PTPRS_CHICK
ID PTPRS_CHICK Reviewed; 1516 AA.
AC F1NWE3; Q90815;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 3.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase S;
DE Short=R-PTP-S;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:B0V2N1};
DE AltName: Full=Chick receptor tyrosine phosphatase alpha {ECO:0000303|PubMed:7918104};
DE Short=CRYP alpha {ECO:0000303|PubMed:7600997};
DE Short=CRYPalpha {ECO:0000303|PubMed:7918104};
DE Flags: Precursor;
GN Name=PTPRS;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|Proteomes:UP000000539};
RN [1] {ECO:0000312|EMBL:AAA64460.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic brain {ECO:0000312|EMBL:AAA64460.1};
RX PubMed=7918104; DOI=10.1016/0925-4773(94)90071-x;
RA Stoker A.W.;
RT "Isoforms of a novel cell adhesion molecule-like protein tyrosine
RT phosphatase are implicated in neural development.";
RL Mech. Dev. 46:201-217(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7600997; DOI=10.1242/dev.121.6.1833;
RA Stoker A.W., Gehrig B., Haj F., Bay B.H.;
RT "Axonal localisation of the CAM-like tyrosine phosphatase CRYP alpha: a
RT signalling molecule of embryonic growth cones.";
RL Development 121:1833-1844(1995).
RN [4]
RP FUNCTION, INTERACTION WITH AGRN AND COL18A1, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF 67-LYS--LYS-71; ARG-96 AND ARG-99.
RX PubMed=11865065; DOI=10.1128/mcb.22.6.1881-1892.2002;
RA Aricescu A.R., McKinnell I.W., Halfter W., Stoker A.W.;
RT "Heparan sulfate proteoglycans are ligands for receptor protein tyrosine
RT phosphatase sigma.";
RL Mol. Cell. Biol. 22:1881-1892(2002).
RN [5]
RP FUNCTION, INTERACTION WITH NTRK1 AND NTRK3, AND SUBCELLULAR LOCATION.
RX PubMed=17967490; DOI=10.1016/j.bbamcr.2007.06.008;
RA Faux C., Hawadle M., Nixon J., Wallace A., Lee S., Murray S., Stoker A.;
RT "PTPsigma binds and dephosphorylates neurotrophin receptors and can
RT suppress NGF-dependent neurite outgrowth from sensory neurons.";
RL Biochim. Biophys. Acta 1773:1689-1700(2007).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17178832; DOI=10.1128/mcb.00535-06;
RA Lee S., Faux C., Nixon J., Alete D., Chilton J., Hawadle M., Stoker A.W.;
RT "Dimerization of protein tyrosine phosphatase sigma governs both ligand
RT binding and isoform specificity.";
RL Mol. Cell. Biol. 27:1795-1808(2007).
RN [7] {ECO:0007744|PDB:2YD4}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 29-226, AND DISULFIDE BONDS.
RX PubMed=21454754; DOI=10.1126/science.1200840;
RA Coles C.H., Shen Y., Tenney A.P., Siebold C., Sutton G.C., Lu W.,
RA Gallagher J.T., Jones E.Y., Flanagan J.G., Aricescu A.R.;
RT "Proteoglycan-specific molecular switch for RPTPsigma clustering and
RT neuronal extension.";
RL Science 332:484-488(2011).
RN [8] {ECO:0007744|PDB:4PBV, ECO:0007744|PDB:4PBW}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-316 IN COMPLEX WITH NTRK3,
RP INTERACTION WITH NTRK3, AND DISULFIDE BONDS.
RX PubMed=25385546; DOI=10.1038/ncomms6209;
RA Coles C.H., Mitakidis N., Zhang P., Elegheert J., Lu W., Stoker A.W.,
RA Nakagawa T., Craig A.M., Jones E.Y., Aricescu A.R.;
RT "Structural basis for extracellular cis and trans RPTPsigma signal
RT competition in synaptogenesis.";
RL Nat. Commun. 5:5209-5209(2014).
CC -!- FUNCTION: Cell surface receptor that binds to glycosaminoglycans,
CC including chondroitin sulfate proteoglycans and heparan sulfate
CC proteoglycans (PubMed:11865065, PubMed:17178832). Binding to
CC chondroitin sulfate and heparan sulfate proteoglycans has opposite
CC effects on PTPRS oligomerization and regulation of neurite outgrowth
CC (By similarity). Contributes to the inhibition of neurite and axonal
CC outgrowth by chondroitin sulfate proteoglycans, also after nerve
CC transection (PubMed:17967490). Plays a role in stimulating neurite
CC outgrowth in response to the heparan sulfate proteoglycan GPC2.
CC Required for normal brain development, especially for normal
CC development of the pituitary gland and the olfactory bulb. Functions as
CC tyrosine phosphatase (PubMed:17967490). Mediates dephosphorylation of
CC NTRK1, NTRK2 and NTRK3 (PubMed:17967490). Plays a role in down-
CC regulation of signaling cascades that lead to the activation of Akt and
CC MAP kinases. Down-regulates TLR9-mediated activation of NF-kappa-B, as
CC well as production of TNF, interferon alpha and interferon beta (By
CC similarity). {ECO:0000250|UniProtKB:B0V2N1,
CC ECO:0000269|PubMed:11865065, ECO:0000269|PubMed:17178832,
CC ECO:0000269|PubMed:17967490}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Homodimer (PubMed:17178832). Binding to large heparan sulfate
CC proteoglycan structures promotes oligomerization. Binding to
CC chondroitin sulfate proteoglycan does not lead to oligomerization (By
CC similarity). Interacts (via Ig-like domains) with NTRK1 and NTRK3, but
CC does not form detectable complexes with NTRK2 (PubMed:17967490,
CC PubMed:25385546). Interacts (via extracellular domain) with the heparan
CC sulfate proteoglycans AGRN and COL18A1 (PubMed:11865065).
CC {ECO:0000250|UniProtKB:B0V2N1, ECO:0000250|UniProtKB:Q13332,
CC ECO:0000269|PubMed:11865065, ECO:0000269|PubMed:17178832,
CC ECO:0000269|PubMed:17967490, ECO:0000269|PubMed:25385546}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17178832,
CC ECO:0000305|PubMed:17967490}; Single-pass type I membrane protein
CC {ECO:0000305|PubMed:17967490}. Cell projection, axon
CC {ECO:0000269|PubMed:7600997}. Perikaryon
CC {ECO:0000250|UniProtKB:B0V2N1}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:Q64605}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:Q64605}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q64605}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:B0V2N1}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:B0V2N1}. Note=Detected along neurites and at
CC axon growth cones. {ECO:0000269|PubMed:7600997}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F1NWE3-1; Sequence=Displayed;
CC Name=2; Synonyms=CRYPalpha1 {ECO:0000303|PubMed:7918104};
CC IsoId=F1NWE3-2; Sequence=VSP_058832, VSP_058833, VSP_058834;
CC -!- TISSUE SPECIFICITY: Detected in embryonic brain, dorsal root ganglion
CC and spinal cord (PubMed:7600997). Detected in embryonic retina (at
CC protein level) (PubMed:11865065). Detected in embryonic brain, spinal
CC cord, dorsal root ganglion, trigeminal ganglion, ganglia associated
CC with the precardinal vein and vagus nerve, the inner and outer nuclear
CC layer of the retina, limb, breast muscle, heart, gut and lung.
CC {ECO:0000269|PubMed:11865065, ECO:0000269|PubMed:7600997,
CC ECO:0000269|PubMed:7918104}.
CC -!- PTM: A cleavage occurs, separating the extracellular domain from the
CC transmembrane segment. This process called 'ectodomain shedding' is
CC thought to be involved in receptor desensitization, signal transduction
CC and/or membrane localization (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; L32780; AAA64460.1; -; mRNA.
DR EMBL; AADN04000371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; I50212; I50212.
DR RefSeq; NP_990738.1; NM_205407.1.
DR PDB; 2YD4; X-ray; 1.65 A; A=29-226.
DR PDB; 4PBV; X-ray; 2.50 A; C/D/E=29-320.
DR PDB; 4PBW; X-ray; 3.05 A; D/E/F=29-320.
DR PDBsum; 2YD4; -.
DR PDBsum; 4PBV; -.
DR PDBsum; 4PBW; -.
DR AlphaFoldDB; F1NWE3; -.
DR SMR; F1NWE3; -.
DR STRING; 9031.ENSGALP00000006433; -.
DR GeneID; 396375; -.
DR KEGG; gga:396375; -.
DR CTD; 5802; -.
DR VEuPathDB; HostDB:geneid_396375; -.
DR eggNOG; KOG4228; Eukaryota.
DR HOGENOM; CLU_001645_0_1_1; -.
DR OrthoDB; 220353at2759; -.
DR PRO; PR:F1NWE3; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISS:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; ISS:UniProtKB.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 7.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Heparin-binding;
KW Hydrolase; Immunoglobulin domain; Membrane; Protein phosphatase; Receptor;
KW Reference proteome; Repeat; Signal; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1516
FT /note="Receptor-type tyrosine-protein phosphatase S"
FT /id="PRO_5008954162"
FT TOPO_DOM 29..854
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..1516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..122
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 134..223
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 235..317
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 324..414
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 419..513
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 517..606
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 608..692
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 961..1216
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1248..1507
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 67..71
FT /note="Important for binding to glycosaminoglycan chains"
FT /evidence="ECO:0000269|PubMed:11865065"
FT ACT_SITE 1157
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1448
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 53..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 256..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 226..229
FT /note="Missing (in isoform 2)"
FT /id="VSP_058832"
FT VAR_SEQ 880
FT /note="N -> NKPDS (in isoform 2)"
FT /id="VSP_058833"
FT VAR_SEQ 918..934
FT /note="DSGLSSPLSDPEFDFES -> G (in isoform 2)"
FT /id="VSP_058834"
FT MUTAGEN 67..71
FT /note="KKGKK->AAGAA: Loss of heparin binding."
FT /evidence="ECO:0000269|PubMed:11865065"
FT MUTAGEN 96
FT /note="R->A: Loss of heparin binding; when associated with
FT A-99."
FT /evidence="ECO:0000269|PubMed:11865065"
FT MUTAGEN 99
FT /note="R->A: Loss of heparin binding; when associated with
FT A-96."
FT /evidence="ECO:0000269|PubMed:11865065"
FT CONFLICT 1339
FT /note="H -> N (in Ref. 1; AAA64460)"
FT /evidence="ECO:0000305"
FT CONFLICT 1487
FT /note="Missing (in Ref. 1; AAA64460)"
FT /evidence="ECO:0000305"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:2YD4"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2YD4"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:2YD4"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2YD4"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2YD4"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4PBW"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:2YD4"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2YD4"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:2YD4"
SQ SEQUENCE 1516 AA; 170604 MW; F577A09B7CA138C0 CRC64;
MRILPSPGMP ALLSLVSLLS VLLMGCVAES PPVFIKKPVD QIGVSGGVAS FVCQATGDPK
PRVTWNKKGK KVNSQRFETI EFDESAGAVL RIQPLRTPRD ENIYECVAQN PHGEVTVHAK
LTVLREDQLP PGFPNIDMGP QLKVVERTRT ATMLCAASGN PDPEITWFKD FLPVDPSTSN
GRIKQLRSGG LQIESSEETD QGKYECVASN SAGVRYSSPA NLYVRELREV RRVAPRFSIL
PVSHEIMPGG NVNITCVAVG SPMPYVKWMQ GAEDLTPEDD MPVGRNVLEL TDVKDSANYT
CVAMSSLGVI EAVAQITVKS LPKAPGTPVV TETTATSITI TWDSGNPDPV SYYVIEYKSK
SQDGPYQIKE DITTTRYSIG GLSPNSEYEI WVSAVNSIGQ GPPSESVVTR TGEQAPASAP
RNVQGRMLSS TTMIIQWEEP VEPNGQIRGY RVYYTMEPDQ PVSNWQKHNV DDSLLTTVGS
LLEDETYTVR VLAFTSVGDG PLSDPIQVKT QQGVPGQPMN FRAEAKTETS IVLSWSPPRQ
EIIVKYELLF KEGDHGREVP RNFEPTTSFT VEGLKPNTEY VFRLAARSAL GLGAFTPEVR
ERTLQSILPK NFKVKMVTKT SVLLSWEFPE NYNSPTPYKI QYNGLNVDVD GRTTKKLITN
LKPHTFYNFV LMNRGNSMGG LQQNVAAWTA ANMLSRKPEV THKPDADGNV VVILPDVKSS
VAVQAYYIVV VPLRKSRGGQ FLNPLGSPEE MDLEELIQDI ARLRRRSLRH SRQLDFPKPY
IAARFRSLPN HFVLGDMKHY DNFENRALEP GQRYVIFILA VLQEPEATFA ASPFSDPIQL
DNPDPQPIID GEEGLIWVIG PVLAVVFIIC IVIAILLYKN KRKDSEPRTK CLLNNAEITP
HHPKDPVEMR RINFQTPDSG LSSPLSDPEF DFESMLSHPP IPVSELAEHT EHLKANDNLK
LSQEYESIDP GQQFTWEHSN LEVNKPKNRY ANVIAYDHSR VILLPIEGIV GSDYINANYI
DGYRKQNAYI ATQGPLPETF GDFWRMVWEQ RSATIVMMTK LEEKSRIKCD QYWPGRGTDT
YGMIQVTLLD TIELATFCVR TFSLHKNGSS EKREVRQFQF TAWPDHGVPE YPTPFLAFLR
RVKTCNPPDA GPIVVHCSAG VGRTGCFIVI DAMLERIKHE KTVDIYGHVT LMRSQRNYMV
QTEDQYSFIH DALLEAVACG NTEVPARNLY TYIQKLAQIE VGEHVTGMEL EFKRLANSKA
HTSRFISANL PCNKFKNRLV NIMPYETTRV CLQPIRGVEG SDYINASFID GYRQQKAYIA
TQGPLAETTE DFWRMLWEHN STIVVMLTKL REMGREKCHQ YWPAERSARY QYFVVDPMAE
YNMPQYILRE FKVTDARDGQ SRTVRQFQFT DWPEQGVPKS GEGFIDFIGQ VHKTKEQFGQ
DGPISVHCSA GVGRTGVFIT LSIVLERMRY EGVVDIFQTV KMLRTQRPAM VQTEDEYQFC
YQAALEYLGS FDHYAT
