;
DE Short=LAMP-1;
DE Short=Lysosome-associated membrane protein 1;
DE AltName: Full=120 kDa lysosomal membrane glycoprotein;
DE AltName: Full=CD107 antigen-like family member A;
DE AltName: Full=LGP-120;
DE AltName: Full=Lysosomal membrane glycoprotein A;
DE Short=LGP-A;
DE AltName: Full=P2B;
DE AltName: CD_antigen=CD107a;
DE Flags: Precursor;
GN Name=Lamp1; Synonyms=Lamp-1;
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].
RX PubMed=2142158; DOI=10.1016/s0021-9258(19)38504-7;
RA Granger B.L., Green S.A., Gabel C.A., Howe C.L., Mellman I., Helenius A.;
RT "Characterization and cloning of lgp110, a lysosomal membrane glycoprotein
RT from mouse and rat cells.";
RL J. Biol. Chem. 265:12036-12043(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2676155;
RA Heffernan M., Yousefi S., Dennis J.W.;
RT "Molecular characterization of P2B/LAMP-1, a major protein target of a
RT metastasis-associated oligosaccharide structure.";
RL Cancer Res. 49:6077-6084(1989).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 25-406, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3379044; DOI=10.1016/s0021-9258(18)68370-x;
RA Chen J.W., Cha Y., Yuksel K.U., Gracy R.W., August J.T.;
RT "Isolation and sequencing of a cDNA clone encoding lysosomal membrane
RT glycoprotein mouse LAMP-1. Sequence similarity to proteins bearing onco-
RT differentiation antigens.";
RL J. Biol. Chem. 263:8754-8758(1988).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=2332434; DOI=10.1016/s0021-9258(19)39130-6;
RA Arterburn L.M., Earles B.J., August J.T.;
RT "The disulfide structure of mouse lysosome-associated membrane protein 1.";
RL J. Biol. Chem. 265:7419-7423(1990).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10212251; DOI=10.1074/jbc.274.18.12692;
RA Andrejewski N., Punnonen E.L., Guhde G., Tanaka Y., Luellmann-Rauch R.,
RA Hartmann D., von Figura K., Saftig P.;
RT "Normal lysosomal morphology and function in LAMP-1-deficient mice.";
RL J. Biol. Chem. 274:12692-12701(1999).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15121881; DOI=10.1091/mbc.e04-02-0103;
RA Eskelinen E.L., Schmidt C.K., Neu S., Willenborg M., Fuertes G.,
RA Salvador N., Tanaka Y., Luellmann-Rauch R., Hartmann D., Heeren J.,
RA von Figura K., Knecht E., Saftig P.;
RT "Disturbed cholesterol traffic but normal proteolytic function in LAMP-
RT 1/LAMP-2 double-deficient fibroblasts.";
RL Mol. Biol. Cell 15:3132-3145(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-252.
RC TISSUE=Epidermis;
RX PubMed=16170054; DOI=10.1074/mcp.m500203-mcp200;
RA Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K.,
RA Nishimura S.;
RT "High throughput quantitative glycomics and glycoform-focused proteomics of
RT murine dermis and epidermis.";
RL Mol. Cell. Proteomics 4:1977-1989(2005).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-177.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97; ASN-101; ASN-159 AND
RP ASN-177.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
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 [13]
RP INTERACTION WITH ABCB9.
RX PubMed=22641697; DOI=10.1242/jcs.087346;
RA Demirel O., Jan I., Wolters D., Blanz J., Saftig P., Tampe R., Abele R.;
RT "The lysosomal polypeptide transporter TAPL is stabilized by interaction
RT with LAMP-1 and LAMP-2.";
RL J. Cell Sci. 125:4230-4240(2012).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=23847195; DOI=10.1182/blood-2012-07-441832;
RA Cohnen A., Chiang S.C., Stojanovic A., Schmidt H., Claus M., Saftig P.,
RA Janssen O., Cerwenka A., Bryceson Y.T., Watzl C.;
RT "Surface CD107a/LAMP-1 protects natural killer cells from degranulation-
RT associated damage.";
RL Blood 122:1411-1418(2013).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=32839608; DOI=10.1038/s41590-020-0758-6;
RA Ng S.S., De Labastida Rivera F., Yan J., Corvino D., Das I., Zhang P.,
RA Kuns R., Chauhan S.B., Hou J., Li X.Y., Frame T.C.M., McEnroe B.A.,
RA Moore E., Na J., Engel J.A., Soon M.S.F., Singh B., Kueh A.J., Herold M.J.,
RA Montes de Oca M., Singh S.S., Bunn P.T., Aguilera A.R., Casey M., Braun M.,
RA Ghazanfari N., Wani S., Wang Y., Amante F.H., Edwards C.L., Haque A.,
RA Dougall W.C., Singh O.P., Baxter A.G., Teng M.W.L., Loukas A., Daly N.L.,
RA Cloonan N., Degli-Esposti M.A., Uzonna J., Heath W.R., Bald T., Tey S.K.,
RA Nakamura K., Hill G.R., Kumar R., Sundar S., Smyth M.J., Engwerda C.R.;
RT "The NK cell granule protein NKG7 regulates cytotoxic granule exocytosis
RT and inflammation.";
RL Nat. Immunol. 21:1205-1218(2020).
CC -!- FUNCTION: Lysosomal membrane glycoprotein which plays an important role
CC in lysosome biogenesis, autophagy, and cholesterol homeostasis
CC (PubMed:15121881). Also plays an important role in NK-cells
CC cytotoxicity (PubMed:23847195). Mechanistically, participates in
CC cytotoxic granule movement to the cell surface and perforin trafficking
CC to the lytic granule (By similarity). In addition, protects NK-cells
CC from degranulation-associated damage induced by their own cytotoxic
CC granule content (By similarity) (PubMed:23847195). Presents
CC carbohydrate ligands to selectins. Also implicated in tumor cell
CC metastasis (By similarity). {ECO:0000250|UniProtKB:P11279,
CC ECO:0000269|PubMed:15121881, ECO:0000269|PubMed:23847195}.
CC -!- SUBUNIT: Interacts with ABCB9; this interaction strongly stabilizes
CC ABCB9 and protects ABCB9 against lysosomal degradation
CC (PubMed:22641697). Interacts with FURIN (By similarity).
CC {ECO:0000250|UniProtKB:P11279, ECO:0000269|PubMed:22641697}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23847195};
CC Single-pass type I membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P11279};
CC Single-pass type I membrane protein {ECO:0000255}. Late endosome
CC membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane
CC protein {ECO:0000255}. Cytolytic granule membrane
CC {ECO:0000305|PubMed:32839608}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=This protein shuttles between lysosomes, endosomes,
CC and the plasma membrane (By similarity). Colocalizes with OSBPL1A at
CC the late endosome (By similarity). {ECO:0000250|UniProtKB:P05300,
CC ECO:0000250|UniProtKB:P11279}.
CC -!- PTM: O- and N-glycosylated; some of the N-glycans attached to LAMP-1
CC are polylactosaminoglycans. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are viable and fertile
CC (PubMed:10212251). However, mice deficient in both LAMP1 and LAMP2 are
CC embryonic lethal, with the accumulation of autophagic vacuoles in many
CC tissues (PubMed:15121881). In addition, LAMP1 deletion results in
CC increased NK-cell apoptosis upon target cell-induced degranulation
CC (PubMed:23847195). {ECO:0000269|PubMed:10212251,
CC ECO:0000269|PubMed:15121881, ECO:0000269|PubMed:23847195}.
CC -!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
CC ProRule:PRU00740}.
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DR EMBL; M32015; AAA39428.1; -; mRNA.
DR EMBL; M25244; AAA39869.1; -; mRNA.
DR EMBL; BC049097; AAH49097.1; -; mRNA.
DR EMBL; J03881; AAA39411.1; -; mRNA.
DR CCDS; CCDS22106.1; -.
DR PIR; A28067; A28067.
DR PIR; A60534; A60534.
DR RefSeq; NP_001304282.1; NM_001317353.1.
DR RefSeq; NP_034814.2; NM_010684.3.
DR PDB; 5GV0; X-ray; 1.50 A; A=208-370.
DR PDBsum; 5GV0; -.
DR AlphaFoldDB; P11438; -.
DR SMR; P11438; -.
DR BioGRID; 201105; 4.
DR IntAct; P11438; 19.
DR MINT; P11438; -.
DR STRING; 10090.ENSMUSP00000033824; -.
DR GlyConnect; 2494; 22 N-Linked glycans (8 sites).
DR GlyGen; P11438; 19 sites, 21 N-linked glycans (8 sites).
DR iPTMnet; P11438; -.
DR PhosphoSitePlus; P11438; -.
DR CPTAC; non-CPTAC-3834; -.
DR EPD; P11438; -.
DR jPOST; P11438; -.
DR PaxDb; P11438; -.
DR PeptideAtlas; P11438; -.
DR PRIDE; P11438; -.
DR ProteomicsDB; 264913; -.
DR Antibodypedia; 2703; 1397 antibodies from 51 providers.
DR DNASU; 16783; -.
DR Ensembl; ENSMUST00000033824; ENSMUSP00000033824; ENSMUSG00000031447.
DR GeneID; 16783; -.
DR KEGG; mmu:16783; -.
DR UCSC; uc009kxa.1; mouse.
DR CTD; 3916; -.
DR MGI; MGI:96745; Lamp1.
DR VEuPathDB; HostDB:ENSMUSG00000031447; -.
DR eggNOG; KOG4818; Eukaryota.
DR GeneTree; ENSGT00950000182899; -.
DR HOGENOM; CLU_055379_2_0_1; -.
DR InParanoid; P11438; -.
DR OMA; NSYKCSA; -.
DR OrthoDB; 1042920at2759; -.
DR PhylomeDB; P11438; -.
DR TreeFam; TF316339; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 16783; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Lamp1; mouse.
DR PRO; PR:P11438; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P11438; protein.
DR Bgee; ENSMUSG00000031447; Expressed in stroma of bone marrow and 266 other tissues.
DR ExpressionAtlas; P11438; baseline and differential.
DR Genevisible; P11438; MM.
DR GO; GO:0097208; C:alveolar lamellar body; ISO:MGI.
DR GO; GO:0044754; C:autolysosome; IDA:MGI.
DR GO; GO:0000421; C:autophagosome membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0044194; C:cytolytic granule; IDA:UniProtKB.
DR GO; GO:0101004; C:cytolytic granule membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0042470; C:melanosome; IDA:MGI.
DR GO; GO:0005771; C:multivesicular body; IDA: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:0045335; C:phagocytic vesicle; IMP:AgBase.
DR GO; GO:0061474; C:phagolysosome membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0005773; C:vacuole; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0048102; P:autophagic cell death; ISO:MGI.
DR GO; GO:0072594; P:establishment of protein localization to organelle; ISO:MGI.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISO:MGI.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; ISO:MGI.
DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; ISO:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; TAS:MGI.
DR InterPro; IPR018134; LAMP_CS.
DR InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR PANTHER; PTHR11506; PTHR11506; 1.
DR Pfam; PF01299; Lamp; 1.
DR PRINTS; PR00336; LYSASSOCTDMP.
DR PROSITE; PS00310; LAMP_1; 2.
DR PROSITE; PS00311; LAMP_2; 1.
DR PROSITE; PS51407; LAMP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Endosome; Glycoprotein; Lysosome; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:3379044"
FT CHAIN 25..406
FT /note="Lysosome-associated membrane glycoprotein 1"
FT /id="PRO_0000017105"
FT TOPO_DOM 25..370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..394
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT TOPO_DOM 395..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740"
FT REGION 25..188
FT /note="First lumenal domain"
FT REGION 180..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..218
FT /note="Hinge"
FT REGION 219..370
FT /note="Second lumenal domain"
FT COMPBIAS 192..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740,
FT ECO:0000269|PubMed:2332434"
FT DISULFID 149..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740,
FT ECO:0000269|PubMed:2332434"
FT DISULFID 222..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740,
FT ECO:0000269|PubMed:2332434"
FT DISULFID 327..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00740,
FT ECO:0000269|PubMed:2332434"
FT CONFLICT 1..10
FT /note="MAAPGARRPL -> MRPPRAAAV (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..26
FT /note="LF -> IP (in Ref. 4; AAA39411)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="V -> I (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 220..237
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:5GV0"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 339..351
FT /evidence="ECO:0007829|PDB:5GV0"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:5GV0"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:5GV0"
SQ SEQUENCE 406 AA; 43865 MW; C1BD373548BB9655 CRC64;
MAAPGARRPL LLLLLAGLAH GASALFEVKN NGTTCIMASF SASFLTTYET ANGSQIVNIS
LPASAEVLKN GSSCGKENVS DPSLTITFGR GYLLTLNFTK NTTRYSVQHM YFTYNLSDTE
HFPNAISKEI YTMDSTTDIK ADINKAYRCV SDIRVYMKNV TVVLRDATIQ AYLSSGNFSK
EETHCTQDGP SPTTGPPSPS PPLVPTNPTV SKYNVTGNNG TCLLASMALQ LNITYLKKDN
KTVTRAFNIS PNDTSSGSCG INLVTLKVEN KNRALELQFG MNASSSLFFL QGVRLNMTLP
DALVPTFSIS NHSLKALQAT VGNSYKCNTE EHIFVSKMLS LNVFSVQVQA FKVDSDRFGS
VEECVQDGNN MLIPIAVGGA LAGLVLIVLI AYLIGRKRSH AGYQTI
