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   13-FEB-2019, entry version 149.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   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
RT   from 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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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
RP   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
RT   project: 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
RP   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.,
RA   Bione S., Tamanini F., Neel B.G., Toniolo D., Comoglio P.M.;
RT   "A family of transmembrane proteins with homology to the MET-
RT   hepatocyte 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.,
RA   Tessier-Lavigne M., Comoglio P.M.;
RT   "Plexins are a large family of receptors for transmembrane, secreted
RT   and 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
RT   multiple 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
RP   BY 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
RP   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
CC       signaling by SEMA6A and class 3 semaphorins and subsequent
CC       remodeling of the cytoskeleton. Plays a role in axon guidance,
CC       invasive growth and cell migration. Class 3 semaphorins bind to a
CC       complex composed of a neuropilin and a plexin. The plexin
CC       modulates the affinity of the complex for specific semaphorins,
CC       and its cytoplasmic domain is required for the activation of down-
CC       stream signaling events in the cytoplasm (By similarity).
CC       {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
CC       with NRP1 and NRP2 (By similarity). Interacts with RND1.
CC       {ECO:0000250, ECO:0000269|Ref.9}.
CC   -!- INTERACTION:
CC       P39688:Fyn (xeno); NbExp=3; IntAct=EBI-308264, EBI-524514;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I 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=Translation N-terminally shortened.; 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   UniGene; Hs.497626; -.
DR   PDB; 3Q3J; X-ray; 1.97 A; A=1490-1600.
DR   PDBsum; 3Q3J; -.
DR   ProteinModelPortal; O75051; -.
DR   SMR; O75051; -.
DR   BioGrid; 111376; 46.
DR   CORUM; O75051; -.
DR   DIP; DIP-31672N; -.
DR   IntAct; O75051; 11.
DR   STRING; 9606.ENSP00000356000; -.
DR   CarbonylDB; O75051; -.
DR   iPTMnet; O75051; -.
DR   PhosphoSitePlus; O75051; -.
DR   SwissPalm; O75051; -.
DR   BioMuta; PLXNA2; -.
DR   EPD; O75051; -.
DR   jPOST; O75051; -.
DR   MaxQB; O75051; -.
DR   PaxDb; O75051; -.
DR   PeptideAtlas; O75051; -.
DR   PRIDE; O75051; -.
DR   ProteomicsDB; 49723; -.
DR   ProteomicsDB; 49724; -. [O75051-2]
DR   DNASU; 5362; -.
DR   Ensembl; ENST00000367033; ENSP00000356000; ENSG00000076356. [O75051-1]
DR   GeneID; 5362; -.
DR   KEGG; hsa:5362; -.
DR   UCSC; uc001hgz.4; human. [O75051-1]
DR   CTD; 5362; -.
DR   DisGeNET; 5362; -.
DR   EuPathDB; HostDB:ENSG00000076356.6; -.
DR   GeneCards; PLXNA2; -.
DR   HGNC; HGNC:9100; PLXNA2.
DR   HPA; CAB009763; -.
DR   MIM; 601054; gene.
DR   neXtProt; NX_O75051; -.
DR   OpenTargets; ENSG00000076356; -.
DR   PharmGKB; PA33426; -.
DR   eggNOG; ENOG410IN3A; Eukaryota.
DR   eggNOG; ENOG410ZA1D; LUCA.
DR   GeneTree; ENSGT00940000153318; -.
DR   HOVERGEN; HBG105711; -.
DR   InParanoid; O75051; -.
DR   KO; K06820; -.
DR   OMA; INISEDC; -.
DR   OrthoDB; 90434at2759; -.
DR   PhylomeDB; O75051; -.
DR   TreeFam; TF312962; -.
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   ChiTaRS; PLXNA2; human.
DR   EvolutionaryTrace; O75051; -.
DR   GeneWiki; PLXNA2; -.
DR   GenomeRNAi; 5362; -.
DR   PRO; PR:O75051; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000076356; Expressed in 202 organ(s), highest expression level in brain.
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   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; 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; 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   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   Complete proteome; Disulfide bond; Glycoprotein; Membrane;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       {ECO:0000255}.
FT   CHAIN        35   1894       Plexin-A2.
FT                                /FTId=PRO_0000232747.
FT   TOPO_DOM     35   1237       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1238   1258       Helical. {ECO:0000255}.
FT   TOPO_DOM   1259   1894       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       35    508       Sema. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00352}.
FT   DOMAIN      858    951       IPT/TIG 1.
FT   DOMAIN      954   1037       IPT/TIG 2.
FT   DOMAIN     1041   1139       IPT/TIG 3.
FT   DOMAIN     1143   1228       IPT/TIG 4.
FT   COILED     1261   1310       {ECO:0000255}.
FT   MOD_RES    1612   1612       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) asparagine.
FT   CARBOHYD     91     91       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    327    327       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    598    598       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    696    696       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    756    756       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1205   1205       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     94    103       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    129    137       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    284    405       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    300    356       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    374    393       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    511    528       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    517    559       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    520    537       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    531    543       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   DISULFID    594    613       {ECO:0000255|PROSITE-ProRule:PRU00352}.
FT   VAR_SEQ       1      1       M -> MGTLGQASLFAPPGNYFWSDHSALCFAESCEGQPGK
FT                                VEQMSTHRSRLLTAAPLSM (in isoform 2).
FT                                {ECO:0000303|PubMed:12975309}.
FT                                /FTId=VSP_017967.
FT   VAR_SEQ     458    498       IRADGPPHGGVQYEMVSVLKDGSPILRDMAFSIDQRYLYVM
FT                                -> VRVYEFRCSNAIHLLSKESLLEGSYWWRFNYRQLYFLG
FT                                EQR (in isoform 2).
FT                                {ECO:0000303|PubMed:12975309}.
FT                                /FTId=VSP_017968.
FT   VAR_SEQ     499   1894       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12975309}.
FT                                /FTId=VSP_017969.
FT   VARIANT       5      5       R -> Q (in dbSNP:rs2782948).
FT                                {ECO:0000269|PubMed:12975309}.
FT                                /FTId=VAR_056722.
FT   VARIANT      57     57       Q -> R (in dbSNP:rs11119014).
FT                                /FTId=VAR_059554.
FT   VARIANT     267    267       A -> T (in dbSNP:rs3748735).
FT                                /FTId=VAR_059555.
FT   VARIANT     369    369       E -> G (in dbSNP:rs4844658).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9455484}.
FT                                /FTId=VAR_058201.
FT   VARIANT     805    805       A -> G (in dbSNP:rs17011882).
FT                                /FTId=VAR_059556.
FT   VARIANT    1443   1443       A -> T (in dbSNP:rs12240051).
FT                                /FTId=VAR_059557.
FT   CONFLICT     94     94       C -> R (in Ref. 2; AAQ88860).
FT                                {ECO:0000305}.
FT   CONFLICT    599    599       L -> P (in Ref. 5; CAB57275).
FT                                {ECO:0000305}.
FT   CONFLICT    661    661       L -> P (in Ref. 5; CAB57275).
FT                                {ECO:0000305}.
FT   CONFLICT   1085   1085       N -> V (in Ref. 4; AAH09343).
FT                                {ECO:0000305}.
FT   CONFLICT   1378   1378       F -> L (in Ref. 5; CAB57275).
FT                                {ECO:0000305}.
FT   CONFLICT   1700   1700       F -> L (in Ref. 4; AAH09343).
FT                                {ECO:0000305}.
FT   STRAND     1499   1504       {ECO:0000244|PDB:3Q3J}.
FT   STRAND     1515   1520       {ECO:0000244|PDB:3Q3J}.
FT   HELIX      1525   1536       {ECO:0000244|PDB:3Q3J}.
FT   HELIX      1548   1550       {ECO:0000244|PDB:3Q3J}.
FT   STRAND     1551   1557       {ECO:0000244|PDB:3Q3J}.
FT   TURN       1558   1560       {ECO:0000244|PDB:3Q3J}.
FT   STRAND     1561   1565       {ECO:0000244|PDB:3Q3J}.
FT   STRAND     1567   1569       {ECO:0000244|PDB:3Q3J}.
FT   HELIX      1584   1587       {ECO:0000244|PDB:3Q3J}.
FT   STRAND     1594   1599       {ECO:0000244|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
//