LSR_HUMAN
ID LSR_HUMAN Reviewed; 649 AA.
AC Q86X29; A6NDW3; B4DKL4; E9PHD4; O00112; O00426; Q6ZT80; Q8NBM0; Q9BT33;
AC Q9UQL3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Lipolysis-stimulated lipoprotein receptor {ECO:0000305};
DE AltName: Full=Angulin-1 {ECO:0000303|PubMed:23239027};
GN Name=LSR {ECO:0000312|HGNC:HGNC:29572}; Synonyms=ILDR3, LISCH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Teramoto T., Thorgeirsson S.S.;
RT "Cloning and functional analysis of LISCH.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 6), AND VARIANT
RP ASN-363.
RC TISSUE=Amygdala, and Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT ASN-363.
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Pancreas, and Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=21245199; DOI=10.1242/jcs.072058;
RA Masuda S., Oda Y., Sasaki H., Ikenouchi J., Higashi T., Akashi M.,
RA Nishi E., Furuse M.;
RT "LSR defines cell corners for tricellular tight junction formation in
RT epithelial cells.";
RL J. Cell Sci. 124:548-555(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND SER-540, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-371; SER-389;
RP SER-432; SER-436; THR-453; SER-464; SER-467; SER-493; THR-501; SER-530;
RP SER-579; SER-643 AND SER-646, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-493; THR-501;
RP SER-530; TYR-535; SER-631 AND SER-646, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=23239027; DOI=10.1242/jcs.116442;
RA Higashi T., Tokuda S., Kitajiri S., Masuda S., Nakamura H., Oda Y.,
RA Furuse M.;
RT "Analysis of the 'angulin' proteins LSR, ILDR1 and ILDR2--tricellulin
RT recruitment, epithelial barrier function and implication in deafness
RT pathogenesis.";
RL J. Cell Sci. 126:966-977(2013).
CC -!- FUNCTION: Probable role in the clearance of triglyceride-rich
CC lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of
CC free fatty acids and allows their subsequent uptake in the cells (By
CC similarity). Maintains epithelial barrier function by recruiting
CC MARVELD2/tricellulin to tricellular tight junctions (By similarity).
CC {ECO:0000250|UniProtKB:Q99KG5, ECO:0000250|UniProtKB:Q9WU74}.
CC -!- SUBUNIT: Homotrimer or homotetramer (By similarity). Assembles into
CC cell-cell contacts. Interacts (via the cytoplasmic domain) with
CC MARVELD2 (via C-terminal cytoplasmic domain); the interaction is
CC required to recruit MARVELD2 to tricellular contacts. Interacts with
CC OCLN (By similarity). {ECO:0000250|UniProtKB:Q99KG5,
CC ECO:0000250|UniProtKB:Q9WU74}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21245199};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight
CC junction {ECO:0000269|PubMed:21245199, ECO:0000269|PubMed:23239027}.
CC Note=Located at tricellular contacts. {ECO:0000269|PubMed:21245199}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q86X29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86X29-2; Sequence=VSP_019691, VSP_019693;
CC Name=3;
CC IsoId=Q86X29-3; Sequence=VSP_019692, VSP_019694;
CC Name=4;
CC IsoId=Q86X29-4; Sequence=VSP_019692;
CC Name=5;
CC IsoId=Q86X29-5; Sequence=VSP_046797;
CC Name=6;
CC IsoId=Q86X29-6; Sequence=VSP_057210, VSP_057211;
CC -!- PTM: Phosphorylation at Ser-365 by MAPK8/JNK1 and MAPK9/JNK2 may be
CC required for exclusive localization at tricellular tight junstions.
CC {ECO:0000250|UniProtKB:Q99KG5}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. LISCH7 family.
CC {ECO:0000305}.
CC -!- CAUTION: In contrast to the rodent orthologous protein, it is longer in
CC N-terminus and no signal sequence is detected by any prediction method.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAB58317.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH04381.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF130366; AAD22101.1; -; mRNA.
DR EMBL; AK075426; BAC11614.1; -; mRNA.
DR EMBL; AK126834; BAC86714.1; -; mRNA.
DR EMBL; AK296618; BAG59226.1; -; mRNA.
DR EMBL; AC002128; AAB58317.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AD000684; AAB51178.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC004381; AAH04381.2; ALT_INIT; mRNA.
DR EMBL; BC047376; AAH47376.2; -; mRNA.
DR RefSeq; NP_001247418.1; NM_001260489.1.
DR RefSeq; NP_001247419.1; NM_001260490.1. [Q86X29-6]
DR RefSeq; NP_057009.3; NM_015925.6.
DR RefSeq; NP_991403.1; NM_205834.3.
DR RefSeq; NP_991404.1; NM_205835.3.
DR AlphaFoldDB; Q86X29; -.
DR BioGRID; 119629; 158.
DR IntAct; Q86X29; 51.
DR MINT; Q86X29; -.
DR STRING; 9606.ENSP00000480821; -.
DR GlyGen; Q86X29; 7 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; Q86X29; -.
DR PhosphoSitePlus; Q86X29; -.
DR SwissPalm; Q86X29; -.
DR BioMuta; LSR; -.
DR DMDM; 116242622; -.
DR EPD; Q86X29; -.
DR jPOST; Q86X29; -.
DR MassIVE; Q86X29; -.
DR MaxQB; Q86X29; -.
DR PaxDb; Q86X29; -.
DR PeptideAtlas; Q86X29; -.
DR PRIDE; Q86X29; -.
DR ProteomicsDB; 20511; -.
DR ProteomicsDB; 4469; -.
DR ProteomicsDB; 70230; -. [Q86X29-1]
DR ProteomicsDB; 70231; -. [Q86X29-2]
DR ProteomicsDB; 70232; -. [Q86X29-3]
DR Antibodypedia; 1523; 192 antibodies from 29 providers.
DR DNASU; 51599; -.
DR Ensembl; ENST00000347609.8; ENSP00000262627.3; ENSG00000105699.17. [Q86X29-2]
DR Ensembl; ENST00000354900.7; ENSP00000346976.2; ENSG00000105699.17. [Q86X29-4]
DR Ensembl; ENST00000360798.7; ENSP00000354034.2; ENSG00000105699.17. [Q86X29-5]
DR Ensembl; ENST00000361790.7; ENSP00000354575.2; ENSG00000105699.17. [Q86X29-1]
DR Ensembl; ENST00000427250.5; ENSP00000394479.1; ENSG00000105699.17. [Q86X29-6]
DR Ensembl; ENST00000602122.5; ENSP00000472569.1; ENSG00000105699.17. [Q86X29-3]
DR Ensembl; ENST00000621372.4; ENSP00000480821.1; ENSG00000105699.17. [Q86X29-1]
DR GeneID; 51599; -.
DR KEGG; hsa:51599; -.
DR UCSC; uc002nyl.4; human. [Q86X29-1]
DR CTD; 51599; -.
DR DisGeNET; 51599; -.
DR GeneCards; LSR; -.
DR HGNC; HGNC:29572; LSR.
DR HPA; ENSG00000105699; Tissue enhanced (liver).
DR MIM; 616582; gene.
DR neXtProt; NX_Q86X29; -.
DR OpenTargets; ENSG00000105699; -.
DR PharmGKB; PA142671504; -.
DR VEuPathDB; HostDB:ENSG00000105699; -.
DR eggNOG; ENOG502QWP5; Eukaryota.
DR GeneTree; ENSGT00950000183058; -.
DR HOGENOM; CLU_028969_2_0_1; -.
DR InParanoid; Q86X29; -.
DR OMA; GPLMNQP; -.
DR OrthoDB; 457764at2759; -.
DR PhylomeDB; Q86X29; -.
DR TreeFam; TF330877; -.
DR PathwayCommons; Q86X29; -.
DR Reactome; R-HSA-8964038; LDL clearance.
DR Reactome; R-HSA-8964046; VLDL clearance.
DR SignaLink; Q86X29; -.
DR BioGRID-ORCS; 51599; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; LSR; human.
DR GeneWiki; LSR_(gene); -.
DR GenomeRNAi; 51599; -.
DR Pharos; Q86X29; Tbio.
DR PRO; PR:Q86X29; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86X29; protein.
DR Bgee; ENSG00000105699; Expressed in mucosa of transverse colon and 147 other tissues.
DR ExpressionAtlas; Q86X29; baseline and differential.
DR Genevisible; Q86X29; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC.
DR GO; GO:0070160; C:tight junction; IDA:UniProtKB.
DR GO; GO:0061689; C:tricellular tight junction; ISS:ARUK-UCL.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0060856; P:establishment of blood-brain barrier; ISS:ARUK-UCL.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:ARUK-UCL.
DR GO; GO:0001889; P:liver development; ISS:HGNC.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0061833; P:protein localization to tricellular tight junction; ISS:ARUK-UCL.
DR GO; GO:1904274; P:tricellular tight junction assembly; ISS:ARUK-UCL.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR008664; LISCH7.
DR Pfam; PF05624; LSR; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Chylomicron;
KW Disulfide bond; Immunoglobulin domain; LDL; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix; VLDL.
FT CHAIN 1..649
FT /note="Lipolysis-stimulated lipoprotein receptor"
FT /id="PRO_0000245308"
FT TOPO_DOM 1..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 86..234
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU74"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 453
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17693683"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 535
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT DISULFID 111..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057210"
FT VAR_SEQ 52..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019691"
FT VAR_SEQ 200..308
FT /note="NADLTFDQTAWGDSGVYYCSVVSAQDLQGNNEAYAELIVLGRTSGVAELLPG
FT FQAGPIEDWLFVVVVCLAAFLIFLLLGICWCQCCPHTCCCYVRCPCCPDKCCCPEAL
FT -> M (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057211"
FT VAR_SEQ 240..308
FT /note="GRTSGVAELLPGFQAGPIEDWLFVVVVCLAAFLIFLLLGICWCQCCPHTCCC
FT YVRCPCCPDKCCCPEAL -> V (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_046797"
FT VAR_SEQ 240..258
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16303743"
FT /id="VSP_019692"
FT VAR_SEQ 366..386
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019693"
FT VAR_SEQ 386
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019694"
FT VARIANT 363
FT /note="S -> N (in dbSNP:rs34259399)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16303743"
FT /id="VAR_049902"
FT CONFLICT 259
FT /note="D -> G (in Ref. 4; AAB51178)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="L -> R (in Ref. 4; AAB51178)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="A -> G (in Ref. 4; AAB51178)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="G -> GR (in Ref. 2; BAC86714, 3; BAC11614 and 5;
FT AAH04381)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="N -> D (in Ref. 4; AAB51178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 649 AA; 71439 MW; 01E8F1CE0197CE9B CRC64;
MQQDGLGVGT RNGSGKGRSV HPSWPWCAPR PLRYFGRDAR ARRAQTAAMA LLAGGLSRGL
GSHPAAAGRD AVVFVWLLLS TWCTAPARAI QVTVSNPYHV VILFQPVTLP CTYQMTSTPT
QPIVIWKYKS FCRDRIADAF SPASVDNQLN AQLAAGNPGY NPYVECQDSV RTVRVVATKQ
GNAVTLGDYY QGRRITITGN ADLTFDQTAW GDSGVYYCSV VSAQDLQGNN EAYAELIVLG
RTSGVAELLP GFQAGPIEDW LFVVVVCLAA FLIFLLLGIC WCQCCPHTCC CYVRCPCCPD
KCCCPEALYA AGKAATSGVP SIYAPSTYAH LSPAKTPPPP AMIPMGPAYN GYPGGYPGDV
DRSSSAGGQG SYVPLLRDTD SSVASEVRSG YRIQASQQDD SMRVLYYMEK ELANFDPSRP
GPPSGRVERA MSEVTSLHED DWRSRPSRGP ALTPIRDEEW GGHSPRSPRG WDQEPAREQA
GGGWRARRPR ARSVDALDDL TPPSTAESGS RSPTSNGGRS RAYMPPRSRS RDDLYDQDDS
RDFPRSRDPH YDDFRSRERP PADPRSHHHR TRDPRDNGSR SGDLPYDGRL LEEAVRKKGS
EERRRPHKEE EEEAYYPPAP PPYSETDSQA SRERRLKKNL ALSRESLVV
