GENTAUR Molecular Products.

 LRP4_MOUSE              Reviewed;        1905 AA.
 Q8VI56; A2AGT4; Q8BPX5; Q8CBB3; Q8CCP5;
 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
 16-JUN-2009, sequence version 3.
 20-JUN-2018, entry version 151.
 RecName: Full=Low-density lipoprotein receptor-related protein 4;
          Short=LRP-4;
 AltName: Full=LDLR dan;
 Flags: Precursor;
 Name=Lrp4; Synonyms=Kiaa0816;
 Mus musculus (Mouse).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Mus; Mus.
 NCBI_TaxID=10090;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE.
 STRAIN=C57BL/6J;
 PubMed=16517118; DOI=10.1016/j.ygeno.2006.01.007;
 Simon-Chazottes D., Tutois S., Kuehn M., Evans M., Bourgade F.,
 Cook S., Davisson M.T., Guenet J.L.;
 "Mutations in the gene encoding the low-density lipoprotein receptor
 LRP4 cause abnormal limb development in the mouse.";
 Genomics 87:673-677(2006).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=C57BL/6J;
 PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
 Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
 She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
 Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
 Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
 Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
 Lindblad-Toh K., Eichler E.E., Ponting C.P.;
 "Lineage-specific biology revealed by a finished genome assembly of
 the mouse.";
 PLoS Biol. 7:E1000112-E1000112(2009).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
 TISSUE=Brain;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-566 (ISOFORMS 1/2).
 STRAIN=C57BL/6J; TISSUE=Bone, and Olfactory bulb;
 PubMed=16141072; DOI=10.1126/science.1112014;
 Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
 Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
 Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
 Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
 Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
 Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
 Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
 Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
 di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
 Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
 Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
 Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
 Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
 Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
 Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
 Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
 Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
 Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
 Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
 Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
 Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
 Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
 Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
 Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
 Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
 Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
 Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
 Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
 Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
 Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
 Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
 Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
 Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
 Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
 Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
 Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
 Hayashizaki Y.;
 "The transcriptional landscape of the mammalian genome.";
 Science 309:1559-1563(2005).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-1905 (ISOFORM 2).
 TISSUE=Brain;
 PubMed=14621295; DOI=10.1093/dnares/10.4.167;
 Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
 Saga Y., Nagase T., Ohara O., Koga H.;
 "Prediction of the coding sequences of mouse homologues of KIAA gene:
 III. The complete nucleotide sequences of 500 mouse KIAA-homologous
 cDNAs identified by screening of terminal sequences of cDNA clones
 randomly sampled from size-fractionated libraries.";
 DNA Res. 10:167-180(2003).
 [6]
 FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, FUNCTION AS RECEPTOR
 FOR AGRIN, AND INTERACTION WITH AGRIN AND MUSK.
 PubMed=18848351; DOI=10.1016/j.cell.2008.10.002;
 Kim N., Stiegler A.L., Cameron T.O., Hallock P.T., Gomez A.M.,
 Huang J.H., Hubbard S.R., Dustin M.L., Burden S.J.;
 "Lrp4 is a receptor for Agrin and forms a complex with MuSK.";
 Cell 135:334-342(2008).
 [7]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Brain, and Lung;
 PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
 Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
 Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
 "A tissue-specific atlas of mouse protein phosphorylation and
 expression.";
 Cell 143:1174-1189(2010).
 [8]
 FUNCTION.
 PubMed=21471202; DOI=10.1074/jbc.M110.190330;
 Leupin O., Piters E., Halleux C., Hu S., Kramer I., Morvan F.,
 Bouwmeester T., Schirle M., Bueno-Lozano M., Fuentes F.J., Itin P.H.,
 Boudin E., de Freitas F., Jennes K., Brannetti B., Charara N.,
 Ebersbach H., Geisse S., Lu C.X., Bauer A., Van Hul W., Kneissel M.;
 "Bone overgrowth-associated mutations in the LRP4 gene impair
 sclerostin facilitator function.";
 J. Biol. Chem. 286:19489-19500(2011).
 [9]
 INTERACTION WITH MESD, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
 FUNCTION.
 PubMed=24140340; DOI=10.1016/j.febslet.2013.10.001;
 Hoshi T., Tezuka T., Yokoyama K., Iemura S., Natsume T., Yamanashi Y.;
 "Mesdc2 plays a key role in cell-surface expression of Lrp4 and
 postsynaptic specialization in myotubes.";
 FEBS Lett. 587:3749-3754(2013).
 -!- FUNCTION: Mediates SOST-dependent inhibition of bone formation.
     Functions as a specific facilitator of SOST-mediated inhibition of
     Wnt signaling. Plays a key role in the formation and the
     maintenance of the neuromuscular junction (NMJ), the synapse
     between motor neuron and skeletal muscle. Directly binds AGRIN and
     recruits it to the MUSK signaling complex. Mediates the AGRIN-
     induced phosphorylation of MUSK, the kinase of the complex. The
     activation of MUSK in myotubes induces the formation of NMJ by
     regulating different processes including the transcription of
     specific genes and the clustering of AChR in the postsynaptic
     membrane. Alternatively, may be involved in the negative
     regulation of the canonical Wnt signaling pathway, being able to
     antagonize the LRP6-mediated activation of this pathway. More
     generally, has been proposed to function as a cell surface
     endocytic receptor binding and internalizing extracellular ligands
     for degradation by lysosomes. Plays an essential role in the
     process of digit differentiation (PubMed:16517118).
     {ECO:0000269|PubMed:16517118, ECO:0000269|PubMed:18848351,
     ECO:0000269|PubMed:21471202}.
 -!- SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms
     an AGRIN receptor complex that binds AGRIN resulting in activation
     of MUSK. Interacts (via the extracellular domain) with SOST; the
     interaction facilitates the inhibition of Wnt signaling (By
     similarity). Interacts with MESD; the interaction promotes
     glycosylation of LRP4 and its cell-surface expression
     (PubMed:24140340). {ECO:0000250, ECO:0000269|PubMed:24140340}.
 -!- INTERACTION:
     P25304:Agrn (xeno); NbExp=3; IntAct=EBI-2106160, EBI-2106099;
     Q9ERE7:Mesd; NbExp=2; IntAct=EBI-2106160, EBI-6662606;
 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24140340};
     Single-pass type I membrane protein {ECO:0000305}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=1;
       IsoId=Q8VI56-1; Sequence=Displayed;
     Name=2;
       IsoId=Q8VI56-2; Sequence=VSP_010034;
 -!- PTM: N-glycosylation is required for cell surface location.
     {ECO:0000269|PubMed:24140340}.
 -!- DISEASE: Note=Defects in Lrp4 are the cause of digitation anormale
     (dan) phenotype, this mutation is the consequence of a retroviral
     insertion. Dan mice shown growth retardation in 10-day-old mice
     dan/dan and polysyndactyly (PubMed:16517118). Defects in Lrp4 are
     the cause of malformed digits (mdig) phenotype. It is a
     spontaneous, autosomal recessive mutation resulting in
     polysyndactyly (PubMed:16517118). {ECO:0000269|PubMed:16517118}.
 -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=BAC27835.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
     Sequence=BAC29416.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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 EMBL; AF247637; AAL36970.1; -; mRNA.
 EMBL; AL732478; CAM24075.1; -; Genomic_DNA.
 EMBL; AL691489; CAM24075.1; JOINED; Genomic_DNA.
 EMBL; BC132240; AAI32241.1; -; mRNA.
 EMBL; AK032360; BAC27835.1; ALT_TERM; mRNA.
 EMBL; AK036406; BAC29416.1; ALT_SEQ; mRNA.
 EMBL; AK129224; BAC98034.1; -; Transcribed_RNA.
 CCDS; CCDS16432.1; -. [Q8VI56-1]
 RefSeq; NP_001139329.1; NM_001145857.1.
 RefSeq; NP_766256.3; NM_172668.3. [Q8VI56-1]
 UniGene; Mm.275149; -.
 UniGene; Mm.469960; -.
 ProteinModelPortal; Q8VI56; -.
 SMR; Q8VI56; -.
 IntAct; Q8VI56; 14.
 MINT; Q8VI56; -.
 STRING; 10090.ENSMUSP00000028689; -.
 iPTMnet; Q8VI56; -.
 PhosphoSitePlus; Q8VI56; -.
 PaxDb; Q8VI56; -.
 PeptideAtlas; Q8VI56; -.
 PRIDE; Q8VI56; -.
 Ensembl; ENSMUST00000028689; ENSMUSP00000028689; ENSMUSG00000027253. [Q8VI56-1]
 GeneID; 228357; -.
 KEGG; mmu:228357; -.
 UCSC; uc008kvx.2; mouse. [Q8VI56-1]
 CTD; 4038; -.
 MGI; MGI:2442252; Lrp4.
 eggNOG; KOG1215; Eukaryota.
 eggNOG; ENOG410XPR2; LUCA.
 GeneTree; ENSGT00760000118968; -.
 HOGENOM; HOG000047507; -.
 HOVERGEN; HBG049163; -.
 InParanoid; Q8VI56; -.
 KO; K20051; -.
 OMA; LNGSNME; -.
 OrthoDB; EOG091G0178; -.
 PhylomeDB; Q8VI56; -.
 TreeFam; TF315253; -.
 ChiTaRS; Lrp4; mouse.
 PRO; PR:Q8VI56; -.
 Proteomes; UP000000589; Chromosome 2.
 Bgee; ENSMUSG00000027253; -.
 Genevisible; Q8VI56; MM.
 GO; GO:0009986; C:cell surface; ISS:UniProtKB.
 GO; GO:0030425; C:dendrite; ISS:UniProtKB.
 GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
 GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
 GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
 GO; GO:0043235; C:receptor complex; IBA:GO_Central.
 GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
 GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
 GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
 GO; GO:0097110; F:scaffold protein binding; ISS:UniProtKB.
 GO; GO:0042813; F:Wnt-activated receptor activity; IBA:GO_Central.
 GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
 GO; GO:0048856; P:anatomical structure development; IMP:MGI.
 GO; GO:0030509; P:BMP signaling pathway; IEA:InterPro.
 GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
 GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
 GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
 GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
 GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO; GO:0001942; P:hair follicle development; IMP:MGI.
 GO; GO:0001822; P:kidney development; IMP:MGI.
 GO; GO:0060173; P:limb development; ISO:MGI.
 GO; GO:0050771; P:negative regulation of axonogenesis; IMP:UniProtKB.
 GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:MGI.
 GO; GO:0030279; P:negative regulation of ossification; ISO:MGI.
 GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
 GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
 GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
 GO; GO:1901631; P:positive regulation of presynaptic membrane organization; IDA:UniProtKB.
 GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
 GO; GO:0097104; P:postsynaptic membrane assembly; IMP:UniProtKB.
 GO; GO:0097105; P:presynaptic membrane assembly; IMP:UniProtKB.
 GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
 GO; GO:0008104; P:protein localization; IMP:MGI.
 GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
 GO; GO:0043113; P:receptor clustering; IMP:MGI.
 GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
 GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
 GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
 GO; GO:0051124; P:synaptic growth at neuromuscular junction; IDA:UniProtKB.
 GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
 GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; IBA:GO_Central.
 CDD; cd00112; LDLa; 7.
 Gene3D; 2.120.10.30; -; 4.
 InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
 InterPro; IPR026823; cEGF.
 InterPro; IPR001881; EGF-like_Ca-bd_dom.
 InterPro; IPR013032; EGF-like_CS.
 InterPro; IPR000742; EGF-like_dom.
 InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
 InterPro; IPR018097; EGF_Ca-bd_CS.
 InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
 InterPro; IPR036055; LDL_receptor-like_sf.
 InterPro; IPR023415; LDLR_class-A_CS.
 InterPro; IPR000033; LDLR_classB_rpt.
 InterPro; IPR002172; LDrepeatLR_classA_rpt.
 InterPro; IPR030799; LRP4.
 PANTHER; PTHR44017:SF4; PTHR44017:SF4; 1.
 Pfam; PF12662; cEGF; 1.
 Pfam; PF00057; Ldl_recept_a; 8.
 Pfam; PF00058; Ldl_recept_b; 16.
 PRINTS; PR00261; LDLRECEPTOR.
 SMART; SM00181; EGF; 7.
 SMART; SM00179; EGF_CA; 3.
 SMART; SM00192; LDLa; 8.
 SMART; SM00135; LY; 20.
 SUPFAM; SSF57184; SSF57184; 2.
 SUPFAM; SSF57424; SSF57424; 8.
 PROSITE; PS00010; ASX_HYDROXYL; 1.
 PROSITE; PS00022; EGF_1; 1.
 PROSITE; PS01186; EGF_2; 3.
 PROSITE; PS01187; EGF_CA; 1.
 PROSITE; PS01209; LDLRA_1; 8.
 PROSITE; PS50068; LDLRA_2; 8.
 PROSITE; PS51120; LDLRB; 20.
 1: Evidence at protein level;
 Alternative splicing; Calcium; Cell membrane; Complete proteome;
 Developmental protein; Differentiation; Disulfide bond;
 EGF-like domain; Endocytosis; Glycoprotein; Membrane; Receptor;
 Reference proteome; Repeat; Signal; Transmembrane;
 Transmembrane helix; Wnt signaling pathway.
 SIGNAL        1     20       {ECO:0000255}.
 CHAIN        21   1905       Low-density lipoprotein receptor-related
                              protein 4.
                              /FTId=PRO_0000017326.
 TOPO_DOM     21   1725       Extracellular. {ECO:0000255}.
 TRANSMEM   1726   1746       Helical. {ECO:0000255}.
 TOPO_DOM   1747   1905       Cytoplasmic. {ECO:0000255}.
 DOMAIN       26     67       LDL-receptor class A 1.
                              {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DOMAIN       70    106       LDL-receptor class A 2.
                              {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DOMAIN      109    144       LDL-receptor class A 3.
                              {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DOMAIN      147    183       LDL-receptor class A 4.
                              {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DOMAIN      190    226       LDL-receptor class A 5.
                              {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DOMAIN      230    266       LDL-receptor class A 6.
                              {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DOMAIN      269    305       LDL-receptor class A 7.
                              {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DOMAIN      311    350       LDL-receptor class A 8.
                              {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DOMAIN      354    394       EGF-like 1; atypical.
 DOMAIN      395    434       EGF-like 2; calcium-binding.
 REPEAT      480    522       LDL-receptor class B 1.
 REPEAT      523    565       LDL-receptor class B 2.
 REPEAT      566    609       LDL-receptor class B 3.
 REPEAT      610    652       LDL-receptor class B 4.
 REPEAT      653    693       LDL-receptor class B 5.
 DOMAIN      698    737       EGF-like 3.
 REPEAT      785    827       LDL-receptor class B 6.
 REPEAT      828    870       LDL-receptor class B 7.
 REPEAT      871    914       LDL-receptor class B 8.
 REPEAT      915    956       LDL-receptor class B 9.
 REPEAT      957    998       LDL-receptor class B 10.
 REPEAT     1093   1135       LDL-receptor class B 11.
 REPEAT     1136   1178       LDL-receptor class B 12.
 REPEAT     1179   1222       LDL-receptor class B 13.
 REPEAT     1223   1263       LDL-receptor class B 14.
 REPEAT     1264   1306       LDL-receptor class B 15.
 REPEAT     1397   1439       LDL-receptor class B 16.
 REPEAT     1440   1482       LDL-receptor class B 17.
 REPEAT     1483   1526       LDL-receptor class B 18.
 REPEAT     1527   1568       LDL-receptor class B 19.
 REPEAT     1569   1610       LDL-receptor class B 20.
 CARBOHYD    264    264       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    498    498       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    719    719       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    901    901       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1077   1077       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1415   1415       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1467   1467       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID     27     44       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID     34     57       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID     51     66       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID     71     83       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID     78     96       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID     90    105       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    110    122       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    117    135       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    129    143       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    148    160       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    155    173       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    167    182       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    191    203       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    198    216       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    210    225       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    231    243       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    238    256       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    250    265       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    270    282       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    277    295       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    289    304       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    312    324       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    319    337       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    331    349       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    358    369       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    365    378       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    380    393       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    399    409       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    405    418       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    420    433       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    702    713       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    709    722       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 DISULFID    724    736       {ECO:0000255|PROSITE-ProRule:PRU00124}.
 VAR_SEQ    1564   1620       Missing (in isoform 2).
                              {ECO:0000303|PubMed:14621295}.
                              /FTId=VSP_010034.
 CONFLICT    196    196       F -> L (in Ref. 4; BAC27835).
                              {ECO:0000305}.
 CONFLICT    325    325       I -> L (in Ref. 4; BAC29416).
                              {ECO:0000305}.
 CONFLICT    380    380       C -> R (in Ref. 1; AAL36970).
                              {ECO:0000305}.
 CONFLICT    682    685       HFPM -> LHTP (in Ref. 5). {ECO:0000305}.
 CONFLICT   1330   1330       G -> S (in Ref. 1; AAL36970).
                              {ECO:0000305}.
 SEQUENCE   1905 AA;  211954 MW;  282CA859B76D9BAD CRC64;
 MRRWWGALLL GALLCAHGIA SSLECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH
 SDEDGCTLPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG
 YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE
 SCPSAVPSPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS
 GLCINSGWRC DGDADCDDQS DERNCTTSMC TAEQFRCRSG RCVRLSWRCD GEDDCADNSD
 EENCENTGSP QCASDQFLCW NGRCIGQRKL CNGINDCGDS SDESPQQNCR PRTGEENCNV
 NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG RTCQDVNECA EEGYCSQGCT NTEGAFQCWC
 EAGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE
 LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL
 DGAHRKVLLW QSLEKPRAIA LHPMEGTIYW TDWGNTPRIE ASSMDGSGRR IIADTHLFWP
 NGLTIDYAGR RMYWVDAKHH VIERANLDGS HRKAVISQGL PHPFAITVFE DSLYWTDWHT
 KSINSANKFT GKNQEIIRNK LHFPMDIHTL HPQRQPAGKN RCGDNNGGCT HLCLPSGQNY
 TCACPTGFRK INSHACAQSL DKFLLFARRM DIRRISFDTE DLSDDVIPLA DVRSAVALDW
 DSRDDHVYWT DVSTDTISRA KWDGTGQEVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI
 EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASSRQVIISS
 NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGQRIYW
 TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRQRP PVTTLCAVEN GGCSHLCLRS
 PNPSGFSCTC PTGINLLRDG KTCSPGMNSF LIFARRIDVR MVSLDIPYFA DVVVPINMTM
 KNTIAIGVDP LEGKVYWSDS TLHRISRASL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW
 TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS
 DRTVLINNNL GWPNGLTVDK TSSQLLWADA HTERIEVADL NGANRHTLVS PVQHPYGLTL
 LDSYIYWTDW QTRSIHRADK STGSNVILVR SNLPGLMDIQ AVDRAQPLGF NKCGSRNGGC
 SHLCLPRPSG FSCACPTGIQ LKGDRKTCDP SPETYLLFSS RGSIRRISLD TDDHTDVHVP
 VPGLNNVISL DYDSVHGKVY YTDVFLDVIR RADLNGSNME TVIGHGLKTT DGLAVDWVAR
 NLYWTDTGRN TIEASRLDGS CRKVLINNSL DEPRAIAVFP RKGYLFWTDW GHIAKIERAN
 LDGSERKVLI NTDLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ VLVSHVSHPF
 ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL MDIIVVSPQR QTGTNACGVN
 NGGCTHLCFA RASDFVCACP DEPDGHPCSL VPGLVPPAPR ATSMNEKSPV LPNTLPTTLH
 SSTTKTRTSL EGAGGRCSER DAQLGLCAHS NEAVPAAPGE GLHVSYAIGG LLSILLILLV
 IAALMLYRHR KSKFTDPGMG NLTYSNPSYR TSTQEVKLEA APKPAVYNQL CYKKEGGPDH
 SYTKEKIKIV EGIRLLAGDD AEWGDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT
 ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS SESQV

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