PLXA2_HUMAN
ID PLXA2_HUMAN Reviewed; 1894 AA.
AC O75051; A2RTX9; B2RMX7; Q6UX61; Q96GN9; Q9BRL1; Q9UIW1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Plexin-A2;
DE AltName: Full=Semaphorin receptor OCT;
DE Flags: Precursor;
GN Name=PLXNA2; Synonyms=KIAA0463, OCT, PLXN2; ORFNames=UNQ209/PRO235;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-369.
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-5.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-369.
RC TISSUE=Brain, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 447-1774 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=8570614; DOI=10.1073/pnas.93.2.674;
RA Maestrini E., Tamagnone L., Longati P., Cremona O., Gulisano M., Bione S.,
RA Tamanini F., Neel B.G., Toniolo D., Comoglio P.M.;
RT "A family of transmembrane proteins with homology to the MET-hepatocyte
RT growth factor receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:674-678(1996).
RN [6]
RP FUNCTION.
RX PubMed=10520995; DOI=10.1016/s0092-8674(00)80063-x;
RA Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L.,
RA Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M., Tessier-Lavigne M.,
RA Comoglio P.M.;
RT "Plexins are a large family of receptors for transmembrane, secreted and
RT GPI-anchored semaphorins in vertebrates.";
RL Cell 99:71-80(1999).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1612, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 1490-1600 IN COMPLEX WITH RND1.
RG Structural genomics consortium (SGC);
RT "Crystal structure of plexin A2 RBD in complex with RND1.";
RL Submitted (JAN-2011) to the PDB data bank.
CC -!- FUNCTION: Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by
CC SEMA6A and class 3 semaphorins and subsequent remodeling of the
CC cytoskeleton. Plays a role in axon guidance, invasive growth and cell
CC migration. Class 3 semaphorins bind to a complex composed of a
CC neuropilin and a plexin. The plexin modulates the affinity of the
CC complex for specific semaphorins, and its cytoplasmic domain is
CC required for the activation of down-stream signaling events in the
CC cytoplasm (By similarity). {ECO:0000250, ECO:0000269|PubMed:10520995}.
CC -!- SUBUNIT: Homodimer. The PLXNA2 homodimer interacts with a SEMA6A
CC homodimer, giving rise to a heterotetramer. Interacts directly with
CC NRP1 and NRP2 (By similarity). Interacts with RND1. {ECO:0000250,
CC ECO:0000269|Ref.9}.
CC -!- INTERACTION:
CC O75051; P39688: Fyn; Xeno; NbExp=3; IntAct=EBI-308264, EBI-524514;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75051-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75051-2; Sequence=VSP_017967, VSP_017968, VSP_017969;
CC -!- TISSUE SPECIFICITY: Detected in fetal brain.
CC {ECO:0000269|PubMed:8570614}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32308.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007932; BAA32308.1; ALT_INIT; mRNA.
DR EMBL; AY358496; AAQ88860.1; -; mRNA.
DR EMBL; AL356275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006193; AAH06193.2; -; mRNA.
DR EMBL; BC009343; AAH09343.2; -; mRNA.
DR EMBL; BC132676; AAI32677.2; -; mRNA.
DR EMBL; BC136530; AAI36531.1; -; mRNA.
DR EMBL; X87831; CAB57275.1; -; mRNA.
DR CCDS; CCDS31013.1; -. [O75051-1]
DR RefSeq; NP_079455.3; NM_025179.3. [O75051-1]
DR PDB; 3Q3J; X-ray; 1.97 A; A=1490-1600.
DR PDBsum; 3Q3J; -.
DR AlphaFoldDB; O75051; -.
DR SMR; O75051; -.
DR BioGRID; 111376; 78.
DR CORUM; O75051; -.
DR DIP; DIP-31672N; -.
DR IntAct; O75051; 37.
DR STRING; 9606.ENSP00000356000; -.
DR CarbonylDB; O75051; -.
DR GlyGen; O75051; 9 sites.
DR iPTMnet; O75051; -.
DR PhosphoSitePlus; O75051; -.
DR SwissPalm; O75051; -.
DR BioMuta; PLXNA2; -.
DR EPD; O75051; -.
DR jPOST; O75051; -.
DR MassIVE; O75051; -.
DR MaxQB; O75051; -.
DR PaxDb; O75051; -.
DR PeptideAtlas; O75051; -.
DR PRIDE; O75051; -.
DR ProteomicsDB; 49723; -. [O75051-1]
DR ProteomicsDB; 49724; -. [O75051-2]
DR Antibodypedia; 4060; 188 antibodies from 27 providers.
DR DNASU; 5362; -.
DR Ensembl; ENST00000367033.4; ENSP00000356000.3; ENSG00000076356.7. [O75051-1]
DR GeneID; 5362; -.
DR KEGG; hsa:5362; -.
DR MANE-Select; ENST00000367033.4; ENSP00000356000.3; NM_025179.4; NP_079455.3.
DR UCSC; uc001hgz.4; human. [O75051-1]
DR CTD; 5362; -.
DR DisGeNET; 5362; -.
DR GeneCards; PLXNA2; -.
DR HGNC; HGNC:9100; PLXNA2.
DR HPA; ENSG00000076356; Tissue enhanced (pancreas).
DR MIM; 601054; gene.
DR neXtProt; NX_O75051; -.
DR OpenTargets; ENSG00000076356; -.
DR PharmGKB; PA33426; -.
DR VEuPathDB; HostDB:ENSG00000076356; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; O75051; -.
DR OMA; GQHHFTA; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; O75051; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; O75051; -.
DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR SignaLink; O75051; -.
DR SIGNOR; O75051; -.
DR BioGRID-ORCS; 5362; 10 hits in 1066 CRISPR screens.
DR ChiTaRS; PLXNA2; human.
DR EvolutionaryTrace; O75051; -.
DR GeneWiki; PLXNA2; -.
DR GenomeRNAi; 5362; -.
DR Pharos; O75051; Tbio.
DR PRO; PR:O75051; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75051; protein.
DR Bgee; ENSG00000076356; Expressed in ganglionic eminence and 178 other tissues.
DR Genevisible; O75051; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0017154; F:semaphorin receptor activity; ISS:UniProtKB.
DR GO; GO:0051642; P:centrosome localization; IEA:Ensembl.
DR GO; GO:0021935; P:cerebellar granule cell precursor tangential migration; IEA:Ensembl.
DR GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR CDD; cd11272; Sema_plexin_A2; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 6.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR042826; Plexin-A2_sema.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR041019; TIG1_plexin.
DR InterPro; IPR041362; TIG2_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF01437; PSI; 2.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 4.
DR Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 4.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1894
FT /note="Plexin-A2"
FT /id="PRO_0000232747"
FT TOPO_DOM 35..1237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1238..1258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1259..1894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..508
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 858..951
FT /note="IPT/TIG 1"
FT DOMAIN 954..1037
FT /note="IPT/TIG 2"
FT DOMAIN 1041..1139
FT /note="IPT/TIG 3"
FT DOMAIN 1143..1228
FT /note="IPT/TIG 4"
FT COILED 1261..1310
FT /evidence="ECO:0000255"
FT MOD_RES 1612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 129..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 284..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 300..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 374..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 511..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 517..559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 520..537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 531..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 594..613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 1
FT /note="M -> MGTLGQASLFAPPGNYFWSDHSALCFAESCEGQPGKVEQMSTHRSRL
FT LTAAPLSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_017967"
FT VAR_SEQ 458..498
FT /note="IRADGPPHGGVQYEMVSVLKDGSPILRDMAFSIDQRYLYVM -> VRVYEFR
FT CSNAIHLLSKESLLEGSYWWRFNYRQLYFLGEQR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_017968"
FT VAR_SEQ 499..1894
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_017969"
FT VARIANT 5
FT /note="R -> Q (in dbSNP:rs2782948)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_056722"
FT VARIANT 57
FT /note="Q -> R (in dbSNP:rs11119014)"
FT /id="VAR_059554"
FT VARIANT 267
FT /note="A -> T (in dbSNP:rs3748735)"
FT /id="VAR_059555"
FT VARIANT 369
FT /note="E -> G (in dbSNP:rs4844658)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9455484"
FT /id="VAR_058201"
FT VARIANT 805
FT /note="A -> G (in dbSNP:rs17011882)"
FT /id="VAR_059556"
FT VARIANT 1443
FT /note="A -> T (in dbSNP:rs12240051)"
FT /id="VAR_059557"
FT CONFLICT 94
FT /note="C -> R (in Ref. 2; AAQ88860)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="L -> P (in Ref. 5; CAB57275)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="L -> P (in Ref. 5; CAB57275)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="N -> V (in Ref. 4; AAH09343)"
FT /evidence="ECO:0000305"
FT CONFLICT 1378
FT /note="F -> L (in Ref. 5; CAB57275)"
FT /evidence="ECO:0000305"
FT CONFLICT 1700
FT /note="F -> L (in Ref. 4; AAH09343)"
FT /evidence="ECO:0000305"
FT STRAND 1499..1504
FT /evidence="ECO:0007829|PDB:3Q3J"
FT STRAND 1515..1520
FT /evidence="ECO:0007829|PDB:3Q3J"
FT HELIX 1525..1536
FT /evidence="ECO:0007829|PDB:3Q3J"
FT HELIX 1548..1550
FT /evidence="ECO:0007829|PDB:3Q3J"
FT STRAND 1551..1557
FT /evidence="ECO:0007829|PDB:3Q3J"
FT TURN 1558..1560
FT /evidence="ECO:0007829|PDB:3Q3J"
FT STRAND 1561..1565
FT /evidence="ECO:0007829|PDB:3Q3J"
FT STRAND 1567..1569
FT /evidence="ECO:0007829|PDB:3Q3J"
FT HELIX 1584..1587
FT /evidence="ECO:0007829|PDB:3Q3J"
FT STRAND 1594..1599
FT /evidence="ECO:0007829|PDB:3Q3J"
SQ SEQUENCE 1894 AA; 211104 MW; DFC3DE5BCBB40357 CRC64;
MEQRRPWPRA LEVDSRSVVL LSVVWVLLAP PAAGMPQFST FHSENRDWTF NHLTVHQGTG
AVYVGAINRV YKLTGNLTIQ VAHKTGPEED NKSCYPPLIV QPCSEVLTLT NNVNKLLIID
YSENRLLACG SLYQGVCKLL RLDDLFILVE PSHKKEHYLS SVNKTGTMYG VIVRSEGEDG
KLFIGTAVDG KQDYFPTLSS RKLPRDPESS AMLDYELHSD FVSSLIKIPS DTLALVSHFD
IFYIYGFASG GFVYFLTVQP ETPEGVAINS AGDLFYTSRI VRLCKDDPKF HSYVSLPFGC
TRAGVEYRLL QAAYLAKPGD SLAQAFNITS QDDVLFAIFS KGQKQYHHPP DDSALCAFPI
RAINLQIKER LQSCYQGEGN LELNWLLGKD VQCTKAPVPI DDNFCGLDIN QPLGGSTPVE
GLTLYTTSRD RMTSVASYVY NGYSVVFVGT KSGKLKKIRA DGPPHGGVQY EMVSVLKDGS
PILRDMAFSI DQRYLYVMSE RQVTRVPVES CEQYTTCGEC LSSGDPHCGW CALHNMCSRR
DKCQQAWEPN RFAASISQCV SLAVHPSSIS VSEHSRLLSL VVSDAPDLSA GIACAFGNLT
EVEGQVSGSQ VICISPGPKD VPVIPLDQDW FGLELQLRSK ETGKIFVSTE FKFYNCSAHQ
LCLSCVNSAF RCHWCKYRNL CTHDPTTCSF QEGRINISED CPQLVPTEEI LIPVGEVKPI
TLKARNLPQP QSGQRGYECV LNIQGAIHRV PALRFNSSSV QCQNSSYQYD GMDISNLAVD
FAVVWNGNFI IDNPQDLKVH LYKCAAQRES CGLCLKADRK FECGWCSGER RCTLHQHCTS
PSSPWLDWSS HNVKCSNPQI TEILTVSGPP EGGTRVTIHG VNLGLDFSEI AHHVQVAGVP
CTPLPGEYII AEQIVCEMGH ALVGTTSGPV RLCIGECKPE FMTKSHQQYT FVNPSVLSLN
PIRGPESGGT MVTITGHYLG AGSSVAVYLG NQTCEFYGRS MSEIVCVSPP SSNGLGPVPV
SVSVDRAHVD SNLQFEYIDD PRVQRIEPEW SIASGHTPLT ITGFNLDVIQ EPRIRVKFNG
KESVNVCKVV NTTTLTCLAP SLTTDYRPGL DTVERPDEFG FVFNNVQSLL IYNDTKFIYY
PNPTFELLSP TGVLDQKPGS PIILKGKNLC PPASGGAKLN YTVLIGETPC AVTVSETQLL
CEPPNLTGQH KVMVHVGGMV FSPGSVSVIS DSLLTLPAIV SIAAGGSLLL IIVIIVLIAY
KRKSRENDLT LKRLQMQMDN LESRVALECK EAFAELQTDI NELTSDLDRS GIPYLDYRTY
AMRVLFPGIE DHPVLRELEV QGNGQQHVEK ALKLFAQLIN NKVFLLTFIR TLELQRSFSM
RDRGNVASLI MTGLQGRLEY ATDVLKQLLS DLIDKNLENK NHPKLLLRRT ESVAEKMLTN
WFAFLLHKFL KECAGEPLFM LYCAIKQQME KGPIDAITGE ARYSLSEDKL IRQQIEYKTL
ILNCVNPDNE NSPEIPVKVL NCDTITQVKE KILDAVYKNV PYSQRPRAVD MDLEWRQGRI
ARVVLQDEDI TTKIEGDWKR LNTLMHYQVS DRSVVALVPK QTSSYNIPAS ASISRTSISR
YDSSFRYTGS PDSLRSRAPM ITPDLESGVK VWHLVKNHDH GDQKEGDRGS KMVSEIYLTR
LLATKGTLQK FVDDLFETLF STVHRGSALP LAIKYMFDFL DEQADRHSIH DTDVRHTWKS
NCLPLRFWVN VIKNPQFVFD IHKGSITDAC LSVVAQTFMD SCSTSEHRLG KDSPSNKLLY
AKDIPSYKSW VERYYADIAK LPAISDQDMN AYLAEQSRLH AVEFNMLSAL NEIYSYVSKY
SEELIGALEQ DEQARRQRLA YKVEQLINAM SIES
