NR4A3_RAT
ID NR4A3_RAT Reviewed; 628 AA.
AC P51179; Q2XPY2; Q63516; Q9QWQ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Nuclear receptor subfamily 4 group A member 3;
DE AltName: Full=Neuron-derived orphan receptor 1/2;
DE AltName: Full=Nuclear hormone receptor NOR-1/NOR-2;
GN Name=Nr4a3; Synonyms=Nor1;
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] (ISOFORM 1), AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7811288; DOI=10.1006/bbrc.1994.2900;
RA Ohkura N., Hijikuro M., Yamamoto A., Miki K.;
RT "Molecular cloning of a novel thyroid/steroid receptor superfamily gene
RT from cultured rat neuronal cells.";
RL Biochem. Biophys. Res. Commun. 205:1959-1965(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7556683; DOI=10.1016/0014-5793(95)00998-o;
RA Petropoulos I., Part D., Ochoa A., Zakin M.M., Lamas E.;
RT "NOR-2 (neuron-derived orphan receptor), a brain zinc finger protein, is
RT highly induced during liver regeneration.";
RL FEBS Lett. 372:273-278(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RA Yin W., Huang Y., Su X., Zhao L., Qiu P., Yan G.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-345.
RC TISSUE=Hippocampus;
RX PubMed=7914660; DOI=10.1016/0169-328x(94)90235-6;
RA Pena de Ortiz S., Cannon M.M., Jamieson G.A. Jr.;
RT "Expression of nuclear hormone receptors within the rat hippocampus:
RT identification of novel orphan receptors.";
RL Brain Res. Mol. Brain Res. 23:278-283(1994).
RN [5]
RP FUNCTION, AND HOMODIMERIZATION.
RX PubMed=10523643; DOI=10.1128/mcb.19.11.7549;
RA Maira M., Martens C., Philips A., Drouin J.;
RT "Heterodimerization between members of the Nur subfamily of orphan nuclear
RT receptors as a novel mechanism for gene activation.";
RL Mol. Cell. Biol. 19:7549-7557(1999).
RN [6]
RP INTERACTION WITH NR3C1.
RX PubMed=15591535; DOI=10.1210/me.2004-0333;
RA Martens C., Bilodeau S., Maira M., Gauthier Y., Drouin J.;
RT "Protein-protein interactions and transcriptional antagonism between the
RT subfamily of NGFI-B/Nur77 orphan nuclear receptors and glucocorticoid
RT receptor.";
RL Mol. Endocrinol. 19:885-897(2005).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=16945922; DOI=10.1074/jbc.m603436200;
RA Nomiyama T., Nakamachi T., Gizard F., Heywood E.B., Jones K.L., Ohkura N.,
RA Kawamori R., Conneely O.M., Bruemmer D.;
RT "The NR4A orphan nuclear receptor NOR1 is induced by platelet-derived
RT growth factor and mediates vascular smooth muscle cell proliferation.";
RL J. Biol. Chem. 281:33467-33476(2006).
RN [8]
RP INTERACTION WITH TRIM28.
RX PubMed=19321449; DOI=10.1074/jbc.m809023200;
RA Rambaud J., Desroches J., Balsalobre A., Drouin J.;
RT "TIF1beta/KAP-1 is a coactivator of the orphan nuclear receptor NGFI-
RT B/Nur77.";
RL J. Biol. Chem. 284:14147-14156(2009).
RN [9]
RP FUNCTION.
RX PubMed=24706823; DOI=10.1073/pnas.1320953111;
RA Tessem J.S., Moss L.G., Chao L.C., Arlotto M., Lu D., Jensen M.V.,
RA Stephens S.B., Tontonoz P., Hohmeier H.E., Newgard C.B.;
RT "Nkx6.1 regulates islet beta-cell proliferation via Nr4a1 and Nr4a3 nuclear
RT receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5242-5247(2014).
RN [10]
RP INTERACTION WITH PARP1.
RX PubMed=25625556; DOI=10.1111/bph.13091;
RA Feng X.J., Gao H., Gao S., Li Z., Li H., Lu J., Wang J.J., Huang X.Y.,
RA Liu M., Zou J., Ye J.T., Liu P.Q.;
RT "The orphan receptor NOR1 participates in isoprenaline-induced cardiac
RT hypertrophy by regulating PARP-1.";
RL Br. J. Pharmacol. 172:2852-2863(2015).
CC -!- FUNCTION: Transcriptional activator that binds to regulatory elements
CC in promoter regions in a cell- and response element (target)-specific
CC manner (PubMed:7811288). Induces gene expression by binding as monomers
CC to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site and as
CC homodimers to the Nur response element (NurRE) site in the promoter of
CC their regulated target genes (PubMed:10523643). Plays a role in the
CC regulation of proliferation, survival and differentiation of many
CC different cell types and also in metabolism and inflammation. Mediates
CC proliferation of vascular smooth muscle, myeloid progenitor cell and
CC type B pancreatic cells; promotes mitogen-induced vascular smooth
CC muscle cell proliferation through transactivation of SKP2 promoter by
CC binding a NBRE site (By similarity). Upon PDGF stimulation, stimulates
CC vascular smooth muscle cell proliferation by regulating CCND1 and CCND2
CC expression (PubMed:16945922). In islets, induces type B pancreatic cell
CC proliferation through up-regulation of genes that activate cell cycle,
CC as well as genes that cause degradation of the CDKN1A
CC (PubMed:24706823). Negatively regulates myeloid progenitor cell
CC proliferation by repressing RUNX1 in a NBRE site-independent manner.
CC During inner ear, plays a role as a key mediator of the proliferative
CC growth phase of semicircular canal development (By similarity).
CC Mediates also survival of neuron and smooth muscle cells; mediates
CC CREB-induced neuronal survival, and during hippocampus development,
CC plays a critical role in pyramidal cell survival and axonal guidance.
CC Is required for S phase entry of the cell cycle and survival of smooth
CC muscle cells by inducing CCND1, resulting in RB1 phosphorylation. Binds
CC to NBRE motif in CCND1 promoter, resulting in the activation of the
CC promoter and CCND1 transcription (By similarity). Also plays a role in
CC inflammation; Upon TNF stimulation, mediates monocyte adhesion by
CC inducing the expression of VCAM1 and ICAM1 by binding to the NBRE
CC consensus site (By similarity). In mast cells activated by Fc-epsilon
CC receptor cross-linking, promotes the synthesis and release of cytokines
CC but impairs events leading to degranulation. Also plays a role in
CC metabolism; by modulating feeding behavior; and by playing a role in
CC energy balance by inhibiting the glucocorticoid-induced orexigenic
CC neuropeptides AGRP expression, at least in part by forming a complex
CC with activated NR3C1 on the AGRP-glucocorticoid response element (GRE),
CC and thus weakening the DNA binding activity of NR3C1. Upon
CC catecholamines stimulation, regulates gene expression that controls
CC oxidative metabolism in skeletal muscle (By similarity). Plays a role
CC in glucose transport by regulating translocation of the SLC2A4 glucose
CC transporter to the cell surface (By similarity). Finally, during
CC gastrulation plays a crucial role in the formation of anterior mesoderm
CC by controlling cell migration (By similarity). Also participates in
CC cardiac hypertrophy by activating PARP1 (PubMed:25625556).
CC {ECO:0000250|UniProtKB:Q92570, ECO:0000250|UniProtKB:Q9QZB6,
CC ECO:0000269|PubMed:10523643, ECO:0000269|PubMed:16945922,
CC ECO:0000269|PubMed:24706823, ECO:0000269|PubMed:25625556,
CC ECO:0000269|PubMed:7811288}.
CC -!- SUBUNIT: Interacts with SIX3 (via homeobox); differentially regulates
CC the transcriptional activities of NR4A3. Interacts with NR3C1 (via
CC nuclear receptor DNA-binding domain); the interactions represses
CC transcription activity of NR4A3 on the POMC promoter Nur response
CC element (NurRE) (PubMed:15591535). Interacts with TRIM28; the
CC interactions potentiates NR4A3 activity on NurRE promoter
CC (PubMed:19321449). Binds DNA as a monomer and homodimer
CC (PubMed:10523643). Interacts with PARP1; activates PARP1 by improving
CC acetylation of PARP1 and suppressing the interaction between PARP1 and
CC SIRT1 (PubMed:25625556). Interacts with the constituents of DNA-PK
CC heterotrimer PRKDC, XRCC6 and XRCC5; phosphorylates and prevents NR4A3
CC ubiquitinylation and degradation (By similarity). Interacts with NCOA2;
CC potentiates the activity of the NR4A3. Interacts with NCOA1, NCOA3,
CC MED1 and KAT2B. Interacts with EP300 and NCOA2; mediates the
CC recruitment of MED1 in the coactivator complex (By similarity).
CC {ECO:0000250|UniProtKB:Q92570, ECO:0000250|UniProtKB:Q9QZB6,
CC ECO:0000269|PubMed:10523643, ECO:0000269|PubMed:15591535,
CC ECO:0000269|PubMed:19321449, ECO:0000269|PubMed:25625556}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NOR-1;
CC IsoId=P51179-1; Sequence=Displayed;
CC Name=2; Synonyms=NOR-2;
CC IsoId=P51179-2; Sequence=VSP_010085, VSP_010086;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in cultured apoptotic
CC neuronal cells and fetal brain, and at low level in adult brain.
CC -!- INDUCTION: By PDGF through a CREB-dependent transactivation of the NOR1
CC promoter. {ECO:0000269|PubMed:16945922}.
CC -!- DOMAIN: The AF-1 domain mediates transcription activation. The N-
CC terminal region (1-292) directly interacts with the C-terminal LBD
CC (380-627): the interaction is potentiated by AF-1-mediated recruitment
CC of NCOA2. {ECO:0000250|UniProtKB:Q9QZB6}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000250|UniProtKB:Q92570}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR4
CC subfamily. {ECO:0000305}.
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DR EMBL; D38530; BAA07535.1; -; mRNA.
DR EMBL; X86003; CAA59993.1; -; mRNA.
DR EMBL; DQ268830; ABB72200.1; -; mRNA.
DR EMBL; L19343; AAB46395.1; -; mRNA.
DR PIR; JC2493; JC2493.
DR PIR; S66671; S66671.
DR RefSeq; NP_113816.1; NM_031628.1. [P51179-1]
DR RefSeq; XP_017449093.1; XM_017593604.1. [P51179-1]
DR AlphaFoldDB; P51179; -.
DR SMR; P51179; -.
DR IntAct; P51179; 1.
DR STRING; 10116.ENSRNOP00000008302; -.
DR PhosphoSitePlus; P51179; -.
DR PaxDb; P51179; -.
DR PRIDE; P51179; -.
DR Ensembl; ENSRNOT00000008302; ENSRNOP00000008302; ENSRNOG00000005964. [P51179-1]
DR GeneID; 58853; -.
DR KEGG; rno:58853; -.
DR UCSC; RGD:61882; rat. [P51179-1]
DR CTD; 8013; -.
DR RGD; 61882; Nr4a3.
DR eggNOG; KOG4217; Eukaryota.
DR GeneTree; ENSGT00950000183038; -.
DR HOGENOM; CLU_007368_14_2_1; -.
DR InParanoid; P51179; -.
DR OMA; MEGHSYG; -.
DR OrthoDB; 454476at2759; -.
DR PhylomeDB; P51179; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR PRO; PR:P51179; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000005964; Expressed in Ammon's horn and 13 other tissues.
DR Genevisible; P51179; RN.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0035497; F:cAMP response element binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:UniProtKB.
DR GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
DR GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0007369; P:gastrulation; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:2000253; P:positive regulation of feeding behavior; ISS:UniProtKB.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:2000108; P:positive regulation of leukocyte apoptotic process; ISO:RGD.
DR GO; GO:0038097; P:positive regulation of mast cell activation by Fc-epsilon receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032765; P:positive regulation of mast cell cytokine production; ISS:UniProtKB.
DR GO; GO:1900625; P:positive regulation of monocyte aggregation; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0009444; P:pyruvate oxidation; ISS:UniProtKB.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0048752; P:semicircular canal morphogenesis; ISO:RGD.
DR GO; GO:0060005; P:vestibular reflex; ISO:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR003072; NOR1_rcpt.
DR InterPro; IPR003070; Nuc_orph_rcpt.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01286; NORNUCRECPTR.
DR PRINTS; PR01284; NUCLEARECPTR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..628
FT /note="Nuclear receptor subfamily 4 group A member 3"
FT /id="PRO_0000053724"
FT DOMAIN 396..625
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 291..366
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 294..314
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 330..354
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..293
FT /note="Interaction with NCOA1, NCOA2, NCOA3 and KAT2B"
FT /evidence="ECO:0000250|UniProtKB:Q9QZB6"
FT REGION 1..140
FT /note="Required for DNA-PK heterotrimer"
FT /evidence="ECO:0000250|UniProtKB:Q92570"
FT REGION 1..112
FT /note="Activation function (AF)-1 domain"
FT /evidence="ECO:0000250|UniProtKB:Q9QZB6"
FT REGION 96..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..628
FT /note="Interaction with KAT2B"
FT /evidence="ECO:0000250|UniProtKB:Q9QZB6"
FT COMPBIAS 98..114
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 421..430
FT /note="YCPTDQATAG -> VSSVNRFEWF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7556683"
FT /id="VSP_010085"
FT VAR_SEQ 431..628
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7556683"
FT /id="VSP_010086"
FT CONFLICT 13
FT /note="P -> Q (in Ref. 2; CAA59993)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="A -> P (in Ref. 2; CAA59993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 68564 MW; 9AC285D9A65226D9 CRC64;
MPCVQAQYSP SPPGSTYATQ TYGSEYTTEI MNPDYAKLTM DLGSTGIMAT ATTSLPSFST
FMEGYPSSCE LKPSCLYQMP PSGPRPLIKM EEGREHGYHH HHHHHHHHHH HHQQQQPSIP
PPSGPEDEVL PSTSMYFKQS PPSTPTTPGF PPQAGALWDD ELPSAPGCIA PGPLLDPQMK
AVPPMAAAAR FPIFFKPSPP HPPAPSPAGG HHLGYDPTAA AALSLPLGAA AAAGSQAAAL
EGHPYGLPLA KRTATLTFPP LGLTASPTAS SLLGESPSLP SPPNRSSSSG EGTCAVCGDN
AACQHYGVRT CEGCKGFFKR TVQKNAKYVC LANKNCPVDK RRRNRCQYCR FQKCLSVGMV
KEVVRTDSLK GRRGRLPSKP KSPLQQEPSQ PSPPSPPICM MNALVRALTD ATPRDLDYSR
YCPTDQATAG TDAEHVQQFY NLLTASIDVS RSWAEKIPGF TDLPKEDQTL LIESAFLELF
VLRLSIRSNT AEDKFVFCNG LVLHRLQCLR GFGEWLDSIK DFSLNLQSLN LDIQALACLS
ALSMITERHG LKEPKRVEEL CNKITSSLKD HQRKGQALEP SEPKVLRALV ELRKICTQGL
QRIFYLKLED LVSPPSVIDK LFLDTLPF
