ID   OPRX_MOUSE              Reviewed;         367 AA.
AC   P35377; Q60645; Q8VI74; Q9QUT5; Q9Z2M8; Q9Z2M9; Q9Z2N0;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   04-NOV-2026, entry version 203.
DE   RecName: Full=Nociceptin receptor;
DE   AltName: Full=K3 opiate receptor;
DE   AltName: Full=Kappa-type 3 opioid receptor;
DE            Short=KOR-3;
DE   AltName: Full=ORGC;
DE   AltName: Full=Orphanin FQ receptor;
GN   Name=Oprl1; Synonyms=Oor, Oprl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM KOR3).
RC   STRAIN=C57BL/6N; TISSUE=Brain;
RA   Yasuda K., Jones E., Reisine T., Bell G.I.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM KOR3).
RX   PubMed=7802669; DOI=10.1006/bbrc.1994.2814;
RA   Nishi M., Takeshima H., Mori M., Nakagawara K., Takeuchi T.;
RT   "Structure and chromosomal mapping of genes for the mouse kappa-opioid
RT   receptor and an opioid receptor homologue (MOR-C).";
RL   Biochem. Biophys. Res. Commun. 205:1353-1357(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KOR3), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Brain;
RX   PubMed=8794880; DOI=10.1016/s0026-895x(25)09290-9;
RA   Matthes H.W.D., Seward E.P., Kieffer B., North R.A.;
RT   "Functional selectivity of orphanin FQ for its receptor coexpressed with
RT   potassium channel subunits in Xenopus laevis oocytes.";
RL   Mol. Pharmacol. 50:447-450(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM KOR3).
RA   Pan Y.-X., Xu J., Pasternak G.W.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KOR3), FUNCTION, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=7603458; DOI=10.1016/s0026-895x(25)08759-0;
RA   Pan Y.-X., Cheng J., Xu J., Rossi G., Jacobson E., Ryan-Moro J.,
RA   Brooks A.I., Dean G.E., Standifer K.M., Pasternak G.W.;
RT   "Cloning and functional characterization through antisense mapping of a
RT   kappa 3-related opioid receptor.";
RL   Mol. Pharmacol. 47:1180-1188(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS KOR3A; KOR3B; KOR3C; KOR3D AND KOR3E),
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=9755860; DOI=10.1016/s0014-5793(98)01039-4;
RA   Pan Y.-X., Xu J., Wan B.-L., Zuckerman A., Pasternak G.W.;
RT   "Identification and differential regional expression of KOR-3/ORL-1 gene
RT   splice variants in mouse brain.";
RL   FEBS Lett. 435:65-68(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM KOR3).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-357 (ISOFORM KOR3), AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Spleen;
RX   PubMed=7797625; DOI=10.1016/0165-5728(95)00030-6;
RA   Halford W.P., Gebhardt B.M., Carr D.J.J.;
RT   "Functional role and sequence analysis of a lymphocyte orphan opioid
RT   receptor.";
RL   J. Neuroimmunol. 59:91-101(1995).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9155012; DOI=10.1093/emboj/16.8.1858;
RA   Nishi M., Houtani T., Noda Y., Mamiya T., Sato K., Doi T., Kuno J.,
RA   Takeshima H., Nukada T., Nabeshima T., Yamashita T., Noda T., Sugimoto T.;
RT   "Unrestrained nociceptive response and disregulation of hearing ability in
RT   mice lacking the nociceptin/orphaninFQ receptor.";
RL   EMBO J. 16:1858-1864(1997).
RN   [10]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=12217419; DOI=10.1016/s0196-9781(02)00102-x;
RA   Bertorelli R., Bastia E., Citterio F., Corradini L., Forlani A., Ongini E.;
RT   "Lack of the nociceptin receptor does not affect acute or chronic
RT   nociception in mice.";
RL   Peptides 23:1589-1596(2002).
RN   [11]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=12814369; DOI=10.1046/j.1460-9568.2003.02676.x;
RA   Depner U.B., Reinscheid R.K., Takeshima H., Brune K., Zeilhofer H.U.;
RT   "Normal sensitivity to acute pain, but increased inflammatory hyperalgesia
RT   in mice lacking the nociceptin precursor polypeptide or the nociceptin
RT   receptor.";
RL   Eur. J. Neurosci. 17:2381-2387(2003).
RN   [12]
RP   FUNCTION.
RX   PubMed=23652222; DOI=10.1124/jpet.113.203984;
RA   Sukhtankar D.D., Zaveri N.T., Husbands S.M., Ko M.C.;
RT   "Effects of spinally administered bifunctional nociceptin/orphanin FQ
RT   peptide receptor/mu-opioid receptor ligands in mouse models of neuropathic
RT   and inflammatory pain.";
RL   J. Pharmacol. Exp. Ther. 346:11-22(2013).
CC   -!- FUNCTION: G protein-coupled opioid receptor that functions as a
CC       receptor for the endogenous neuropeptide nociceptin. Ligand binding
CC       causes a conformation change that triggers signaling via guanine
CC       nucleotide-binding proteins (G proteins) and modulates the activity of
CC       down-stream effectors. Signaling via G proteins mediates inhibition of
CC       adenylate cyclase activity and calcium channel activity. Arrestins
CC       modulate signaling via G proteins and mediate the activation of
CC       alternative signaling pathways that lead to the activation of MAP
CC       kinases. Plays a role in modulating nociception and the perception of
CC       pain. Plays a role in the regulation of locomotor activity by the
CC       neuropeptide nociceptin. {ECO:0000269|PubMed:12217419,
CC       ECO:0000269|PubMed:12814369, ECO:0000269|PubMed:23652222,
CC       ECO:0000269|PubMed:7603458, ECO:0000269|PubMed:8794880}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cytoplasmic vesicle {ECO:0000250}. Note=Ligand binding leads to
CC       receptor internalization into cytoplasmic vesicles, decreasing the
CC       amount of available receptor at the cell surface. Internalization
CC       requires phosphorylation at Ser-360. Can recycle to the cell membrane
CC       (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=KOR3;
CC         IsoId=P35377-1; Sequence=Displayed;
CC       Name=KOR3A;
CC         IsoId=P35377-2; Sequence=VSP_001899, VSP_001900;
CC       Name=KOR3B;
CC         IsoId=P35377-3; Sequence=VSP_001903, VSP_001904;
CC       Name=KOR3C;
CC         IsoId=P35377-4; Sequence=VSP_001901, VSP_001902;
CC       Name=KOR3D;
CC         IsoId=P35377-5; Sequence=VSP_001898;
CC       Name=KOR3E;
CC         IsoId=P35377-6; Sequence=VSP_001905, VSP_001906;
CC   -!- TISSUE SPECIFICITY: In the brain, isoform KOR3 and isoform KOR3C are
CC       most abundant in hypothalamus and periaqueductal gray. Isoform KOR3A is
CC       highly expressed in cortex, striatum and brainstem. Isoform KOR3D is
CC       highly expressed in cerebellum, hypothalamus and brainstem. Detected in
CC       spleen lymphocytes. {ECO:0000269|PubMed:7603458,
CC       ECO:0000269|PubMed:7797625, ECO:0000269|PubMed:9755860}.
CC   -!- PTM: Phosphorylation at Ser-360 requires GRK3. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice do not show altered basal
CC       nociception, but are no longer susceptible to modulation of nociception
CC       by the neuropeptide nociceptin. Contrary to wild-type, they do not show
CC       reduced locomotion in response to the neuropeptide nociceptin. In
CC       addition, mutant mice show subtle hearing defects.
CC       {ECO:0000269|PubMed:12217419, ECO:0000269|PubMed:12814369,
CC       ECO:0000269|PubMed:9155012}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U04952; AAA03730.1; -; mRNA.
DR   EMBL; D31667; BAA06509.1; -; Genomic_DNA.
DR   EMBL; X91813; CAA62922.1; -; mRNA.
DR   EMBL; U32932; AAC52669.1; -; Genomic_DNA.
DR   EMBL; U32928; AAC52669.1; JOINED; Genomic_DNA.
DR   EMBL; U32930; AAC52669.1; JOINED; Genomic_DNA.
DR   EMBL; U09421; AAA81333.1; -; mRNA.
DR   EMBL; AF043276; AAC64507.1; -; mRNA.
DR   EMBL; AF043277; AAC64508.1; -; mRNA.
DR   EMBL; AF043278; AAC64509.1; -; mRNA.
DR   EMBL; AF062381; AAF21258.1; -; mRNA.
DR   EMBL; AF075605; AAF21781.1; -; mRNA.
DR   EMBL; AF126469; AAL54889.1; -; mRNA.
DR   EMBL; BC050885; AAH50885.1; -; mRNA.
DR   EMBL; U14165; AAA87899.1; -; mRNA.
DR   CCDS; CCDS17222.1; -. [P35377-1]
DR   PIR; I49022; I49022.
DR   PIR; JC2421; JC2421.
DR   RefSeq; NP_001239494.1; NM_001252565.2. [P35377-1]
DR   RefSeq; NP_001305848.1; NM_001318919.2.
DR   RefSeq; NP_001305849.1; NM_001318920.2. [P35377-5]
DR   RefSeq; NP_001407426.1; NM_001420497.1. [P35377-5]
DR   RefSeq; NP_035142.1; NM_011012.6. [P35377-1]
DR   RefSeq; XP_017171814.1; XM_017316325.2. [P35377-1]
DR   RefSeq; XP_036015363.1; XM_036159470.1. [P35377-5]
DR   AlphaFoldDB; P35377; -.
DR   SMR; P35377; -.
DR   CORUM; P35377; -.
DR   FunCoup; P35377; 973.
DR   STRING; 10090.ENSMUSP00000071513; -.
DR   BindingDB; P35377; -.
DR   ChEMBL; CHEMBL3621; -.
DR   GuidetoPHARMACOLOGY; 320; -.
DR   GlyCosmos; P35377; 3 sites, No reported glycans.
DR   GlyGen; P35377; 3 sites.
DR   PhosphoSitePlus; P35377; -.
DR   SwissPalm; P35377; -.
DR   PaxDb; 10090-ENSMUSP00000071513; -.
DR   Antibodypedia; 29994; 242 antibodies from 30 providers.
DR   DNASU; 18389; -.
DR   Ensembl; ENSMUST00000071585.10; ENSMUSP00000071513.4; ENSMUSG00000027584.18. [P35377-1]
DR   Ensembl; ENSMUST00000108766.2; ENSMUSP00000104397.2; ENSMUSG00000027584.18. [P35377-6]
DR   Ensembl; ENSMUST00000108767.2; ENSMUSP00000104398.2; ENSMUSG00000027584.18. [P35377-1]
DR   Ensembl; ENSMUST00000108768.8; ENSMUSP00000104399.2; ENSMUSG00000027584.18. [P35377-1]
DR   Ensembl; ENSMUST00000183693.8; ENSMUSP00000138810.2; ENSMUSG00000027584.18. [P35377-4]
DR   Ensembl; ENSMUST00000184127.2; ENSMUSP00000139119.2; ENSMUSG00000027584.18. [P35377-3]
DR   GeneID; 18389; -.
DR   KEGG; mmu:18389; -.
DR   UCSC; uc008onj.2; mouse. [P35377-1]
DR   UCSC; uc008ono.1; mouse. [P35377-5]
DR   UCSC; uc008onq.1; mouse. [P35377-6]
DR   AGR; MGI:97440; -.
DR   CTD; 4987; -.
DR   MGI; MGI:97440; Oprl1.
DR   VEuPathDB; HostDB:ENSMUSG00000027584; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000160661; -.
DR   HOGENOM; CLU_009579_8_1_1; -.
DR   InParanoid; P35377; -.
DR   OMA; ACFRNFC; -.
DR   OrthoDB; 6076970at2759; -.
DR   PhylomeDB; P35377; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 18389; 2 hits in 77 CRISPR screens.
DR   PRO; PR:P35377; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P35377; protein.
DR   Bgee; ENSMUSG00000027584; Expressed in neural tube lateral wall and 128 other cell types or tissues.
DR   ExpressionAtlas; P35377; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0097060; C:synaptic membrane; IGI:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR   GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR   GO; GO:0001626; F:nociceptin receptor activity; IMP:UniProtKB.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048148; P:behavioral response to cocaine; ISO:GO_Central.
DR   GO; GO:0048149; P:behavioral response to ethanol; ISO:GO_Central.
DR   GO; GO:0035095; P:behavioral response to nicotine; ISO:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISO:GO_Central.
DR   GO; GO:0071361; P:cellular response to ethanol; ISO:GO_Central.
DR   GO; GO:1990708; P:conditioned place preference; ISO:GO_Central.
DR   GO; GO:0042755; P:eating behavior; ISO:GO_Central.
DR   GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0045776; P:negative regulation of blood pressure; ISO:GO_Central.
DR   GO; GO:0141162; P:negative regulation of cAMP/PKA signal transduction; ISO:GO_Central.
DR   GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISO:GO_Central.
DR   GO; GO:0007270; P:neuron-neuron synaptic transmission; IGI:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0035810; P:positive regulation of urine volume; ISO:GO_Central.
DR   GO; GO:0014059; P:regulation of dopamine secretion; ISO:GO_Central.
DR   GO; GO:1904059; P:regulation of locomotor rhythm; ISO:GO_Central.
DR   GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISO:GO_Central.
DR   GO; GO:0042220; P:response to cocaine; ISO:GO_Central.
DR   GO; GO:0045471; P:response to ethanol; ISO:GO_Central.
DR   GO; GO:0035902; P:response to immobilization stress; ISO:GO_Central.
DR   GO; GO:1901652; P:response to peptide; ISO:GO_Central.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR   CDD; cd15092; 7tmA_NOFQ_opioid_R; 1.
DR   FunFam; 1.20.1070.10:FF:000014; Kappa-type opioid receptor 1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001418; Opioid_rcpt.
DR   InterPro; IPR001420; X_opioid_rcpt.
DR   PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1.
DR   PANTHER; PTHR24229:SF11; NOCICEPTIN RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00384; OPIOIDR.
DR   PRINTS; PR00547; XOPIOIDR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Behavior; Cell membrane; Cytoplasmic vesicle;
KW   Disulfide bond; G protein-coupled receptor; Glycoprotein; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="Nociceptin receptor"
FT                   /id="PRO_0000069981"
FT   TOPO_DOM        1..45
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        46..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        72..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        85..106
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        107..121
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        122..143
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        144..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        163..185
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        186..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        209..233
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        234..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        262..282
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        283..297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        298..319
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        320..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   SITE            107
FT                   /note="Important for G protein-mediated signaling"
FT                   /evidence="ECO:0000250"
FT   SITE            127
FT                   /note="Important for G protein-mediated signaling"
FT                   /evidence="ECO:0000250"
FT   LIPID           331
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         71..75
FT                   /note="Missing (in isoform KOR3D)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001898"
FT   VAR_SEQ         75..99
FT                   /note="RHTKMKTATNIYIFNLALADTLVLL -> SWEGIEGNWRQQAHQDEDCYQHL
FT                   HI (in isoform KOR3A)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001899"
FT   VAR_SEQ         76..111
FT                   /note="HTKMKTATNIYIFNLALADTLVLLTLPFQGTDILLG -> QCPENPLRGVLR
FT                   ETEERRQHLSLLIPSTNSHSGTPR (in isoform KOR3B)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001903"
FT   VAR_SEQ         76..95
FT                   /note="HTKMKTATNIYIFNLALADT -> QHCALGRSLMNFTGSALKTL (in
FT                   isoform KOR3C)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001901"
FT   VAR_SEQ         96..367
FT                   /note="Missing (in isoform KOR3C)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001902"
FT   VAR_SEQ         100..367
FT                   /note="Missing (in isoform KOR3A)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001900"
FT   VAR_SEQ         112..367
FT                   /note="Missing (in isoform KOR3B)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001904"
FT   VAR_SEQ         194..213
FT                   /note="EIECLVEIPAPQDYWGPVFA -> GQWAVLLPDQSVPHGSCRPL (in
FT                   isoform KOR3E)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001905"
FT   VAR_SEQ         214..367
FT                   /note="Missing (in isoform KOR3E)"
FT                   /evidence="ECO:0000303|PubMed:9755860"
FT                   /id="VSP_001906"
FT   CONFLICT        348..349
FT                   /note="SI -> TV (in Ref. 2; AAA81333)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  40491 MW;  E498CA9FE5276026 CRC64;
     MESLFPAPFW EVLYGSHFQG NLSLLNETVP HHLLLNASHS AFLPLGLKVT IVGLYLAVCI
     GGLLGNCLVM YVILRHTKMK TATNIYIFNL ALADTLVLLT LPFQGTDILL GFWPFGNALC
     KTVIAIDYYN MFTSTFTLTA MSVDRYVAIC HPIRALDVRT SSKAQAVNVA IWALASVVGV
     PVAIMGSAQV EDEEIECLVE IPAPQDYWGP VFAICIFLFS FIIPVLIISV CYSLMIRRLR
     GVRLLSGSRE KDRNLRRITR LVLVVVAVFV GCWTPVQVFV LVQGLGVQPG SETAVAILRF
     CTALGYVNSC LNPILYAFLD ENFKACFRKF CCASALHREM QVSDRVRSIA KDVGLGCKTS
     ETVPRPA
//