PSN_DROME
ID PSN_DROME Reviewed; 541 AA.
AC O02194; O02395; O76802; O96340; Q9TY80; Q9V3L9; Q9V3S1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Presenilin homolog;
DE Short=DmPS;
DE EC=3.4.23.-;
DE AltName: Full=dPS;
GN Name=Psn; Synonyms=PS; ORFNames=CG18803;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9141085; DOI=10.1097/00001756-199703030-00041;
RA Boulianne G.L., Livne-Bar I., Humphreys J.M., Liang Y., Lin C., Rogaev E.,
RA St George-Hyslop P.H.;
RT "Cloning and characterization of the Drosophila presenilin homologue.";
RL NeuroReport 8:1025-1029(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Embryo, and Head;
RX PubMed=9106743; DOI=10.1097/00001756-199702100-00017;
RA Hong C.-S., Koo E.H.;
RT "Isolation and characterization of Drosophila presenilin homolog.";
RL NeuroReport 8:665-668(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=10349633; DOI=10.1016/s0925-4773(98)00169-5;
RA Ye Y., Fortini M.E.;
RT "Characterization of Drosophila Presenilin and its colocalization with
RT Notch during development.";
RL Mech. Dev. 79:199-211(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), AND FUNCTION IN S3 CLEAVAGE OF
RP NOTCH.
RX PubMed=10206647; DOI=10.1038/19096;
RA Ye Y., Lukinova N., Fortini M.E.;
RT "Neurogenic phenotypes and altered Notch processing in Drosophila
RT Presenilin mutants.";
RL Nature 398:525-529(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=9666900; DOI=10.3109/01677069809108554;
RA Marfany G., Del-Favero J., Valero R., De Jonghe C., Woodrow S.,
RA Hendriks L., Van Broeckhoven C., Gonzalez-Duarte R.;
RT "Identification of a Drosophila presenilin homologue: evidence of
RT alternatively spliced forms.";
RL J. Neurogenet. 12:41-54(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=10493744; DOI=10.1523/jneurosci.19-19-08435.1999;
RA Guo Y., Livne-Bar I., Zhou L., Boulianne G.L.;
RT "Drosophila presenilin is required for neuronal differentiation and affects
RT notch subcellular localization and signaling.";
RL J. Neurosci. 19:8435-8442(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [8]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [10]
RP ALTERNATIVE SPLICING (ISOFORM 3), AND CLEAVAGE.
RX PubMed=10662508; DOI=10.1006/mcne.1999.0805;
RA Nowotny P., Gorski S.M., Han S.W., Philips K., Ray W.J., Nowotny V.,
RA Jones C.J., Clark R.F., Cagan R.L., Goate A.M.;
RT "Posttranslational modification and plasma membrane localization of the
RT Drosophila melanogaster presenilin.";
RL Mol. Cell. Neurosci. 15:88-98(2000).
RN [11]
RP FUNCTION IN S3 CLEAVAGE OF NOTCH.
RX PubMed=10206646; DOI=10.1038/19091;
RA Struhl G., Greenwald I.;
RT "Presenilin is required for activity and nuclear access of Notch in
RT Drosophila.";
RL Nature 398:522-525(1999).
RN [12]
RP INTERACTION WITH METL.
RX PubMed=11738826; DOI=10.1016/s0378-1119(01)00770-3;
RA Zhang S.X., Guo Y., Boulianne G.L.;
RT "Identification of a novel family of putative methyltransferases that
RT interact with human and Drosophila presenilins.";
RL Gene 280:135-144(2001).
RN [13]
RP FUNCTION IN THE GAMMA-SECRETASE COMPLEX, AND INTERACTION WITH PEN-2; APH-1
RP AND NCT.
RX PubMed=12660785; DOI=10.1038/nature01506;
RA Takasugi N., Tomita T., Hayashi I., Tsuruoka M., Niimura M., Takahashi Y.,
RA Thinakaran G., Iwatsubo T.;
RT "The role of presenilin cofactors in the gamma-secretase complex.";
RL Nature 422:438-441(2003).
CC -!- FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral membrane proteins such as Notch receptor. Required for S3
CC cleavage of Notch, which releases activated Notch protein from the cell
CC membrane. Involved in the patterning of the optic lobes.
CC {ECO:0000269|PubMed:10206646, ECO:0000269|PubMed:10206647,
CC ECO:0000269|PubMed:12660785}.
CC -!- SUBUNIT: Homodimer (By similarity). Component of the gamma-secretase
CC complex, a complex composed of a presenilin (Psn) homodimer, nicastrin
CC (Nct), Aph-1 and Pen-2. Interacts with Metl. Isoform 2 shows a better
CC interaction with Metl than isoform 1. {ECO:0000250,
CC ECO:0000269|PubMed:11738826, ECO:0000269|PubMed:12660785}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A2, A, DLA-b;
CC IsoId=O02194-1; Sequence=Displayed;
CC Name=2; Synonyms=A1, B, PS-d, DLA-a;
CC IsoId=O02194-2; Sequence=VSP_005195;
CC Name=3;
CC IsoId=O02194-3; Sequence=VSP_007988;
CC -!- TISSUE SPECIFICITY: Maternally expressed in nurse and follicle cells.
CC In early embryos, expressed in all or most cells and later increases in
CC CNS and epidermal tissues. In larvae, expression is seen in all
CC imaginal disks, brain and optic lobes. In pupae, expression is seen in
CC eye disk and brain. {ECO:0000269|PubMed:10349633}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development. {ECO:0000269|PubMed:10349633,
CC ECO:0000269|PubMed:9106743, ECO:0000269|PubMed:9141085,
CC ECO:0000269|PubMed:9666900}.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- PTM: Cleaved. The cleavage, which probably takes place between the 6th
CC and the 7th transmembrane regions, may be required for activation of
CC the gamma-secretase activity. {ECO:0000269|PubMed:10662508}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
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DR EMBL; U77934; AAB61139.1; -; mRNA.
DR EMBL; U78084; AAB53369.1; -; mRNA.
DR EMBL; AF084184; AAC33129.1; -; Genomic_DNA.
DR EMBL; AF084184; AAC33128.1; -; Genomic_DNA.
DR EMBL; AF017024; AAD01610.1; -; mRNA.
DR EMBL; AF017025; AAD01611.1; -; mRNA.
DR EMBL; AF017026; AAD01612.1; -; Genomic_DNA.
DR EMBL; AF093402; AAD52707.1; -; Genomic_DNA.
DR EMBL; AF093402; AAD52708.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12132.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51598.1; -; Genomic_DNA.
DR EMBL; AY061316; AAL28864.1; -; mRNA.
DR RefSeq; NP_001262110.1; NM_001275181.1. [O02194-2]
DR RefSeq; NP_001262111.1; NM_001275182.1. [O02194-1]
DR RefSeq; NP_524184.1; NM_079460.2. [O02194-1]
DR RefSeq; NP_730535.1; NM_168856.3. [O02194-2]
DR AlphaFoldDB; O02194; -.
DR SMR; O02194; -.
DR BioGRID; 65518; 43.
DR DIP; DIP-1139N; -.
DR IntAct; O02194; 1.
DR STRING; 7227.FBpp0077850; -.
DR MEROPS; A22.014; -.
DR GlyGen; O02194; 1 site.
DR PaxDb; O02194; -.
DR PRIDE; O02194; -.
DR DNASU; 40260; -.
DR EnsemblMetazoa; FBtr0078192; FBpp0077850; FBgn0284421. [O02194-1]
DR EnsemblMetazoa; FBtr0078193; FBpp0077851; FBgn0284421. [O02194-2]
DR EnsemblMetazoa; FBtr0114517; FBpp0113009; FBgn0284421. [O02194-3]
DR EnsemblMetazoa; FBtr0333478; FBpp0305665; FBgn0284421. [O02194-2]
DR EnsemblMetazoa; FBtr0333479; FBpp0305666; FBgn0284421. [O02194-1]
DR GeneID; 40260; -.
DR KEGG; dme:Dmel_CG18803; -.
DR UCSC; CG18803-RA; d. melanogaster. [O02194-1]
DR CTD; 40260; -.
DR FlyBase; FBgn0284421; Psn.
DR VEuPathDB; VectorBase:FBgn0284421; -.
DR eggNOG; KOG2736; Eukaryota.
DR GeneTree; ENSGT00940000174002; -.
DR InParanoid; O02194; -.
DR OMA; YEARPVN; -.
DR PhylomeDB; O02194; -.
DR Reactome; R-DME-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; O02194; -.
DR BioGRID-ORCS; 40260; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40260; -.
DR PRO; PR:O02194; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0284421; Expressed in eye disc (Drosophila) and 27 other tissues.
DR ExpressionAtlas; O02194; baseline and differential.
DR Genevisible; O02194; DM.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
DR GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070765; C:gamma-secretase complex; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004175; F:endopeptidase activity; IDA:FlyBase.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IBA:GO_Central.
DR GO; GO:0034205; P:amyloid-beta formation; IDA:FlyBase.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IMP:CACAO.
DR GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0007220; P:Notch receptor processing; IMP:FlyBase.
DR GO; GO:0035333; P:Notch receptor processing, ligand-dependent; IDA:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:FlyBase.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IDA:FlyBase.
DR Gene3D; 1.10.472.100; -; 1.
DR InterPro; IPR001108; Peptidase_A22A.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR042524; Presenilin_C.
DR PANTHER; PTHR10202; PTHR10202; 1.
DR Pfam; PF01080; Presenilin; 1.
DR PRINTS; PR01072; PRESENILIN.
DR SMART; SM00730; PSN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Hydrolase; Membrane; Notch signaling pathway; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..541
FT /note="Presenilin homolog"
FT /id="PRO_0000073901"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..154
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..216
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..265
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..481
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 507..527
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..481
FT /note="Interaction with metl"
FT REGION 327..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 507..509
FT /note="PAL"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /evidence="ECO:0000250"
FT ACT_SITE 461
FT /evidence="ECO:0000250"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 365..397
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_007988"
FT VAR_SEQ 384..397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9106743"
FT /id="VSP_005195"
FT CONFLICT 80..81
FT /note="GG -> RS (in Ref. 2; AAB53369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 59304 MW; A3B3D54348A2C03F CRC64;
MAAVNLQASC SSGLASEDDA NVGSQIGAAE RLERPPRRQQ QRNNYGSSNQ DQPDAAILAV
PNVVMREPCG SRPSRLTGGG GGSGGPPTNE MEEEQGLKYG AQHVIKLFVP VSLCMLVVVA
TINSISFYNS TDVYLLYTPF HEQSPEPSVK FWSALANSLI LMSVVVVMTF LLIVLYKKRC
YRIIHGWLIL SSFMLLFIFT YLYLEELLRA YNIPMDYPTA LLIMWNFGVV GMMSIHWQGP
LRLQQGYLIF VAALMALVFI KYLPEWTAWA VLAAISIWDL IAVLSPRGPL RILVETAQER
NEQIFPALIY SSTVVYALVN TVTPQQSQAT ASSSPSSSNS TTTTRATQNS LASPEAAAAS
GQRTGNSHPR QNQRDDGSVL ATEGMPLVTF KSNLRGNAEA AGFTQEWSAN LSERVARRQI
EVQSTQSGNA QRSNEYRTVT APDQNHPDGQ EERGIKLGLG DFIFYSVLVG KASSYGDWTT
TIACFVAILI GLCLTLLLLA IWRKALPALP ISITFGLIFC FATSAVVKPF MEDLSAKQVF
I
