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NRX1A_BOVIN
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   03-AUG-2022, entry version 170.
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 (By similarity). Both alpha-
CC       type and beta-type isoforms may play a role in the formation or
CC       maintenance of synaptic junctions via their interactions (via the
CC       extracellular domains) with neuroligin family members, CBLN1 or CBLN2.
CC       In vitro, triggers the de novo formation of presynaptic structures. May
CC       be involved in specification of excitatory synapses. Alpha-type
CC       isoforms were first identified as receptors for alpha-latrotoxin from
CC       spider venom. {ECO:0000250}.
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).
CC       Interacts (via cytoplasmic C-terminus) with CASK (via the PDZ, SH3 and
CC       guanylate kinase-like domains) (By similarity). Interacts (via
CC       cytoplasmic C-terminal region) with CASKIN1 and APBA1 (By similarity).
CC       Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6)
CC       with NLGN1, NLGN2, NLGN3 and NLGN4; these interactions are calcium-
CC       dependent. Interacts (via laminin G-like domain 2) with NXPH1 and
CC       NXPH3. Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4 (By
CC       similarity). Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4 (By
CC       similarity). 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). Alpha-type isoforms interact with alpha-
CC       latrotoxin from spider venom. Interacts with SYT13 and SYTL1.
CC       {ECO:0000250, ECO:0000250|UniProtKB:Q63372,
CC       ECO:0000250|UniProtKB:Q9CS84, ECO:0000269|PubMed:1621094,
CC       ECO:0000269|PubMed:18334217, ECO:0000269|PubMed:21552542,
CC       ECO:0000269|PubMed:21620717, ECO:0000269|PubMed:8699246}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Presynaptic cell membrane
CC       {ECO:0000250}.
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: N-glycosylated.
CC   -!- PTM: O-glycosylated.
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.ENSBTAP00000033006; -.
DR   iPTMnet; Q28146; -.
DR   PaxDb; Q28146; -.
DR   PRIDE; Q28146; -.
DR   GeneID; 281950; -.
DR   KEGG; bta:281950; -.
DR   CTD; 9378; -.
DR   eggNOG; KOG3514; Eukaryota.
DR   InParanoid; Q28146; -.
DR   OrthoDB; 35129at2759; -.
DR   EvolutionaryTrace; Q28146; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; 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; cd00110; LamG; 6.
DR   DisProt; DP02503; -.
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   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 6.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00282; LamG; 6.
DR   SUPFAM; SSF49899; SSF49899; 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; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250"
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"
FT   BINDING         1216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1298
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1300
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
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   DISULFID        228..243
FT                   /evidence="ECO:0000250"
FT   DISULFID        245..255
FT                   /evidence="ECO:0000250"
FT   DISULFID        460..496
FT   DISULFID        666..695
FT   DISULFID        703..714
FT   DISULFID        708..723
FT   DISULFID        725..735
FT   DISULFID        906..914
FT   DISULFID        1075..1103
FT   DISULFID        1110..1121
FT   DISULFID        1115..1130
FT   DISULFID        1132..1142
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
 
 
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