PRIC1_DROME
ID PRIC1_DROME Reviewed; 1299 AA.
AC A1Z6W3; A1Z6V4; A1Z6V8; Q9N9H6; Q9U5X0; Q9U5X1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein prickle;
DE AltName: Full=Protein spiny legs;
GN Name=pk {ECO:0000312|EMBL:AAF59281.2}; ORFNames=CG11084;
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] {ECO:0000305, ECO:0000312|EMBL:CAB57345.3}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=DP CN BW; TISSUE=Embryo {ECO:0000269|PubMed:10485852};
RX PubMed=10485852; DOI=10.1101/gad.13.17.2315;
RA Gubb D., Green C., Huen D., Coulson D., Johnson G., Tree D.R.P.,
RA Collier S., Roote J.;
RT "The balance between isoforms of the prickle LIM domain protein is critical
RT for planar polarity in Drosophila imaginal discs.";
RL Genes Dev. 13:2315-2327(1999).
RN [2] {ECO:0000312|EMBL:AAF59281.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF59281.2}
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 [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DSH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12015986; DOI=10.1016/s0092-8674(02)00715-8;
RA Tree D.R.P., Shulman J.M., Rousset R., Scott M.P., Gubb D., Axelrod J.D.;
RT "Prickle mediates feedback amplification to generate asymmetric planar cell
RT polarity signaling.";
RL Cell 109:371-381(2002).
RN [5] {ECO:0000305}
RP INTERACTION WITH VANG, AND SUBCELLULAR LOCATION.
RX PubMed=12941693; DOI=10.1093/emboj/cdg424;
RA Jenny A., Darken R.S., Wilson P.A., Mlodzik M.;
RT "Prickle and Strabismus form a functional complex to generate a correct
RT axis during planar cell polarity signaling.";
RL EMBO J. 22:4409-4420(2003).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH VANG, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12642492; DOI=10.1242/dev.00411;
RA Rawls A.S., Wolff T.;
RT "Strabismus requires Flamingo and Prickle function to regulate tissue
RT polarity in the Drosophila eye.";
RL Development 130:1877-1887(2003).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DSH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15937478; DOI=10.1038/ncb1271;
RA Jenny A., Reynolds-Kenneally J., Das G., Burnett M., Mlodzik M.;
RT "Diego and Prickle regulate Frizzled planar cell polarity signalling by
RT competing for Dishevelled binding.";
RL Nat. Cell Biol. 7:691-697(2005).
CC -!- FUNCTION: Acts in a planar cell polarity (PCP) complex; polarization
CC along the apical/basal axis of epithelial cells. Correct expression of
CC the alternative isoforms is required for PCP signaling in imaginal
CC disks. PCP signaling in the wing disk requires the receptor fz and the
CC cytoplasmic proteins dsh and pk. These act in a feedback loop leading
CC to activation of the jnk cascade and subsequent polarized arrangement
CC of hairs and bristles. Dgo and pk compete with one another for dsh
CC binding, thereby modulating fz dsh activity and ensuring tight control
CC over fz PCP signaling. Vang, stan and pk function together to regulate
CC the establishment of tissue polarity in the adult eye.
CC {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492,
CC ECO:0000269|PubMed:15937478}.
CC -!- SUBUNIT: Interacts with dsh; PET and LIM domains interact with dsh DEP
CC domain, in wing cells. Interacts with Vang in photoreceptor cells.
CC {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492,
CC ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12015986,
CC ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693,
CC ECO:0000269|PubMed:15937478}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492,
CC ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}; Cytoplasmic
CC side {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492,
CC ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}.
CC Note=Localized to the proximal wing cell boundary where fz and dsh
CC localization is antagonized by binding the dsh DEP domain and
CC preventing dsh cortical localization. Localization to the anterior
CC photoreceptor cell membrane. {ECO:0000269|PubMed:12015986,
CC ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693,
CC ECO:0000269|PubMed:15937478}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C {ECO:0000269|PubMed:10731132}; Synonyms=sple
CC {ECO:0000269|PubMed:10485852};
CC IsoId=A1Z6W3-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:10731132}; Synonyms=pk
CC {ECO:0000269|PubMed:10485852};
CC IsoId=A1Z6W3-2; Sequence=VSP_052413, VSP_052414;
CC Name=B {ECO:0000269|PubMed:10731132}; Synonyms=pkM
CC {ECO:0000269|PubMed:10485852};
CC IsoId=A1Z6W3-3; Sequence=VSP_052412, VSP_052415;
CC -!- TISSUE SPECIFICITY: Expressed in the wing, leg and eye imaginal disks.
CC Expressed within the photoreceptors of the eye.
CC {ECO:0000269|PubMed:10485852, ECO:0000269|PubMed:12015986,
CC ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:15937478}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Isoform
CC B is expressed in embryos only. Isoform A and isoform C are expressed
CC in embryos and pupae. {ECO:0000269|PubMed:10485852}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit aberrant hair and bristle
CC orientation on the wings and aberrant ommatidial arrangement in the
CC compound eye. {ECO:0000269|PubMed:12015986,
CC ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:15937478}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; AJ243708; CAB57344.3; -; mRNA.
DR EMBL; AJ243710; CAB57345.3; -; mRNA.
DR EMBL; AJ243709; CAB99211.2; -; mRNA.
DR EMBL; AE013599; AAF59281.2; -; Genomic_DNA.
DR EMBL; AE013599; AAF59284.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68908.1; -; Genomic_DNA.
DR RefSeq; NP_724534.1; NM_165508.2. [A1Z6W3-2]
DR RefSeq; NP_724535.1; NM_165509.2. [A1Z6W3-3]
DR RefSeq; NP_724538.1; NM_165512.2. [A1Z6W3-1]
DR AlphaFoldDB; A1Z6W3; -.
DR SMR; A1Z6W3; -.
DR BioGRID; 69608; 31.
DR DIP; DIP-59584N; -.
DR IntAct; A1Z6W3; 4.
DR STRING; 7227.FBpp0088115; -.
DR PaxDb; A1Z6W3; -.
DR EnsemblMetazoa; FBtr0089042; FBpp0088113; FBgn0003090. [A1Z6W3-2]
DR EnsemblMetazoa; FBtr0089043; FBpp0088114; FBgn0003090. [A1Z6W3-3]
DR EnsemblMetazoa; FBtr0089044; FBpp0088115; FBgn0003090. [A1Z6W3-1]
DR GeneID; 45343; -.
DR KEGG; dme:Dmel_CG11084; -.
DR CTD; 18745; -.
DR FlyBase; FBgn0003090; pk.
DR VEuPathDB; VectorBase:FBgn0003090; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000153629; -.
DR InParanoid; A1Z6W3; -.
DR OMA; WPAKPTN; -.
DR PhylomeDB; A1Z6W3; -.
DR Reactome; R-DME-350368; Activation of RHO1 by FZ:DSH complex.
DR Reactome; R-DME-350369; Negative feedback loop regulates asymmetric localisation.
DR Reactome; R-DME-350376; Activation of RAC1:GTP by FZ:DSH complex.
DR Reactome; R-DME-350411; Formation and asymmetric localisation of transmembrane complexes.
DR Reactome; R-DME-350480; Activation of non-muscle Myosin II.
DR Reactome; R-DME-450728; Inhibition of actin polymerisation.
DR Reactome; R-DME-4608870; Asymmetric localization of PCP proteins.
DR BioGRID-ORCS; 45343; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45343; -.
DR PRO; PR:A1Z6W3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003090; Expressed in eye disc (Drosophila) and 20 other tissues.
DR ExpressionAtlas; A1Z6W3; baseline and differential.
DR Genevisible; A1Z6W3; DM.
DR GO; GO:0030424; C:axon; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; TAS:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0098930; P:axonal transport; IMP:FlyBase.
DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; TAS:FlyBase.
DR GO; GO:0007164; P:establishment of tissue polarity; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:FlyBase.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:FlyBase.
DR GO; GO:0045185; P:maintenance of protein location; TAS:FlyBase.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0045773; P:positive regulation of axon extension; IGI:FlyBase.
DR GO; GO:1902669; P:positive regulation of axon guidance; IMP:FlyBase.
DR CDD; cd09415; LIM1_Prickle; 1.
DR CDD; cd09418; LIM2_Prickle; 1.
DR CDD; cd09420; LIM3_Prickle; 1.
DR CDD; cd09827; PET_Prickle; 1.
DR InterPro; IPR033725; LIM1_prickle.
DR InterPro; IPR033726; LIM2_prickle.
DR InterPro; IPR033727; LIM3_prickle.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR033723; PET_prickle.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein; LIM domain;
KW Membrane; Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..1299
FT /note="Protein prickle"
FT /id="PRO_0000288834"
FT DOMAIN 515..623
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 622..686
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 687..747
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 748..810
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1042
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1180
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2..80
FT /note="SSLSTGGGAGGSSGGPGGADAAAAPAAGQATVTATGNMEPAMVPRTANLLAC
FT KQWWRVCFLYGDQQKYYRQLYSKAAAQ -> NDSTDNLHADCDGRVSNNNNGNSNTNDG
FT PNNDGDSDEEVIEGMALLEGNYQVLRQWVPPAPNYWDAPPKAIIKSAEVR (in
FT isoform B)"
FT /evidence="ECO:0000303|PubMed:10485852"
FT /id="VSP_052412"
FT VAR_SEQ 2..13
FT /note="SSLSTGGGAGGS -> DTPNQMPVELER (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10485852"
FT /id="VSP_052413"
FT VAR_SEQ 14..349
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10485852"
FT /id="VSP_052414"
FT VAR_SEQ 81..349
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10485852"
FT /id="VSP_052415"
FT CONFLICT 175..177
FT /note="ESS -> VSN (in Ref. 1; CAB57345)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="V -> A (in Ref. 1; CAB57345)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="Q -> P (in Ref. 1; CAB57345)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="A -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="A -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="A -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="A -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="R -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="S -> P (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="L -> V (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="G -> S (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1231
FT /note="E -> K (in Ref. 1; CAB57344/CAB57345/CAB99211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1299 AA; 140722 MW; 8BFAF1F75F352485 CRC64;
MSSLSTGGGA GGSSGGPGGA DAAAAPAAGQ ATVTATGNME PAMVPRTANL LACKQWWRVC
FLYGDQQKYY RQLYSKAAAQ RLADANQEPD NARDREYDTV DCDLIAGQLD AVEDADDGID
LGDHSSTPKG GATTAGRPLF PHSSSPRRSK KLLRSLRAHV RGEKLPKNDT TTANESSEVT
QRNARVTVLD DPFLFGIDAD HLGDLVVRGK RYSTLDATEN MARFYAEQEA TAQVLEIIEQ
EEESPEQEAP KPALPPKQKQ QRPVPPLPPP PANRVTQDQG TQPAAPQVPL QPLTAGDLQF
LNLSLRQRSL PRSMKPFKDA HDISFTFNEL DTSAEPEVAT GAAQQESNEP ISRTPLTQIS
YLQKIPTLPR HFSPSGQGLA TPPALGSGGM GLPSSSSASA LYAAQAAAGI LPTSPLPLQR
HQQYLPPHHQ QHPGAGMGPG PGSGAAAGPP LGPQYSPGCS ANPKYSNAQL PPPPHHHHQL
SPALSTPSPP SLLHHPAGGT SSASAHAPFL GGPHMDMQRQ SHSDDDSGCA LEEYTWVPPG
LRPDQVRLYF SQIPDDKVPY VNSPGEQYRV RQLLHQLPPH DNEVRYCHSL TDEERKELRL
FSTQRKRDAL GRGNVRQLMS ARPCDGCDDL ISTGDIAVFA TRLGPNASWH PACFACSVCR
ELLVDLIYFH RDGRMYCGRH HAETLKPRCS ACDEIILADE CTEAEGRAWH MNHFACHECD
KQLGGQRYIM REGKPYCLHC FDAMFAEYCD YCGEAIGVDQ GQMSHDGQHW HATDECFSCN
TCRCSLLGRA FLPRRGAIYC SIACSKGEPP TPSDSSGTGM YTTPTPPTQR VRPHPQAPLP
ARIPSSHASS SPPMSPQQQQ QHQATFNQAM YQMQSQQMEA AGGLVDQSKS YAASDSDAGV
VKDLEHGGHM GGGDLTDFSG GRASSTSQNL SPLNSPGDFQ PHFLPKPMEL QRDGVYNFNE
MSSNLDAAWS AKPTNSYHLQ RQLLENPHTA SMPELAGKLV APPAHMQHLS QLHAVSSHQF
QQHEYADILH PPPPPPGEIP ELPTPNLSVA STALPPELMG SPTHSAGDRS LNTPMSTQSA
SHAPPHPVSI LSGASSSSPM SGEPAKKKGV RFEGIPDTLP RSRSYSGNGA GTSGGGERER
DRDKDKEGGG RHGHGHSSRR RRRRKSSSSS SHHRSGSGHR SHSTTRADTY APAQPLSSSY
QGPPSVLQAA NLVHESPSRQ QRERERERER EESEESDVCS TCSSSSSSSE DYMMMYQLPQ
RRHYGGVRVS YVPNDALAYD RKRKPSELGG DKDKNCIIS
