ID NRX1A_BOVIN Reviewed; 1530 AA.
AC Q28146;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 177.
DE RecName: Full=Neurexin-1;
DE AltName: Full=Neurexin I-alpha;
DE AltName: Full=Neurexin-1-alpha;
DE Flags: Precursor;
GN Name=NRXN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=7695896; DOI=10.1016/0896-6273(95)90306-2;
RA Ullrich B., Ushkaryov Y.A., Suedhof T.C.;
RT "Cartography of neurexins: more than 1000 isoforms generated by alternative
RT splicing and expressed in distinct subsets of neurons.";
RL Neuron 14:497-507(1995).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, INTERACTION WITH ALPHA-LATROTOXIN, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Brain;
RX PubMed=1621094; DOI=10.1126/science.1621094;
RA Ushkaryov Y.A., Petrenko A.G., Geppert M., Suedhof T.C.;
RT "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin
RT receptor and laminin.";
RL Science 257:50-56(1992).
RN [3]
RP INTERACTION WITH NXPH1.
RX PubMed=8699246; DOI=10.1523/jneurosci.16-14-04360.1996;
RA Petrenko A.G., Ullrich B., Missler M., Krasnoperov V., Rosahl T.W.,
RA Suedhof T.C.;
RT "Structure and evolution of neurexophilin.";
RL J. Neurosci. 16:4360-4369(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 295-491, AND CALCIUM-BINDING.
RX PubMed=16772286; DOI=10.1074/jbc.m603464200;
RA Sheckler L.R., Henry L., Sugita S., Suedhof T.C., Rudenko G.;
RT "Crystal structure of the second LNS/LG domain from neurexin 1alpha: Ca2+
RT binding and the effects of alternative splicing.";
RL J. Biol. Chem. 281:22896-22905(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF 737-925 IN COMPLEX WITH CALCIUM,
RP ALTERNATIVE SPLICING, AND DISULFIDE BOND.
RX PubMed=18334217; DOI=10.1016/j.str.2008.01.005;
RA Shen K.C., Kuczynska D.A., Wu I.J., Murray B.H., Sheckler L.R., Rudenko G.;
RT "Regulation of neurexin 1beta tertiary structure and ligand binding through
RT alternative splicing.";
RL Structure 16:422-431(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 923-1353, GLYCOSYLATION AT
RP ASN-1246, INTERACTION WITH NLGN1, ELECTRON MICROSCOPY, AND DISULFIDE BONDS.
RX PubMed=21552542; DOI=10.1371/journal.pone.0019411;
RA Tanaka H., Nogi T., Yasui N., Iwasaki K., Takagi J.;
RT "Structural basis for variant-specific neuroligin-binding by alpha-
RT neurexin.";
RL PLoS ONE 6:E19411-E19411(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 296-1349, GLYCOSYLATION AT
RP SER-705 AND ASN-1246, INTERACTION WITH NLGN1, AND DISULFIDE BONDS.
RX PubMed=21620717; DOI=10.1016/j.str.2011.03.011;
RA Miller M.T., Mileni M., Comoletti D., Stevens R.C., Harel M., Taylor P.;
RT "The crystal structure of the alpha-neurexin-1 extracellular region reveals
RT a hinge point for mediating synaptic adhesion and function.";
RL Structure 19:767-778(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 31-1355, GLYCOSYLATION AT
RP ASN-1246, AND DISULFIDE BONDS.
RX PubMed=21620716; DOI=10.1016/j.str.2011.03.012;
RA Chen F., Venugopal V., Murray B., Rudenko G.;
RT "The structure of neurexin 1alpha reveals features promoting a role as
RT synaptic organizer.";
RL Structure 19:779-789(2011).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions,
CC exocytosis of secretory granules and regulation of signal transmission.
CC Function is isoform-specific. Alpha-type isoforms have a long N-
CC terminus with six laminin G-like domains and play an important role in
CC synaptic signal transmission. Alpha-type isoforms play a role in the
CC regulation of calcium channel activity and Ca(2+)-triggered
CC neurotransmitter release at synapses and at neuromuscular junctions.
CC They play an important role in Ca(2+)-triggered exocytosis of secretory
CC granules in pituitary gland. They may affect their functions at
CC synapses and in endocrine cells via their interactions with proteins
CC from the exocytotic machinery. Likewise, alpha-type isoforms play a
CC role in regulating the activity of postsynaptic NMDA receptors, a
CC subtype of glutamate-gated ion channels. Both alpha-type and beta-type
CC isoforms may play a role in the formation or maintenance of synaptic
CC junctions via their interactions (via the extracellular domains) with
CC neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de
CC novo formation of presynaptic structures. May be involved in
CC specification of excitatory synapses. Alpha-type isoforms were first
CC identified as receptors for alpha-latrotoxin from spider venom.
CC {ECO:0000250|UniProtKB:Q9CS84}.
CC -!- SUBUNIT: Interacts (via laminin G-like domain 2 and/or laminin G-like
CC domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer
CC interacts with one NRXN1 dimer (PubMed:21552542, PubMed:21620717). Also
CC interacts (via laminin G-like domain 2 and/or laminin G-like domain 6)
CC with NLGN2, NLGN3 and NLGN4L; interactions with NLGN1, NLGN2, NLGN3 and
CC NLGN4L are calcium-dependent (By similarity). Interacts (via
CC cytoplasmic C-terminal region) with CASK (via the PDZ, SH3 and
CC guanylate kinase-like domains) (By similarity). Interacts (via
CC cytoplasmic C-terminus) with CASKIN1 and APBA1 (By similarity).
CC Interacts (via laminin G-like domain 2) with NXPH1 and NXPH3
CC (PubMed:8699246). Alpha-type isoforms (neurexin-1-alpha) interact (via
CC laminin G-like domain 2 and/or laminin G-like domain 6) with DAG1 (via
CC alpha-dystroglycan chain) (By similarity). Interacts with LRRTM1,
CC LRRTM2, LRRTM3 and LRRTM4 (By similarity). Interacts with SYT13 and
CC SYTL1 (By similarity). Interacts with CBLN1, CBLN2 and, less avidly,
CC with CBLN4 (By similarity). Interacts with CLSTN3 (By similarity).
CC Alpha-type isoforms interact with alpha-latrotoxin from spider venom
CC (PubMed:1621094). {ECO:0000250|UniProtKB:Q63372,
CC ECO:0000250|UniProtKB:Q9CS84, ECO:0000269|PubMed:1621094,
CC ECO:0000269|PubMed:21552542, ECO:0000269|PubMed:21620717,
CC ECO:0000269|PubMed:8699246}.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9CS84}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=16;
CC Comment=A number of isoforms alpha-type and beta-type are produced by
CC alternative promoter usage. Beta-type isoforms differ from alpha-type
CC isoforms in their N-terminus. In addition, there are at least five
CC alternatively spliced sites, each of which may be spliced in up to
CC seven different ways. Combinatorial splicing at each of these sites
CC may lead to the generation of at least 96 isoforms. Experimental
CC confirmation may be lacking for some isoforms.
CC {ECO:0000269|PubMed:18334217, ECO:0000269|PubMed:7695896};
CC Name=1a; Synonyms=Alpha-1A2A3A4A5A;
CC IsoId=Q28146-1; Sequence=Displayed;
CC Name=2a; Synonyms=Alpha-1B;
CC IsoId=Q28146-2; Sequence=VSP_003478;
CC Name=3a; Synonyms=Alpha-1C;
CC IsoId=Q28146-3; Sequence=VSP_003474, VSP_003478;
CC Name=4a; Synonyms=Alpha-1D;
CC IsoId=Q28146-4; Sequence=VSP_003477;
CC Name=5a; Synonyms=Alpha-1E;
CC IsoId=Q28146-5; Sequence=VSP_003474, VSP_003477;
CC Name=6a; Synonyms=Alpha-1F;
CC IsoId=Q28146-6; Sequence=VSP_003476, VSP_003478;
CC Name=7a; Synonyms=Alpha-1G;
CC IsoId=Q28146-7; Sequence=VSP_003475;
CC Name=8a; Synonyms=Alpha-2B;
CC IsoId=Q28146-8; Sequence=VSP_003480;
CC Name=9a; Synonyms=Alpha-2C;
CC IsoId=Q28146-9; Sequence=VSP_003479;
CC Name=10a; Synonyms=Alpha-3B;
CC IsoId=Q28146-10; Sequence=VSP_003481;
CC Name=11a; Synonyms=Alpha-4B;
CC IsoId=Q28146-11; Sequence=VSP_003482;
CC Name=12a; Synonyms=Alpha-5B;
CC IsoId=Q28146-12; Sequence=VSP_003483;
CC Name=1b; Synonyms=Beta-4A5A;
CC IsoId=Q28142-1; Sequence=External;
CC Name=2b; Synonyms=Beta-4A5B;
CC IsoId=Q28142-2; Sequence=External;
CC Name=3b; Synonyms=Beta-4B5A;
CC IsoId=Q28142-3; Sequence=External;
CC Name=4b; Synonyms=Beta-4B5B;
CC IsoId=Q28142-4; Sequence=External;
CC -!- PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate
CC attachment is required for synapse development by mediating
CC interactions with neuroligins and LRRTM2.
CC {ECO:0000250|UniProtKB:Q9CS84}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; L14855; AAA74123.1; -; mRNA.
DR PIR; I45944; I45944.
DR RefSeq; NP_776829.1; NM_174404.2. [Q28146-1]
DR PDB; 2H0B; X-ray; 2.10 A; A/B/C/D=295-491.
DR PDB; 2R16; X-ray; 1.04 A; A=737-925.
DR PDB; 3ASI; X-ray; 2.30 A; A=923-1353.
DR PDB; 3POY; X-ray; 3.02 A; A=296-1349.
DR PDB; 3QCW; X-ray; 2.65 A; A/B=31-1355.
DR PDB; 3R05; X-ray; 2.95 A; A/B=31-1355.
DR PDB; 6CW1; X-ray; 2.84 A; A/B=258-690.
DR PDBsum; 2H0B; -.
DR PDBsum; 2R16; -.
DR PDBsum; 3ASI; -.
DR PDBsum; 3POY; -.
DR PDBsum; 3QCW; -.
DR PDBsum; 3R05; -.
DR PDBsum; 6CW1; -.
DR AlphaFoldDB; Q28146; -.
DR SMR; Q28146; -.
DR DIP; DIP-59135N; -.
DR IntAct; Q28146; 1.
DR STRING; 9913.ENSBTAP00000053469; -.
DR GlyCosmos; Q28146; 5 sites, No reported glycans.
DR iPTMnet; Q28146; -.
DR PaxDb; 9913-ENSBTAP00000033006; -.
DR GeneID; 281950; -.
DR KEGG; bta:281950; -.
DR CTD; 9378; -.
DR eggNOG; KOG3514; Eukaryota.
DR InParanoid; Q28146; -.
DR OrthoDB; 2999458at2759; -.
DR EvolutionaryTrace; Q28146; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097109; F:neuroligin family protein binding; IPI:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00110; LamG; 6.
DR DisProt; DP02503; -.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF51; NEUREXIN-1; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing; Calcium;
KW Cell adhesion; Cell membrane; Cell projection; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Glycoprotein; Heparan sulfate; Membrane;
KW Metal-binding; Proteoglycan; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000250|UniProtKB:Q63372"
FT CHAIN 31..1530
FT /note="Neurexin-1"
FT /id="PRO_0000019489"
FT TOPO_DOM 31..1454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1455..1475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1476..1530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..212
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 213..256
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 299..496
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 503..695
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 699..736
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 741..914
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 928..1103
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1106..1143
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1149..1347
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 199..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1523
FT /note="Interaction with CASK"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT COMPBIAS 1497..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18334217"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18334217"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18334217"
FT BINDING 788
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18334217"
FT BINDING 805
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18334217"
FT BINDING 864
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18334217"
FT BINDING 1199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT BINDING 1216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT BINDING 1298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT BINDING 1300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000305|PubMed:21620717"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21552542,
FT ECO:0000269|PubMed:21620716, ECO:0000269|PubMed:21620717"
FT CARBOHYD 1408
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT DISULFID 228..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 245..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 460..496
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 666..695
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 703..714
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 708..723
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 725..735
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 906..914
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 1075..1103
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 1110..1121
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 1115..1130
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT DISULFID 1132..1142
FT /evidence="ECO:0000269|PubMed:21620716,
FT ECO:0000269|PubMed:21620717"
FT VAR_SEQ 258..293
FT /note="Missing (in isoform 7a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003475"
FT VAR_SEQ 258
FT /note="Missing (in isoform 3a and isoform 5a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003474"
FT VAR_SEQ 264..273
FT /note="Missing (in isoform 6a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003476"
FT VAR_SEQ 274..293
FT /note="Missing (in isoform 4a and isoform 5a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003477"
FT VAR_SEQ 278..293
FT /note="Missing (in isoform 2a, isoform 3a and isoform 6a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003478"
FT VAR_SEQ 395..409
FT /note="Missing (in isoform 9a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003479"
FT VAR_SEQ 403..409
FT /note="Missing (in isoform 8a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003480"
FT VAR_SEQ 806..815
FT /note="DCIRINCNSS -> G (in isoform 10a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003481"
FT VAR_SEQ 1263..1292
FT /note="Missing (in isoform 11a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003482"
FT VAR_SEQ 1426..1428
FT /note="Missing (in isoform 12a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003483"
FT STRAND 299..311
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 317..331
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 355..364
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:2H0B"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:2H0B"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:3POY"
FT STRAND 458..470
FT /evidence="ECO:0007829|PDB:2H0B"
FT HELIX 475..481
FT /evidence="ECO:0007829|PDB:2H0B"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:2H0B"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:6CW1"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:3R05"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 522..532
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:3QCW"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:6CW1"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 572..581
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:3R05"
FT STRAND 599..606
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 636..640
FT /evidence="ECO:0007829|PDB:3QCW"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 665..672
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:3QCW"
FT HELIX 679..682
FT /evidence="ECO:0007829|PDB:3QCW"
FT TURN 684..687
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 691..694
FT /evidence="ECO:0007829|PDB:3QCW"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:3QCW"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:3R05"
FT STRAND 713..716
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 718..724
FT /evidence="ECO:0007829|PDB:3QCW"
FT TURN 726..729
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 741..747
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 750..770
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 774..782
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 784..786
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 789..795
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 798..805
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 819..823
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 833..840
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 843..848
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 853..857
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:3QCW"
FT STRAND 865..874
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 889..897
FT /evidence="ECO:0007829|PDB:2R16"
FT HELIX 902..907
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 914..916
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 919..921
FT /evidence="ECO:0007829|PDB:2R16"
FT STRAND 930..932
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 934..936
FT /evidence="ECO:0007829|PDB:3POY"
FT STRAND 938..942
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 950..957
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 963..971
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 975..981
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 984..993
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 995..999
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1008..1010
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1012..1018
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1023..1028
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1031..1036
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1049..1052
FT /evidence="ECO:0007829|PDB:3ASI"
FT HELIX 1056..1061
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1069..1071
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1074..1083
FT /evidence="ECO:0007829|PDB:3ASI"
FT TURN 1088..1091
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1093..1102
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1114..1116
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1120..1123
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1125..1131
FT /evidence="ECO:0007829|PDB:3ASI"
FT TURN 1133..1135
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1136..1139
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1148..1161
FT /evidence="ECO:0007829|PDB:3ASI"
FT HELIX 1164..1166
FT /evidence="ECO:0007829|PDB:3R05"
FT STRAND 1170..1180
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1184..1193
FT /evidence="ECO:0007829|PDB:3ASI"
FT TURN 1195..1197
FT /evidence="ECO:0007829|PDB:3POY"
FT STRAND 1200..1206
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1209..1219
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1221..1224
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1232..1234
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1236..1243
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1246..1251
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1257..1259
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1302..1309
FT /evidence="ECO:0007829|PDB:3ASI"
FT TURN 1310..1313
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1318..1325
FT /evidence="ECO:0007829|PDB:3ASI"
FT HELIX 1330..1335
FT /evidence="ECO:0007829|PDB:3ASI"
FT STRAND 1341..1350
FT /evidence="ECO:0007829|PDB:3ASI"
SQ SEQUENCE 1530 AA; 167939 MW; 8A4E4A75C4EC03D1 CRC64;
MGTALLQRGG CFLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLTDTPVN DGAWHNVRIR
RQFRNTTLFI DQVEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF
KGWIRDVRVN SSLALPVDSG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ
AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKEDN NVEGLAHLMM GDQGKEEYIA
TFKGSEYFCY DLSQNPIQSS SDEITLSFKT LQRNGLMLHT GKSADYVNLA LKNGAVSLVI
NLGSGAFEAL VEPVNGKFND NAWHDVKVTR NLRQTSGIGH AMVNKLHCSV TISVDGILTT
TGYTQEDYTM LGSDDFFYVG GSPSTADLPG SPVSNNFMGC LKEVVYKNND VRLELSRLAK
QGDPKMKIHG VVAFKCENVA TLDPITFETP ESFISLPKWN AKKTGSISFD FRTTEPNGLI
LFSHGKPRHQ KDAKHPQMIK VDFFAIEMLD GHLYLLLDMG SGTIKIKALQ KKVNDGEWYH
VDFQRDGRSG TISVNTLRTP YTAPGESQIL DLDDELYLGG LPENKAGLVF PTEVWTALLN
YGYVGCIRDL FIDGQSKDIR QMAEVQSTAG VKPSCSRETA KPCLSNPCKN NGMCRDGWNR
YVCDCSGTGY LGRSCEREAT VLSYDGSMFM KIQLPVVMHT EAEDVSLRFR SQRAYGILMA
TTSRDSADTL RLELDAGRVK LTVNLDCIRI NCNSSKGPET LFAGYNLNDN EWHTVRVVRR
GKSLKLTVDD QQAMTGQMAG DHTRLEFHNI ETGIITERRY LSSVPSNFIG HLQSLTFNGM
AYIDLCKNGD IDYCELNARF GFRNIIADPV TFKTKSSYVA LATLQAYTSM HLFFQFKTTS
LDGLILYNSG DGNDFIVVEL VKGYLHYVFD LGNGANLIKG SSNKPLNDNQ WHNVMISRDT
SNLHTVKIDT KITTQITAGA RNLDLKSDLY IGGVAKETYK SLPKLVHAKE GFQGCLASVD
LNGRLPDLIS DALFCNGQIE RGCEGPSTTC QEDSCSNQGV CLQQWDGISC DCSMTSFSGP
LCNDPGTTYI FSKGGGQITY KWPPNDRPST RADRLAIGFS TVQKEAVLVR VDSSSGLGDY
LELHIHQGKI GVKFNVGTDD IAIEESNAII NDGKYHVVRF TRSGGNATLQ VDSWPVIERY
PAGNNDNERL AIARQRIPYR LGRVVDEWLL DKGRQLTIFN SQATIIIGGK EQGQPFQGQL
SGLYYNGLKV LNMAAENDAN IAIVGNVRLV GEVPSSMTTE STATAMQSEM STSIMETTTT
LATSTARRGK PPTKEPVSQT TDDILVASAE CPSDDEDIDP CEPSSGGLAN PTRAGGREPY
PGSAEVIRES SSTTGMVVGI VAAAALCILI LLYAMYKYRN RDEGSYHVDE SRNYISNSAQ
SNGAVVKEKQ PSSAKSANKN KKNKDKEYYV
//
