NRX1B_RAT
ID NRX1B_RAT Reviewed; 468 AA.
AC Q63373;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Neurexin-1-beta {ECO:0000305};
DE AltName: Full=Neurexin I-beta;
DE Flags: Precursor;
GN Name=Nrxn1 {ECO:0000312|RGD:628659};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
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 [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND GLYCOSYLATION.
RC TISSUE=Brain;
RX PubMed=8163501; DOI=10.1016/s0021-9258(17)32671-6;
RA Ushkaryov Y.A., Hata Y., Ichtchenko K., Moomaw C., Afendis S.,
RA Slaughter C.A., Suedhof T.C.;
RT "Conserved domain structure of beta-neurexins. Unusual cleaved signal
RT sequences in receptor-like neuronal cell-surface proteins.";
RL J. Biol. Chem. 269:11987-11992(1994).
RN [3]
RP FUNCTION, AND INTERACTION WITH NLGN1.
RX PubMed=9325340; DOI=10.1074/jbc.272.41.26032;
RA Nguyen T., Suedhof T.C.;
RT "Binding properties of neuroligin 1 and neurexin 1beta reveal function as
RT heterophilic cell adhesion molecules.";
RL J. Biol. Chem. 272:26032-26039(1997).
RN [4]
RP INTERACTION WITH NLGN1; NLGN2 AND NLGN3, AND REGION.
RX PubMed=8576240; DOI=10.1074/jbc.271.5.2676;
RA Ichtchenko K., Nguyen T., Suedhof T.C.;
RT "Structures, alternative splicing, and neurexin binding of multiple
RT neuroligins.";
RL J. Biol. Chem. 271:2676-2682(1996).
RN [5]
RP INTERACTION WITH CASK.
RX PubMed=8786425; DOI=10.1523/jneurosci.16-08-02488.1996;
RA Hata Y., Butz S., Suedhof T.C.;
RT "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent
RT protein kinase domain identified by interaction with neurexins.";
RL J. Neurosci. 16:2488-2494(1996).
RN [6]
RP INTERACTION WITH ALPHA-LATROTOXIN, AND REGION.
RX PubMed=10197529; DOI=10.1016/s0896-6273(00)80704-7;
RA Sugita S., Khvochtev M., Suedhof T.C.;
RT "Neurexins are functional alpha-latrotoxin receptors.";
RL Neuron 22:489-496(1999).
RN [7]
RP INTERACTION WITH DAG1 (ALPHA-DYSTROGLYCAN), AND REGION.
RX PubMed=11470830; DOI=10.1083/jcb.200105003;
RA Sugita S., Saito F., Tang J., Satz J., Campbell K., Suedhof T.C.;
RT "A stoichiometric complex of neurexins and dystroglycan in brain.";
RL J. Cell Biol. 154:435-445(2001).
RN [8]
RP SUBUNIT.
RX PubMed=17042500; DOI=10.1021/bi0614131;
RA Comoletti D., Flynn R.E., Boucard A.A., Demeler B., Schirf V., Shi J.,
RA Jennings L.L., Newlin H.R., Sudhof T.C., Taylor P.;
RT "Gene selection, alternative splicing, and post-translational processing
RT regulate neuroligin selectivity for beta-neurexins.";
RL Biochemistry 45:12816-12827(2006).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17868325; DOI=10.1111/j.1471-4159.2007.04918.x;
RA Berninghausen O., Rahman M.A., Silva J.P., Davletov B., Hopkins C.,
RA Ushkaryov Y.A.;
RT "Neurexin Ibeta and neuroligin are localized on opposite membranes in
RT mature central synapses.";
RL J. Neurochem. 103:1855-1863(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 47-302.
RX PubMed=10520997; DOI=10.1016/s0092-8674(00)80065-3;
RA Rudenko G., Nguyen T., Chelliah Y., Suedhof T.C., Deisenhofer J.;
RT "The structure of the ligand-binding domain of neurexin Ibeta: regulation
RT of LNS domain function by alternative splicing.";
RL Cell 99:93-101(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 80-288 IN COMPLEX WITH HUMAN
RP NLGN4X, AND CALCIUM-BINDING SITES.
RX PubMed=18093521; DOI=10.1016/j.neuron.2007.11.013;
RA Fabrichny I.P., Leone P., Sulzenbacher G., Comoletti D., Miller M.T.,
RA Taylor P., Bourne Y., Marchot P.;
RT "Structural analysis of the synaptic protein neuroligin and its beta-
RT neurexin complex: determinants for folding and cell adhesion.";
RL Neuron 56:979-991(2007).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion by forming intracellular junctions
CC through binding to neuroligins. May play a role in formation or
CC maintenance of synaptic junctions. May mediate intracellular signaling.
CC May play a role in angiogenesis (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9325340}.
CC -!- SUBUNIT: The cytoplasmic C-terminal region binds to CASK
CC (PubMed:8786425). Binds NLGN1, NLGN2 and NLGN3, DAG1 (alpha-
CC dystroglycan) and alpha-latrotoxin. Binding to neuroligins is calcium-
CC dependent, and the binding preference ranks as follow: NLGN1 > NLGN4 >>
CC NLGN3 > NLGN2 (PubMed:17042500, PubMed:9325340, PubMed:8576240,
CC PubMed:10197529, PubMed:11470830). Interacts CBLN2 and more weakly with
CC CBLN4 (By similarity). Interacts with CBLN1; interaction is CBLN1
CC hexamer form-dependent; CBLN1-binding is calcium-independent; isoform
CC 1b does not interact with CBLN1 (By similarity).
CC {ECO:0000250|UniProtKB:P0DI97, ECO:0000250|UniProtKB:P58400,
CC ECO:0000269|PubMed:10197529, ECO:0000269|PubMed:11470830,
CC ECO:0000269|PubMed:17042500, ECO:0000269|PubMed:8576240,
CC ECO:0000269|PubMed:8786425, ECO:0000269|PubMed:9325340}.
CC -!- INTERACTION:
CC Q63373; O14936: CASK; Xeno; NbExp=3; IntAct=EBI-1780696, EBI-1215506;
CC Q63373-3; Q62765-2: Nlgn1; NbExp=5; IntAct=EBI-20994045, EBI-20994039;
CC Q63373-3; Q8N0W4: NLGN4X; Xeno; NbExp=5; IntAct=EBI-20994045, EBI-2862707;
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000269|PubMed:17868325}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:17868325}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=17;
CC Comment=Two isoform types, alpha-type and beta-type are produced by
CC alternative promoter usage. 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 five
CC sites may lead to the generation of at least 96 isoforms but for
CC simplicity only individual splice events or observed combinations are
CC explicitly described below. Beta-type isoforms share the possibility
CC of alternative splicing at sites 4 and 5. Experimental confirmation
CC may be lacking for some isoforms.;
CC Name=1b; Synonyms=Beta-4A5A;
CC IsoId=Q63373-1; Sequence=Displayed;
CC Name=2b; Synonyms=Beta-4A5B;
CC IsoId=Q63373-2; Sequence=VSP_003497;
CC Name=3b; Synonyms=Beta-4B5A;
CC IsoId=Q63373-3; Sequence=VSP_003496;
CC Name=4b; Synonyms=Beta-4B5B;
CC IsoId=Q63373-4; Sequence=VSP_003496, VSP_003497;
CC Name=1a; Synonyms=Alpha-1A2A3A4A5A;
CC IsoId=Q63372-2; Sequence=External;
CC Name=2a; Synonyms=Alpha-1B;
CC IsoId=Q63372-1; Sequence=External;
CC Name=3a; Synonyms=Alpha-1C;
CC IsoId=Q63372-3; Sequence=External;
CC Name=4a; Synonyms=Alpha-1D;
CC IsoId=Q63372-4; Sequence=External;
CC Name=5a; Synonyms=Alpha-1E;
CC IsoId=Q63372-5; Sequence=External;
CC Name=6a; Synonyms=Alpha-1F;
CC IsoId=Q63372-6; Sequence=External;
CC Name=7a; Synonyms=Alpha-1G;
CC IsoId=Q63372-7; Sequence=External;
CC Name=8a; Synonyms=Alpha-2B;
CC IsoId=Q63372-8; Sequence=External;
CC Name=9a; Synonyms=Alpha-2C;
CC IsoId=Q63372-9; Sequence=External;
CC Name=10a; Synonyms=Alpha-3B;
CC IsoId=Q63372-10; Sequence=External;
CC Name=11a; Synonyms=Alpha-4B;
CC IsoId=Q63372-11; Sequence=External;
CC Name=12a; Synonyms=Alpha-5B;
CC IsoId=Q63372-12; Sequence=External;
CC Name=13a; Synonyms=Alpha-1B2B;
CC IsoId=Q63372-13; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- PTM: Highly O-glycosylated and minor N-glycosylated.
CC {ECO:0000269|PubMed:8163501}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; M96375; AAA41705.1; -; mRNA.
DR PIR; B40228; B40228.
DR PDB; 1C4R; X-ray; 2.60 A; A/B/C/D/E/F/G/H=81-292.
DR PDB; 2R1B; X-ray; 1.72 A; A/B=77-294.
DR PDB; 2R1D; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/W=48-302.
DR PDB; 2WQZ; X-ray; 3.90 A; C/D=80-288.
DR PDB; 2XB6; X-ray; 2.60 A; C/D=80-288.
DR PDBsum; 1C4R; -.
DR PDBsum; 2R1B; -.
DR PDBsum; 2R1D; -.
DR PDBsum; 2WQZ; -.
DR PDBsum; 2XB6; -.
DR AlphaFoldDB; Q63373; -.
DR SMR; Q63373; -.
DR ComplexPortal; CPX-4061; NLGN1(-SSA-SSB) - NRXN1-beta(-SS4) complex. [Q63373-3]
DR ComplexPortal; CPX-4123; NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex. [Q63373-3]
DR DIP; DIP-40508N; -.
DR IntAct; Q63373; 5.
DR MINT; Q63373; -.
DR PaxDb; Q63373; -.
DR PRIDE; Q63373; -.
DR ABCD; Q63373; 2 sequenced antibodies.
DR UCSC; RGD:628659; rat. [Q63373-1]
DR RGD; 628659; Nrxn1.
DR eggNOG; KOG3514; Eukaryota.
DR PhylomeDB; Q63373; -.
DR EvolutionaryTrace; Q63373; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044295; C:axonal growth cone; ISS:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; IC:ComplexPortal.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0060077; C:inhibitory synapse; IC:ComplexPortal.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IC:ComplexPortal.
DR GO; GO:0098984; C:neuron to neuron synapse; IC:ComplexPortal.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0098635; C:protein complex involved in cell-cell adhesion; IPI:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0033130; F:acetylcholine receptor binding; ISO:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0097109; F:neuroligin family protein binding; IPI:ARUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISO:RGD.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR GO; GO:0090125; P:cell-cell adhesion involved in synapse maturation; IC:ComplexPortal.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:ARUK-UCL.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; ISS:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0045184; P:establishment of protein localization; ISS:BHF-UCL.
DR GO; GO:0046847; P:filopodium assembly; ISO:RGD.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISS:BHF-UCL.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
DR GO; GO:0097117; P:guanylate kinase-associated protein clustering; ISS:BHF-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0099558; P:maintenance of synapse structure; IC:ComplexPortal.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; ISS:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0007158; P:neuron cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0042551; P:neuron maturation; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IC:ComplexPortal.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; ISS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IC:ComplexPortal.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IC:ComplexPortal.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:1905520; P:positive regulation of presynaptic active zone assembly; TAS:BHF-UCL.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISO:RGD.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IC:ComplexPortal.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISS:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0060134; P:prepulse inhibition; ISO:RGD.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0035418; P:protein localization to synapse; ISS:BHF-UCL.
DR GO; GO:0090126; P:protein-containing complex assembly involved in synapse maturation; ISS:BHF-UCL.
DR GO; GO:0097120; P:receptor localization to synapse; ISS:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR GO; GO:2000821; P:regulation of grooming behavior; ISO:RGD.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:BHF-UCL.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:RGD.
DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; ISO:RGD.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR GO; GO:0060074; P:synapse maturation; IC:ComplexPortal.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
DR GO; GO:0097091; P:synaptic vesicle clustering; ISS:BHF-UCL.
DR GO; GO:0099542; P:trans-synaptic signaling by endocannabinoid; ISO:RGD.
DR GO; GO:0042297; P:vocal learning; ISO:RGD.
DR GO; GO:0071625; P:vocalization behavior; ISO:RGD.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Angiogenesis; Calcium; Cell adhesion; Cell membrane; Cell projection;
KW Direct protein sequencing; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..46
FT /evidence="ECO:0000269|PubMed:8163501"
FT CHAIN 47..468
FT /note="Neurexin-1-beta"
FT /id="PRO_0000019494"
FT TOPO_DOM 47..391
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 87..285
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 201..230
FT /note="Essential for interaction with CBLN1; modulates
FT interaction affinity with NLGN1, NLGN2 and NLGN3; prevents
FT interaction with DAG1/alpha-dystroglycan; modulates
FT interaction with alpha-latrotoxin"
FT /evidence="ECO:0000250|UniProtKB:P58400,
FT ECO:0000269|PubMed:10197529, ECO:0000269|PubMed:11470830,
FT ECO:0000269|PubMed:8576240"
FT REGION 350..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 201..230
FT /note="Missing (in isoform 3b and isoform 4b)"
FT /evidence="ECO:0000305"
FT /id="VSP_003496"
FT VAR_SEQ 363..468
FT /note="Missing (in isoform 2b and isoform 4b)"
FT /evidence="ECO:0000305"
FT /id="VSP_003497"
FT STRAND 84..99
FT /evidence="ECO:0007829|PDB:2R1B"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 108..118
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2R1B"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:2R1B"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:2R1B"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:2R1B"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:2R1B"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:2R1B"
SQ SEQUENCE 468 AA; 50268 MW; B24A3CEFF5A2394E CRC64;
MYQRMLRCGA ELGSPGGGSS GGAGGRLALL WIVPLTLSGL LGVAWGASSL GAHHIHHFHG
SSKHHSVPIA IYRSPASLRG GHAGTTYIFS KGGGQITYKW PPNDRPSTRA DRLAIGFSTV
QKEAVLVRVD SSSGLGDYLE LHIHQGKIGV KFNVGTDDIA IEESNAIIND GKYHVVRFTR
SGGNATLQVD SWPVIERYPA GNNDNERLAI ARQRIPYRLG RVVDEWLLDK GRQLTIFNSQ
ATIIIGGKEQ GQPFQGQLSG LYYNGLKVLN MAAENDANIA IVGNVRLVGE VPSSMTTEST
ATAMQSEMST SIMETTTTLA TSTARRGKPP TKEPISQTTD DILVASAECP SDDEDIDPCE
PSSGGLANPT RVGGREPYPG SAEVIRESSS TTGMVVGIVA AAALCILILL YAMYKYRNRD
EGSYHVDESR NYISNSAQSN GAVVKEKQPS SAKSANKNKK NKDKEYYV
