P2RX2_MOUSE
ID P2RX2_MOUSE Reviewed; 485 AA.
AC Q8K3P1; Q3KP15; Q3TYV0; Q812E6; Q812E7;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=P2X purinoceptor 2;
DE Short=P2X2;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2rx2; Synonyms=P2x2;
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 [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Pituitary;
RX PubMed=16467187; DOI=10.1124/mol.105.019802;
RA Koshimizu T.A., Kretschmannova K., He M.L., Ueno S., Tanoue A.,
RA Yanagihara N., Stojilkovic S.S., Tsujimoto G.;
RT "Carboxyl-terminal splicing enhances physical interactions between the
RT cytoplasmic tails of purinergic P2X receptors.";
RL Mol. Pharmacol. 69:1588-1598(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 [6]
RP FUNCTION.
RX PubMed=12917379; DOI=10.1523/jneurosci.23-19-07426.2003;
RA Khakh B.S., Gittermann D., Cockayne D.A., Jones A.;
RT "ATP modulation of excitatory synapses onto interneurons.";
RL J. Neurosci. 23:7426-7437(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12937291; DOI=10.1113/jphysiol.2003.047944;
RA Ren J., Bian X., DeVries M., Schnegelsberg B., Cockayne D.A., Ford A.P.,
RA Galligan J.J.;
RT "P2X2 subunits contribute to fast synaptic excitation in myenteric neurons
RT of the mouse small intestine.";
RL J. Physiol. (Lond.) 552:809-821(2003).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=14672995; DOI=10.1523/jneurosci.23-36-11315.2003;
RA Rong W., Gourine A.V., Cockayne D.A., Xiang Z., Ford A.P., Spyer K.M.,
RA Burnstock G.;
RT "Pivotal role of nucleotide P2X2 receptor subunit of the ATP-gated ion
RT channel mediating ventilatory responses to hypoxia.";
RL J. Neurosci. 23:11315-11321(2003).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15961431; DOI=10.1113/jphysiol.2005.088435;
RA Cockayne D.A., Dunn P.M., Zhong Y., Rong W., Hamilton S.G., Knight G.E.,
RA Ruan H.Z., Ma B., Yip P., Nunn P., McMahon S.B., Burnstock G., Ford A.P.;
RT "P2X2 knockout mice and P2X2/P2X3 double knockout mice reveal a role for
RT the P2X2 receptor subunit in mediating multiple sensory effects of ATP.";
RL J. Physiol. (Lond.) 567:621-639(2005).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16322458; DOI=10.1126/science.1118435;
RA Finger T.E., Danilova V., Barrows J., Bartel D.L., Vigers A.J., Stone L.,
RA Hellekant G., Kinnamon S.C.;
RT "ATP signaling is crucial for communication from taste buds to gustatory
RT nerves.";
RL Science 310:1495-1499(2005).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17706883; DOI=10.1016/j.neuroscience.2007.06.050;
RA Ryten M., Koshi R., Knight G.E., Turmaine M., Dunn P., Cockayne D.A.,
RA Ford A.P., Burnstock G.;
RT "Abnormalities in neuromuscular junction structure and skeletal muscle
RT function in mice lacking the P2X2 nucleotide receptor.";
RL Neuroscience 148:700-711(2007).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23345450; DOI=10.1073/pnas.1222285110;
RA Yan D., Zhu Y., Walsh T., Xie D., Yuan H., Sirmaci A., Fujikawa T.,
RA Wong A.C., Loh T.L., Du L., Grati M., Vlajkovic S.M., Blanton S.,
RA Ryan A.F., Chen Z.Y., Thorne P.R., Kachar B., Tekin M., Zhao H.B.,
RA Housley G.D., King M.C., Liu X.Z.;
RT "Mutation of the ATP-gated P2X(2) receptor leads to progressive hearing
RT loss and increased susceptibility to noise.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2228-2233(2013).
CC -!- FUNCTION: Ion channel gated by extracellular ATP involved in a variety
CC of cellular responses, such as excitatory postsynaptic responses in
CC sensory neurons, neuromuscular junctions (NMJ) formation, hearing,
CC perception of taste and peristalsis. In the inner ear, regulates sound
CC transduction and auditory neurotransmission, outer hair cell
CC electromotility, inner ear gap junctions, and K(+) recycling. Mediates
CC synaptic transmission between neurons and from neurons to smooth
CC muscle. {ECO:0000269|PubMed:12917379, ECO:0000269|PubMed:12937291,
CC ECO:0000269|PubMed:15961431, ECO:0000269|PubMed:16322458,
CC ECO:0000269|PubMed:17706883, ECO:0000269|PubMed:23345450}.
CC -!- SUBUNIT: Homotrimer and heterotrimer; functional P2XRs are organized as
CC homomeric and heteromeric trimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17706883};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17706883}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8K3P1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K3P1-2; Sequence=VSP_053890;
CC Name=3;
CC IsoId=Q8K3P1-3; Sequence=VSP_053889;
CC Name=4;
CC IsoId=Q8K3P1-4; Sequence=VSP_053887;
CC Name=5;
CC IsoId=Q8K3P1-5; Sequence=VSP_053888;
CC -!- DEVELOPMENTAL STAGE: In skeletal muscle, strongly expressed in
CC postnatal day 3 (P3), P7 and P15 muscles. Expression is not maintained
CC in P21 in adult skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:17706883}.
CC -!- DISRUPTION PHENOTYPE: Mice show small differences in body weight, but
CC are visibly and histopathologically normal for up to 1 year of age.
CC Simultaneous knockout of P2rx2 and P2rx3 results in reduced pain-
CC related behaviors in response to intraplantar injection of formalin and
CC reduced urinary bladder reflexes and decreased pelvic afferent nerve
CC activity in response to bladder distension. Neurons have minimal to no
CC response to ATP (PubMed:15961431). P2rx2 null mice show impaired
CC peristalsis in ileal segments of small intestine (PubMed:12937291).
CC P2rx2 null mice show disorganized neuromuscular junctions (NMJ) with
CC misapposition of nerve terminals and post-synaptic AChR expression
CC localization, reduction of the density of post-synaptic and increased
CC end-plate fragmentation. These changes in NMJ structure are associated
CC with muscle fiber atrophy and an increase in the proportion of fast
CC type muscle fibers (PubMed:17706883). P2rx2 null mice display age-
CC related hearing loss: in the absence of exposure to noise, auditory
CC thresholds are normal until at least age 19-23 week. Then, mice develop
CC severe progressive hearing loss, and their early exposure to continuous
CC moderate noise leads to high-frequency hearing loss as young adults
CC (PubMed:23345450). Simultaneous knockout of P2rx2 and P2rx3 results in
CC defects in taste responses in the taste nerves and reduced behavioral
CC responses to sweeteners, glutamate and bitter substances
CC (PubMed:16322458). {ECO:0000269|PubMed:12937291,
CC ECO:0000269|PubMed:14672995, ECO:0000269|PubMed:15961431,
CC ECO:0000269|PubMed:16322458, ECO:0000269|PubMed:17706883,
CC ECO:0000269|PubMed:23345450}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; AY044240; AAK95327.2; -; mRNA.
DR EMBL; AB094663; BAC55013.1; -; mRNA.
DR EMBL; AB094664; BAC55014.1; -; mRNA.
DR EMBL; AK141196; BAE24579.1; -; mRNA.
DR EMBL; AK158334; BAE34462.1; -; mRNA.
DR EMBL; AC123699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL20025.1; -; Genomic_DNA.
DR EMBL; BC106964; AAI06965.1; -; mRNA.
DR CCDS; CCDS51607.1; -. [Q8K3P1-1]
DR CCDS; CCDS51608.1; -. [Q8K3P1-2]
DR CCDS; CCDS80361.1; -. [Q8K3P1-4]
DR CCDS; CCDS80362.1; -. [Q8K3P1-3]
DR CCDS; CCDS80363.1; -. [Q8K3P1-5]
DR RefSeq; NP_001158305.1; NM_001164833.1. [Q8K3P1-2]
DR RefSeq; NP_001158306.1; NM_001164834.1. [Q8K3P1-3]
DR RefSeq; NP_001297629.1; NM_001310700.1. [Q8K3P1-5]
DR RefSeq; NP_001297630.1; NM_001310701.1. [Q8K3P1-4]
DR RefSeq; NP_700449.2; NM_153400.4. [Q8K3P1-1]
DR RefSeq; XP_011247750.1; XM_011249448.2. [Q8K3P1-4]
DR AlphaFoldDB; Q8K3P1; -.
DR SMR; Q8K3P1; -.
DR STRING; 10090.ENSMUSP00000054233; -.
DR GlyGen; Q8K3P1; 3 sites.
DR PhosphoSitePlus; Q8K3P1; -.
DR PaxDb; Q8K3P1; -.
DR PRIDE; Q8K3P1; -.
DR ProteomicsDB; 294298; -. [Q8K3P1-1]
DR ProteomicsDB; 294299; -. [Q8K3P1-2]
DR ProteomicsDB; 294300; -. [Q8K3P1-3]
DR ProteomicsDB; 294301; -. [Q8K3P1-4]
DR ProteomicsDB; 294302; -. [Q8K3P1-5]
DR Antibodypedia; 2714; 336 antibodies from 32 providers.
DR DNASU; 231602; -.
DR Ensembl; ENSMUST00000058016; ENSMUSP00000054233; ENSMUSG00000029503. [Q8K3P1-5]
DR Ensembl; ENSMUST00000112478; ENSMUSP00000108097; ENSMUSG00000029503. [Q8K3P1-2]
DR Ensembl; ENSMUST00000195985; ENSMUSP00000143047; ENSMUSG00000029503. [Q8K3P1-1]
DR Ensembl; ENSMUST00000200037; ENSMUSP00000143554; ENSMUSG00000029503. [Q8K3P1-3]
DR Ensembl; ENSMUST00000200214; ENSMUSP00000142567; ENSMUSG00000029503. [Q8K3P1-4]
DR GeneID; 231602; -.
DR KEGG; mmu:231602; -.
DR UCSC; uc008yqq.1; mouse. [Q8K3P1-1]
DR UCSC; uc008yqs.2; mouse. [Q8K3P1-3]
DR UCSC; uc008yqt.2; mouse. [Q8K3P1-5]
DR UCSC; uc008yqu.2; mouse. [Q8K3P1-2]
DR CTD; 22953; -.
DR MGI; MGI:2665170; P2rx2.
DR VEuPathDB; HostDB:ENSMUSG00000029503; -.
DR eggNOG; ENOG502QVP9; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR InParanoid; Q8K3P1; -.
DR OMA; SHCKPTY; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; Q8K3P1; -.
DR TreeFam; TF328633; -.
DR Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-MMU-418346; Platelet homeostasis.
DR BioGRID-ORCS; 231602; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8K3P1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K3P1; protein.
DR Bgee; ENSMUSG00000029503; Expressed in vestibular membrane of cochlear duct and 54 other tissues.
DR Genevisible; Q8K3P1; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0046870; F:cadmium ion binding; ISO:MGI.
DR GO; GO:0050897; F:cobalt ion binding; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISO:MGI.
DR GO; GO:0045340; F:mercury ion binding; ISO:MGI.
DR GO; GO:0016151; F:nickel cation binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; ISO:MGI.
DR GO; GO:0043924; F:suramin binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0003029; P:detection of hypoxic conditions in blood by carotid body chemoreceptor signaling; IMP:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0030432; P:peristalsis; IMP:MGI.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0033198; P:response to ATP; IMP:MGI.
DR GO; GO:0009743; P:response to carbohydrate; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0002931; P:response to ischemia; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0010033; P:response to organic substance; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0050909; P:sensory perception of taste; IGI:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IMP:MGI.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003045; P2X2_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01309; P2X2RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein; Hearing;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..485
FT /note="P2X purinoceptor 2"
FT /id="PRO_0000425905"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..339
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 322..335
FT /note="Pore-forming motif"
FT /evidence="ECO:0000255"
FT REGION 406..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..443
FT /evidence="ECO:0000250"
FT DISULFID 126..177
FT /evidence="ECO:0000250"
FT DISULFID 137..160
FT /evidence="ECO:0000250"
FT DISULFID 143..171
FT /evidence="ECO:0000250"
FT DISULFID 227..237
FT /evidence="ECO:0000250"
FT DISULFID 271..280
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053887"
FT VAR_SEQ 59
FT /note="W -> WVASGAGTALSHR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053888"
FT VAR_SEQ 383..472
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16467187"
FT /id="VSP_053889"
FT VAR_SEQ 383..451
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16467187"
FT /id="VSP_053890"
FT CONFLICT 341
FT /note="I -> T (in Ref. 2; BAE34462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 53937 MW; ABDE08727CA66B70 CRC64;
MAAAQPRLPA GAAMVRRLAR GCWSAFWDYE TPKVIVVRNR RLGFVHRMVQ LLILLYFVWY
VFIVQKSYQD SETGPESSII TKVKGITMSE HKVWDVEEYV KPPEGGSVVS IITRIEVTPS
QTLGTCPESM RVHSSTCHLD DDCVAGQLDM QGNGIRTGRC VPYYHGDSKT CEVSAWCPVE
DGTSENHFLG KMAPNFTILI KNSIHYPKFK FSKGNIASQK SDYLKHCTFD QDSDPYCPIF
RLGFIVEQAG ENFTELAHKG GVIGVIINWN CDLDLSESEC NPKYSFRRLD PKYDPASSGY
NFRFAKYYKI NGTTTTRTLI KAYGIRIDVI VHGQAGKFSL IPTIINLATA LTSIGVGSFL
CDWILLTFMN KNKLYSHKKF DKVRTPRHPS SRWPVTLALV LGQIPPPPSH YSQDQPPSLP
SGEGPALGEG AELPLAVQPP RSCSSSALTE QVVDTLDQHM GQRPPVPEPS QQDSTSTDPK
GLAQL
