LEPR_RAT
ID LEPR_RAT Reviewed; 1162 AA.
AC Q62959; O35772; O35773; O54805; P70493; P70494; P70495; P97589; Q62960;
AC Q63007; Q63385; Q63386; Q9ERI4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=Leptin receptor;
DE Short=LEP-R;
DE AltName: Full=OB receptor;
DE Short=OB-R;
DE AltName: CD_antigen=CD295;
DE Flags: Precursor;
GN Name=Lepr; Synonyms=Fa, Obr;
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 B), AND VARIANT FA PRO-269.
RC STRAIN=Zucker; TISSUE=Hypothalamus;
RX PubMed=8673096; DOI=10.1038/ng0596-18;
RA Phillips M.S., Liu Q., Hammond H.A., Dugan V., Hey P.J., Caskey C.T.,
RA Hess J.F.;
RT "Leptin receptor missense mutation in the fatty Zucker rat.";
RL Nat. Genet. 13:18-19(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT FA PRO-269.
RC STRAIN=Sprague-Dawley, and Zucker fatty; TISSUE=Brain;
RX PubMed=8702432; DOI=10.1006/bbrc.1996.1070;
RA Iida M., Murakami T., Ishida K., Mizuno A., Kuwajima M., Shima K.;
RT "Substitution at codon 269 (glutamine --> proline) of the leptin receptor
RT (OB-R) cDNA is the only mutation found in the Zucker fatty (fa/fa) rat.";
RL Biochem. Biophys. Res. Commun. 224:597-604(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND E), AND VARIANT FA PRO-269.
RC STRAIN=Sprague-Dawley, and Zucker fatty;
RX PubMed=8769097; DOI=10.1006/bbrc.1996.1133;
RA Takaya K., Ogawa Y., Isse N., Okazaki T., Satoh N., Masuzaki H., Mori K.,
RA Tamura N., Hosoda K., Nakao K.;
RT "Molecular cloning of rat leptin receptor isoform complementary DNAs
RT -- identification of a missense mutation in Zucker fatty (fa/fa) rats.";
RL Biochem. Biophys. Res. Commun. 225:75-83(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RA Karlsson C., Lindell K., Robinson I.C.A.F., Carlsson L.M.S., Carlsson B.;
RT "Cloning of the rat leptin receptor.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANT FA PRO-269.
RC STRAIN=Sprague-Dawley, and Zucker fatty;
RX PubMed=8630068; DOI=10.1006/bbrc.1996.0691;
RA Iida M., Murakami T., Ishida K., Mizuno A., Kuwajima M., Shima K.;
RT "Phenotype-linked amino acid alteration in leptin receptor cDNA from Zucker
RT fatty (fa/fa) rat.";
RL Biochem. Biophys. Res. Commun. 222:19-26(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RA Park J.H., Ju S.K., Na S.Y., You K.H., Kim K.L.;
RT "Molecular cloning, sequencing, and recombinant expression of the long form
RT of the rat leptin receptor isolated from whole spleen RNA.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8772180; DOI=10.1016/0014-5793(96)00790-9;
RA Wang M.-Y., Zhou Y.T., Newgard C.B., Unger R.H.;
RT "A novel leptin receptor isoform in rat.";
RL FEBS Lett. 392:87-90(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
RA Morishita T., Hidaka T., Kuzuyama T., Noguchi T.;
RT "Analysis of rat leptin receptor gene.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 557-802 AND 843-892 (ISOFORMS C AND E).
RC STRAIN=Sprague-Dawley;
RX PubMed=9268737; DOI=10.1006/bbrc.1997.7159;
RA Chien E.K., Hara M., Rouard M., Yano H., Phillippe M., Polonsky K.S.,
RA Bell G.I.;
RT "Increase in serum leptin and uterine leptin receptor messenger RNA levels
RT during pregnancy in rats.";
RL Biochem. Biophys. Res. Commun. 237:476-480(1997).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 694-878.
RC STRAIN=Sprague-Dawley; TISSUE=Pancreas;
RA Ma Z.;
RT "Identification of a leptin receptor in islet.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 821-894 (ISOFORM A).
RC STRAIN=Wistar Munich; TISSUE=Kidney;
RA Totsune K., Takahashi K., Mackenzie H.S., Murakami O., Arihara Z., Sone M.,
RA Satoh F., Mouri T., Brenner B.M., Ito S.;
RT "Leptin receptor gene expression in rat kidney.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP FUNCTION (ISOFORM A).
RX PubMed=10698121; DOI=10.1016/s0196-9781(99)00156-4;
RA Kastin A.J., Pan W., Maness L.M., Koletsky R.J., Ernsberger P.;
RT "Decreased transport of leptin across the blood-brain barrier in rats
RT lacking the short form of the leptin receptor.";
RL Peptides 20:1449-1453(1999).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=11861497; DOI=10.1210/endo.143.3.8669;
RA Hileman S.M., Pierroz D.D., Masuzaki H., Bjoerbaek C., El-Haschimi K.,
RA Banks W.A., Flier J.S.;
RT "Characterization of short isoforms of the leptin receptor in rat cerebral
RT microvessels and of brain uptake of leptin in mouse models of obesity.";
RL Endocrinology 143:775-783(2002).
RN [14]
RP REVIEW ON FUNCTION, AND SUBUNIT.
RX PubMed=25232147; DOI=10.1530/joe-14-0404;
RA Allison M.B., Myers M.G. Jr.;
RT "20 years of leptin: connecting leptin signaling to biological function.";
RL J. Endocrinol. 223:T25-T35(2014).
RN [15]
RP VARIANT FA PRO-269.
RX PubMed=8690163; DOI=10.2337/diab.45.8.1141;
RA Chua S.C. Jr., White D.W., Wu-Peng X.S., Liu S.M., Okada N., Kershaw E.E.,
RA Chung W.K., Power-Kehoe L., Chua M., Tartaglia L.A., Leibel R.L.;
RT "Phenotype of fatty due to Gln269Pro mutation in the leptin receptor
RT (Lepr).";
RL Diabetes 45:1141-1143(1996).
CC -!- FUNCTION: Receptor for hormone LEP/leptin (Probable). On ligand
CC binding, mediates LEP central and peripheral effects through the
CC activation of different signaling pathways such as JAK2/STAT3 and MAPK
CC cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating
CC factor that induces a decrease in food intake and an increase in energy
CC consumption by inducing anorexinogenic factors and suppressing
CC orexigenic neuropeptides, also regulates bone mass and secretion of
CC hypothalamo-pituitary-adrenal hormones (PubMed:8690163). In the
CC periphery, increases basal metabolism, influences reproductive
CC function, regulates pancreatic beta-cell function and insulin
CC secretion, is pro-angiogenic and affects innate and adaptive immunity
CC (By similarity). Control of energy homeostasis and melanocortin
CC production (stimulation of POMC and full repression of AgRP
CC transcription) is mediated by STAT3 signaling, whereas distinct signals
CC regulate NPY and the control of fertility, growth and glucose
CC homeostasis. Involved in the regulation of counter-regulatory response
CC to hypoglycemia by inhibiting neurons of the parabrachial nucleus. Has
CC a specific effect on T lymphocyte responses, differentially regulating
CC the proliferation of naive and memory T-cells. Leptin increases Th1 and
CC suppresses Th2 cytokine production (By similarity).
CC {ECO:0000250|UniProtKB:P48356, ECO:0000250|UniProtKB:P48357,
CC ECO:0000269|PubMed:8690163, ECO:0000305|PubMed:25232147}.
CC -!- FUNCTION: [Isoform A]: May transport LEP across the blood-brain
CC barrier. Binds LEP and mediates LEP endocytosis (PubMed:10698121). Does
CC not induce phosphorylation of and activate STAT3 (By similarity).
CC {ECO:0000250|UniProtKB:P48356, ECO:0000269|PubMed:10698121}.
CC -!- FUNCTION: [Isoform E]: Antagonizes Isoform A and isoform B-mediated LEP
CC binding and endocytosis. {ECO:0000250|UniProtKB:P48356}.
CC -!- SUBUNIT: Present as a mixture of monomers and dimers (Probable). The
CC phosphorylated receptor binds a number of SH2 domain-containing
CC proteins such as JAK2, STAT3, PTPN11, and SOCS3 (By similarity).
CC Interaction with SOCS3 inhibits JAK/STAT signaling and MAPK cascade (By
CC similarity). {ECO:0000250|UniProtKB:P48356,
CC ECO:0000250|UniProtKB:P48357, ECO:0000305|PubMed:25232147}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48357};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P48357}.
CC Basolateral cell membrane {ECO:0000250|UniProtKB:P48357}.
CC -!- SUBCELLULAR LOCATION: [Isoform E]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=B;
CC IsoId=Q62959-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q62959-2; Sequence=VSP_001705, VSP_001706;
CC Name=C;
CC IsoId=Q62959-3; Sequence=VSP_001707, VSP_001708;
CC Name=D;
CC IsoId=Q62959-6; Sequence=Not described;
CC Name=E;
CC IsoId=Q62959-4; Sequence=VSP_001709, VSP_001710;
CC Name=F;
CC IsoId=Q62959-5; Sequence=VSP_001711, VSP_001712;
CC -!- TISSUE SPECIFICITY: Isoform B is expressed in kidney, liver, lung,
CC ovary, spleen and uterus. Increased level in uterus during gestation
CC (PubMed:8772180). Isoform A and isoform C are predominantly expressed
CC in cerebral microvessels and choroid plexus, with lower levels in
CC cortex, cerebellum and hypothalamus but also liver and lung
CC (PubMed:11861497). Isoform F is expressed at high levels in brain,
CC liver and spleen and less in stomach, kidney, thymus, heart, lung and
CC hypothalamus (PubMed:11861497, PubMed:8772180).
CC {ECO:0000269|PubMed:11861497, ECO:0000269|PubMed:8772180}.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- PTM: On ligand binding, phosphorylated on two conserved C-terminal
CC tyrosine residues (isoform B only) by JAK2. Tyr-985 is required for
CC complete binding and activation of PTPN11, ERK/FOS activation,for
CC interaction with SOCS3 and SOCS3 mediated inhibition of leptin
CC signaling. Phosphorylation on Tyr-1138 is required for STAT3
CC binding/activation. Phosphorylation of Tyr-1077 has a more accessory
CC role. {ECO:0000250|UniProtKB:P48356}.
CC -!- DISEASE: Note=The fatty (Fa) mutation produces profound obesity of
CC early onset caused by hyperphagia, defective non-shivering
CC thermogenesis, and preferential deposition of energy into adipose
CC tissue.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; U52966; AAC52587.1; -; mRNA.
DR EMBL; D84550; BAA12697.1; -; mRNA.
DR EMBL; D84551; BAA12698.1; -; mRNA.
DR EMBL; D85557; BAA12830.1; -; mRNA.
DR EMBL; D85558; BAA12831.1; -; mRNA.
DR EMBL; D85559; BAA12832.1; -; mRNA.
DR EMBL; U60151; AAB06616.1; -; mRNA.
DR EMBL; D84125; BAA12230.1; -; mRNA.
DR EMBL; D84126; BAA12231.1; -; mRNA.
DR EMBL; AF287268; AAF89300.1; -; mRNA.
DR EMBL; U53144; AAB03088.1; -; mRNA.
DR EMBL; AB011006; BAA24899.1; -; Genomic_DNA.
DR EMBL; AF007818; AAB63201.1; -; mRNA.
DR EMBL; AF007819; AAB63202.1; -; mRNA.
DR EMBL; U67207; AAB40654.1; -; mRNA.
DR EMBL; AF304191; AAG22823.1; -; mRNA.
DR PIR; JC4895; PC4184.
DR PIR; S74225; S74225.
DR RefSeq; NP_036728.1; NM_012596.1. [Q62959-1]
DR AlphaFoldDB; Q62959; -.
DR BioGRID; 246689; 1.
DR STRING; 10116.ENSRNOP00000046647; -.
DR GlyGen; Q62959; 17 sites.
DR iPTMnet; Q62959; -.
DR PhosphoSitePlus; Q62959; -.
DR PaxDb; Q62959; -.
DR GeneID; 24536; -.
DR KEGG; rno:24536; -.
DR CTD; 3953; -.
DR RGD; 3001; Lepr.
DR eggNOG; ENOG502RK5B; Eukaryota.
DR InParanoid; Q62959; -.
DR OrthoDB; 144839at2759; -.
DR PhylomeDB; Q62959; -.
DR PRO; PR:Q62959; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0038021; F:leptin receptor activity; ISS:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
DR GO; GO:0016500; F:protein-hormone receptor activity; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0001525; P:angiogenesis; IMP:RGD.
DR GO; GO:0098868; P:bone growth; ISS:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; IEP:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:RGD.
DR GO; GO:0014009; P:glial cell proliferation; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:RGD.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:1903999; P:negative regulation of eating behavior; IMP:RGD.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:RGD.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; ISO:RGD.
DR GO; GO:1904060; P:negative regulation of locomotor rhythm; IMP:RGD.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IEP:RGD.
DR GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB.
DR GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
DR GO; GO:0051049; P:regulation of transport; ISO:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0044321; P:response to leptin; IEP:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR010457; IgC2-like_lig-bd.
DR InterPro; IPR041182; LEP-R_IGD.
DR InterPro; IPR015752; Lep_receptor.
DR PANTHER; PTHR23036:SF109; PTHR23036:SF109; 1.
DR Pfam; PF06328; Lep_receptor_Ig; 1.
DR Pfam; PF18589; ObR_Ig; 2.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW Glycoprotein; Membrane; Obesity; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1162
FT /note="Leptin receptor"
FT /id="PRO_0000010908"
FT TOPO_DOM 22..839
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 861..1162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 238..331
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 537..632
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 637..729
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 738..831
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 465..482
FT /note="Leptin-binding"
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT REGION 891..896
FT /note="Required for JAK2 activation"
FT /evidence="ECO:0000250|UniProtKB:P48356"
FT REGION 896..904
FT /note="Required for STAT3 phosphorylation"
FT /evidence="ECO:0000250|UniProtKB:P48356"
FT MOTIF 620..624
FT /note="WSXWS motif"
FT MOTIF 869..877
FT /note="Box 1 motif"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT MOD_RES 985
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:P48356"
FT MOD_RES 1077
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P48356"
FT MOD_RES 1138
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:P48356"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..90
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 89..99
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 131..142
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 186..195
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 188..193
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 350..410
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 411..416
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 434..445
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 471..526
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT DISULFID 486..496
FT /evidence="ECO:0000250|UniProtKB:P48357"
FT VAR_SEQ 797..805
FT /note="DNFIPIEKY -> GMCTVLLLN (in isoform E)"
FT /evidence="ECO:0000303|PubMed:8769097,
FT ECO:0000303|PubMed:9268737"
FT /id="VSP_001709"
FT VAR_SEQ 806..1162
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:8769097,
FT ECO:0000303|PubMed:9268737"
FT /id="VSP_001710"
FT VAR_SEQ 890..895
FT /note="PETFEH -> IMPGRN (in isoform F)"
FT /evidence="ECO:0000303|PubMed:8772180"
FT /id="VSP_001711"
FT VAR_SEQ 890..894
FT /note="PETFE -> RADTL (in isoform A)"
FT /evidence="ECO:0000303|PubMed:8630068,
FT ECO:0000303|PubMed:8769097, ECO:0000303|Ref.11"
FT /id="VSP_001705"
FT VAR_SEQ 890..892
FT /note="PET -> VTV (in isoform C)"
FT /evidence="ECO:0000303|PubMed:9268737"
FT /id="VSP_001707"
FT VAR_SEQ 893..1162
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:9268737"
FT /id="VSP_001708"
FT VAR_SEQ 895..1162
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:8630068,
FT ECO:0000303|PubMed:8769097, ECO:0000303|Ref.11"
FT /id="VSP_001706"
FT VAR_SEQ 896..1162
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000303|PubMed:8772180"
FT /id="VSP_001712"
FT VARIANT 269
FT /note="Q -> P (in FA)"
FT /evidence="ECO:0000269|PubMed:8630068,
FT ECO:0000269|PubMed:8673096, ECO:0000269|PubMed:8690163,
FT ECO:0000269|PubMed:8702432, ECO:0000269|PubMed:8769097"
FT CONFLICT 2
FT /note="T -> M (in Ref. 4; AAB06616)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="H -> P (in Ref. 8; BAA24899)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="K -> R (in Ref. 8; BAA24899)"
FT /evidence="ECO:0000305"
FT CONFLICT 415..417
FT /note="ACH -> QCQ (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="E -> D (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="F -> L (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="F -> S (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="R -> Q (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="S -> T (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 703..704
FT /note="WA -> SG (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="A -> D (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 738..739
FT /note="AV -> GW (in Ref. 7; AAB03088)"
FT /evidence="ECO:0000305"
FT CONFLICT 751..752
FT /note="CV -> SL (in Ref. 10; AAB40654)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="L -> S (in Ref. 9; AAB63202)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="R -> K (in Ref. 9; AAB63202)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="Y -> N (in Ref. 9; AAB63202)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="I -> V (in Ref. 9; AAB63201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1162 AA; 130833 MW; BA7AC2CA2D2E62AF CRC64;
MTCQKFYVVL LHWEFLYVIT ALNLAYPTSP WRFKLFCAPP STTDDSFLSP AGVPNNTSSL
KGASEALVEA KFNSTGIYVS ELSKTIFHCC FGNEQGQNCS ALTGNTEGKT LASVVKPLVF
RQLGVNWDIE CWMKGDLTLF ICHMEPLLKN PFKNYDSKVH LLYDLPEVID DLPLPPLKDS
FQTVQCNCSV RECECHVPVP RAKVNYALLM YLEITSAGVS FQSPLMSLQP MLVVKPDPPL
GLRMEVTDDG NLKISWDSQT KAPFPLQYQV KYLENSTIVR EAAEIVSDTS LLVDSVLPGS
SYEVQVRSKR LDGSGVWSDW SLPQLFTTQD VMYFPPKILT SVGSNASFCC IYKNENQTIS
SKQIVWWMNL AEKIPETQYN TVSDHISKVT FSNLKATRPR GKFTYDAVYC CNEQACHHRY
AELYVIDVNI NISCETDGYL TKMTCRWSPS TIQSLVGSTV QLRYHRRSLY CPDNPSIRPT
SELKNCVLQT DGFYECVFQP IFLLSGYTMW IRINHSLGSL DSPPTCVLPD SVVKPLPPSN
VKAEITINTG LLKVSWEKPV FPENNLQFQI RYGLNGKEIQ WKTHEVFDAK SKSASLPVSD
LCAVYVVQVR CRRLDGLGYW SNWSSPAYTL VMDVKVPMRG PEFWRIMDGD ITKKERNVTL
LWKPLMKNDS LCSVRRYVVK HRTAHNGTWS QDVGNQTNLT FLWAESAHTV TVLAINSIGA
SLVNFNLTFS WPMSKVNAVQ SLSAYPLSSS CVILSWTLSP NDYSLLYLVI EWKNLNDDDG
MKWLRIPSNV NKYYIHDNFI PIEKYQFSLY PVFMEGVGKP KIINGFTKDD IAKQQNDAGL
YVIVPIIISS CVLLLGTLLI SHQRMKKLFW DDVPNPKNCS WAQGLNFQKP ETFEHLFTKH
AESVIFGPLL LEPEPVSEEI SVDTAWKNKD EMVPAAMVSL LLTTPDSTRG SICISDQCNS
ANFSGAQSTQ GTCEDECQSQ PSVKYATLVS NVKTVETDEE QGAIHSSVSQ CIARKHSPLR
QSFSSNSWEI EAQAFFLLSD HPPNVISPQL SFSGLDELLE LEGNFPEENH GEKSVYYLGV
SSGNKRENDM LLTDEAGVLC PFPAHCLFSD IRILQESCSH FVENNLNLGT SGKNFVPYMP
QFQSCSTHSH KIIENKMCDL TV
