NRP1_RAT
ID NRP1_RAT Reviewed; 922 AA.
AC Q9QWJ9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Neuropilin-1;
DE AltName: Full=Vascular endothelial cell growth factor 165 receptor;
DE AltName: CD_antigen=CD304;
DE Flags: Precursor;
GN Name=Nrp1;
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 TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=9288754; DOI=10.1016/s0092-8674(00)80535-8;
RA Kolodkin A.L., Levengood D.V., Rowe E.G., Tai Y.-T., Giger R.J.,
RA Ginty D.D.;
RT "Neuropilin is a semaphorin III receptor.";
RL Cell 90:753-762(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION BY INJURY.
RX PubMed=28270793; DOI=10.3389/fneur.2017.00049;
RA Lindholm T., Risling M., Carlstedt T., Hammarberg H., Wallquist W.,
RA Cullheim S., Skoeld M.K.;
RT "Expression of Semaphorins, Neuropilins, VEGF, and Tenascins in Rat and
RT Human Primary Sensory Neurons after a Dorsal Root Injury.";
RL Front. Neurol. 8:49-49(2017).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 273-586 IN COMPLEX WITH VEGF
RP FRAGMENT, HEPARIN-BINDING, AND DISULFIDE BONDS.
RX PubMed=17405859; DOI=10.1073/pnas.0700043104;
RA Vander Kooi C.W., Jusino M.A., Perman B., Neau D.B., Bellamy H.D.,
RA Leahy D.J.;
RT "Structural basis for ligand and heparin binding to neuropilin B domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6152-6157(2007).
CC -!- FUNCTION: Cell-surface receptor involved in the development of the
CC cardiovascular system, in angiogenesis, in the formation of certain
CC neuronal circuits and in organogenesis outside the nervous system.
CC Mediates the chemorepulsant activity of semaphorins. Recognizes a C-end
CC rule (CendR) motif R/KXXR/K on its ligands which causes cellular
CC internalization and vascular leakage. It binds to semaphorin 3A, the
CC PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (By
CC similarity). Coexpression with KDR results in increased VEGF165 binding
CC to KDR as well as increased chemotaxis. Regulates VEGF-induced
CC angiogenesis. Binding to VEGFA initiates a signaling pathway needed for
CC motor neuron axon guidance and cell body migration, including for the
CC caudal migration of facial motor neurons from rhombomere 4 to
CC rhombomere 6 during embryonic development (By similarity). Regulates
CC mitochondrial iron transport via interaction with ABCB8/MITOSUR (By
CC similarity). {ECO:0000250|UniProtKB:O14786,
CC ECO:0000250|UniProtKB:P97333}.
CC -!- SUBUNIT: Homodimer, and heterodimer with NRP2. Binds PLXNB1 (By
CC similarity). Interacts with FER. Interacts with VEGFA (By similarity).
CC Interacts with ABCB8/MITOSUR in mitochondria (By similarity).
CC {ECO:0000250|UniProtKB:O14786, ECO:0000250|UniProtKB:P97333}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:O14786}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O14786}; Single-
CC pass type I membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:O14786}.
CC -!- TISSUE SPECIFICITY: Found in the embryonic nervous system
CC (PubMed:9288754). Expressed in dorsal root ganglia (PubMed:28270793).
CC {ECO:0000269|PubMed:28270793, ECO:0000269|PubMed:9288754}.
CC -!- INDUCTION: Increased in dorsal root ganglia in response to injury
CC caused by dorsal rhizotomy (PubMed:28270793). Increased in dorsal root
CC ganglia in response to both sciatic nerve crush and transection injury
CC (PubMed:28270793). {ECO:0000269|PubMed:28270793}.
CC -!- DOMAIN: The tandem CUB domains mediate binding to semaphorin, while the
CC tandem F5/8 domains are responsible for heparin and VEGF binding. F5/8
CC domains mediate the recognition and binding to R/KXXR/K CendR motifs.
CC {ECO:0000250|UniProtKB:O14786}.
CC -!- SIMILARITY: Belongs to the neuropilin family. {ECO:0000305}.
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DR EMBL; AF016296; AAC53337.1; -; mRNA.
DR EMBL; BC085689; AAH85689.1; -; mRNA.
DR RefSeq; NP_659566.1; NM_145098.2.
DR RefSeq; XP_006255887.1; XM_006255825.3.
DR PDB; 2ORX; X-ray; 2.40 A; A=273-586.
DR PDB; 2ORZ; X-ray; 2.15 A; A=273-586.
DR PDBsum; 2ORX; -.
DR PDBsum; 2ORZ; -.
DR AlphaFoldDB; Q9QWJ9; -.
DR SMR; Q9QWJ9; -.
DR BioGRID; 251596; 4.
DR DIP; DIP-44935N; -.
DR IntAct; Q9QWJ9; 2.
DR STRING; 10116.ENSRNOP00000014492; -.
DR BindingDB; Q9QWJ9; -.
DR ChEMBL; CHEMBL3309098; -.
DR GlyGen; Q9QWJ9; 6 sites.
DR iPTMnet; Q9QWJ9; -.
DR PhosphoSitePlus; Q9QWJ9; -.
DR SwissPalm; Q9QWJ9; -.
DR PaxDb; Q9QWJ9; -.
DR PRIDE; Q9QWJ9; -.
DR Ensembl; ENSRNOT00000014492; ENSRNOP00000014492; ENSRNOG00000010744.
DR GeneID; 246331; -.
DR KEGG; rno:246331; -.
DR UCSC; RGD:621588; rat.
DR CTD; 8829; -.
DR RGD; 621588; Nrp1.
DR eggNOG; ENOG502QUEH; Eukaryota.
DR GeneTree; ENSGT00940000157169; -.
DR HOGENOM; CLU_015228_6_1_1; -.
DR InParanoid; Q9QWJ9; -.
DR OMA; QEDCTKP; -.
DR OrthoDB; 124611at2759; -.
DR PhylomeDB; Q9QWJ9; -.
DR TreeFam; TF316506; -.
DR Reactome; R-RNO-194306; Neurophilin interactions with VEGF and VEGFR.
DR Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-RNO-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-RNO-399956; CRMPs in Sema3A signaling.
DR Reactome; R-RNO-445144; Signal transduction by L1.
DR EvolutionaryTrace; Q9QWJ9; -.
DR PRO; PR:Q9QWJ9; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000010744; Expressed in lung and 19 other tissues.
DR Genevisible; Q9QWJ9; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; NAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005883; C:neurofilament; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0097443; C:sorting endosome; ISO:RGD.
DR GO; GO:0019838; F:growth factor binding; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0017154; F:semaphorin receptor activity; IMP:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:RGD.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; ISO:RGD.
DR GO; GO:0048844; P:artery morphogenesis; ISO:RGD.
DR GO; GO:0048846; P:axon extension involved in axon guidance; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007413; P:axonal fasciculation; ISO:RGD.
DR GO; GO:0060385; P:axonogenesis involved in innervation; ISO:RGD.
DR GO; GO:0150020; P:basal dendrite arborization; ISO:RGD.
DR GO; GO:0150018; P:basal dendrite development; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:RGD.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:RGD.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISO:RGD.
DR GO; GO:0060982; P:coronary artery morphogenesis; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; ISO:RGD.
DR GO; GO:1904835; P:dorsal root ganglion morphogenesis; ISO:RGD.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISO:RGD.
DR GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR GO; GO:0021612; P:facial nerve structural organization; ISO:RGD.
DR GO; GO:1903375; P:facioacoustic ganglion development; ISO:RGD.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0008045; P:motor neuron axon guidance; ISO:RGD.
DR GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; ISO:RGD.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IMP:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0021675; P:nerve development; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; NAS:RGD.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; ISO:RGD.
DR GO; GO:0048666; P:neuron development; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0038189; P:neuropilin signaling pathway; ISO:RGD.
DR GO; GO:1905040; P:otic placode development; ISO:RGD.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISO:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISO:RGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISO:RGD.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:RGD.
DR GO; GO:1902336; P:positive regulation of retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0099173; P:postsynapse organization; ISO:RGD.
DR GO; GO:1902946; P:protein localization to early endosome; ISO:RGD.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; ISO:RGD.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:RGD.
DR GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0061441; P:renal artery morphogenesis; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISO:RGD.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; ISO:RGD.
DR GO; GO:1902285; P:semaphorin-plexin signaling pathway involved in neuron projection guidance; ISO:RGD.
DR GO; GO:0097374; P:sensory neuron axon guidance; ISO:RGD.
DR GO; GO:0002040; P:sprouting angiogenesis; ISO:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISO:RGD.
DR GO; GO:0061549; P:sympathetic ganglion development; ISO:RGD.
DR GO; GO:0048485; P:sympathetic nervous system development; ISO:RGD.
DR GO; GO:0097490; P:sympathetic neuron projection extension; ISO:RGD.
DR GO; GO:0097491; P:sympathetic neuron projection guidance; ISO:RGD.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
DR GO; GO:0061551; P:trigeminal ganglion development; ISO:RGD.
DR GO; GO:0021636; P:trigeminal nerve morphogenesis; ISO:RGD.
DR GO; GO:0021637; P:trigeminal nerve structural organization; ISO:RGD.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; IBA:GO_Central.
DR GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; ISO:RGD.
DR GO; GO:1902378; P:VEGF-activated neuropilin signaling pathway involved in axon guidance; ISO:RGD.
DR GO; GO:0036486; P:ventral trunk neural crest cell migration; ISO:RGD.
DR GO; GO:0021649; P:vestibulocochlear nerve structural organization; ISO:RGD.
DR GO; GO:0046718; P:viral entry into host cell; ISO:RGD.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00057; FA58C; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR014648; Neuropilin.
DR InterPro; IPR022579; Neuropilin_C.
DR InterPro; IPR027146; NRP1.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46806:SF4; PTHR46806:SF4; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF11980; DUF3481; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF00629; MAM; 1.
DR PIRSF; PIRSF036960; Neuropilin; 1.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00231; FA58C; 2.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; Calcium; Cell membrane; Cytoplasm;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Heparan sulfate; Heparin-binding; Membrane; Metal-binding; Mitochondrion;
KW Neurogenesis; Phosphoprotein; Proteoglycan; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..922
FT /note="Neuropilin-1"
FT /id="PRO_0000021861"
FT TOPO_DOM 22..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 881..922
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..141
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 147..265
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 275..424
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 431..583
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 645..811
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97333"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 612
FT /note="O-linked (Xyl...) (heparan sulfate) serine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..54
FT /evidence="ECO:0000305|PubMed:17405859"
FT DISULFID 82..104
FT /evidence="ECO:0000305|PubMed:17405859"
FT DISULFID 147..173
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 206..228
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 275..424
FT /evidence="ECO:0000269|PubMed:17405859"
FT DISULFID 431..583
FT /evidence="ECO:0000269|PubMed:17405859"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2ORZ"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:2ORZ"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2ORZ"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 326..342
FT /evidence="ECO:0007829|PDB:2ORZ"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 352..368
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 391..414
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:2ORZ"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:2ORX"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:2ORZ"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:2ORX"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:2ORZ"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:2ORZ"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 485..501
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 512..525
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 544..547
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 550..570
FT /evidence="ECO:0007829|PDB:2ORZ"
FT STRAND 573..583
FT /evidence="ECO:0007829|PDB:2ORZ"
SQ SEQUENCE 922 AA; 103082 MW; CC6F82AD098B0F2E CRC64;
MERGLPLLCA TLALALALAG AFRSDKCGGT IKIENPGYLT SPGYPHSYHP SEKCEWLIQA
PEPYQRIMIN FNPHFDLEDR DCKYDYVEVI DGENEGGRLW GKFCGKIAPS PVVSSGPFLF
IKFVSDYETH GAGFSIRYEI FKRGPECSQN YTAPTGVIKS PGFPEKYPNS LECTYIIFAP
KMSEIILEFE SFDLEQDSNP PGGVFCRYDR LEIWDGFPEV GPHIGRYCGQ KTPGRIRSSS
GILSMVFYTD SAIAKEGFSA NYSVLQSSIS EDFKCMEALG MESGEIHSDQ ITASSQYGTN
WSVERSRLNY PENGWTPGED SYREWIQVDL GLLRFVTAVG TQGAISKETK KKYYVKTYRV
DISSNGEDWI TLKEGNKAII FQGNTNPTDV VFGVFPKPLI TRFVRIKPAS WETGISMRFE
VYGCKITDYP CSGMLGMVSG LISDSQITAS NQGDRNWMPE NIRLVTSRTG WALPPSPHPY
INEWLQVDLG DEKIVRGVII QGGKHRENKV FMRKFKIAYS NNGSDWKMIM DDSKRKAKSF
EGNNNYDTPE LRAFTPLSTR FIRIYPERAT HSGLGLRMEL LGCEVEVPTA GPTTPNGNPV
DECDDDQANC HSGTGDDFQL TGGTTVLATE KPTIIDSTIQ SEFPTYGFNC EFGWGSHKTF
CHWEHDSHAQ LRWRVLTSKT GPIQDHTGDG NFIYSQADEN QKGKVARLVS PVVYSQSSAH
CMTFWYHMSG SHVGTLRVKL HYQKPEEYDQ LVWMVVGHQG DHWKEGRVLL HKSLKLYQVI
FEGEIGKGNL GGIAVDDISI NNHIPQEDCA KPTDLDKKNT EIKIDETGST PGYEEGKGDK
NISRKPGNVL KTLDPILITI IAMSALGVLL GAVCGVVLYC ACWHNGMSER NLSALENYNF
ELVDGVKLKK DKLNPQSNYS EA
