LTBP4_MOUSE
ID LTBP4_MOUSE Reviewed; 1666 AA.
AC Q8K4G1; E9QPD9; Q8K4G0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Latent-transforming growth factor beta-binding protein 4;
DE Short=LTBP-4;
DE Flags: Precursor;
GN Name=Ltbp4;
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 AND 2), AND DISRUPTION PHENOTYPE.
RX PubMed=12208849; DOI=10.1101/gad.229102;
RA Sterner-Kock A., Thorey I.S., Koli K., Wempe F., Otte J., Bangsow T.,
RA Kuhlmeier K., Kirchner T., Jin S., Keski-Oja J., von Melchner H.;
RT "Disruption of the gene encoding the latent transforming growth factor-beta
RT binding protein 4 (LTBP-4) causes abnormal lung development,
RT cardiomyopathy, and colorectal cancer.";
RL Genes Dev. 16:2264-2273(2002).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-1666 (ISOFORM 3).
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19836010; DOI=10.1016/j.ajhg.2009.09.013;
RA Urban Z., Hucthagowder V., Schuermann N., Todorovic V., Zilberberg L.,
RA Choi J., Sens C., Brown C.W., Clark R.D., Holland K.E., Marble M.,
RA Sakai L.Y., Dabovic B., Rifkin D.B., Davis E.C.;
RT "Mutations in LTBP4 cause a syndrome of impaired pulmonary,
RT gastrointestinal, genitourinary, musculoskeletal, and dermal development.";
RL Am. J. Hum. Genet. 85:593-605(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1564, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH EFEMP2.
RX PubMed=25713297; DOI=10.1242/dmm.018960;
RA Bultmann-Mellin I., Conradi A., Maul A.C., Dinger K., Wempe F., Wohl A.P.,
RA Imhof T., Wunderlich F.T., Bunck A.C., Nakamura T., Koli K., Bloch W.,
RA Ghanem A., Heinz A., von Melchner H., Sengle G., Sterner-Kock A.;
RT "Modeling autosomal recessive cutis laxa type 1C in mice reveals distinct
RT functions for Ltbp-4 isoforms.";
RL Dis. Model. Mech. 8:403-415(2015).
CC -!- FUNCTION: Key regulator of transforming growth factor beta (TGFB1,
CC TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in
CC a latent state during storage in extracellular space. Associates
CC specifically via disulfide bonds with the Latency-associated peptide
CC (LAP), which is the regulatory chain of TGF-beta, and regulates
CC integrin-dependent activation of TGF-beta.
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- SUBUNIT: Forms part of the large latent transforming growth factor beta
CC precursor complex; removal is essential for activation of complex.
CC Interacts with LTBP1 and TGFB1. Interacts with EFEMP2; this interaction
CC promotes fibrillar deposition of EFEMP2 (PubMed:25713297).
CC {ECO:0000250|UniProtKB:Q8N2S1, ECO:0000269|PubMed:25713297}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q8N2S1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=LTBP4L;
CC IsoId=Q8K4G1-1; Sequence=Displayed;
CC Name=2; Synonyms=LTBP4S;
CC IsoId=Q8K4G1-2; Sequence=VSP_009248, VSP_009250;
CC Name=3;
CC IsoId=Q8K4G1-3; Sequence=VSP_009249;
CC -!- PTM: Contains hydroxylated asparagine residues.
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- DISRUPTION PHENOTYPE: Mice reveal significant disruption of elastic
CC fibers in multiple tissues. They develop pulmonary septation defects,
CC rectal prolapse, colorectal adenomas, and dilated cardiomyopathy. They
CC survive up to six months (mid-adult age) without major clinical
CC symptoms. {ECO:0000269|PubMed:12208849, ECO:0000269|PubMed:19836010}.
CC -!- MISCELLANEOUS: [Isoform 3]: Sequence incomplete. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
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DR EMBL; AF410798; AAN04661.1; -; mRNA.
DR EMBL; AF410799; AAN04662.1; -; mRNA.
DR EMBL; AC157561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059016; AAH59016.1; -; mRNA.
DR CCDS; CCDS21017.1; -. [Q8K4G1-1]
DR CCDS; CCDS52158.1; -. [Q8K4G1-2]
DR RefSeq; NP_001107021.1; NM_001113549.1. [Q8K4G1-2]
DR RefSeq; NP_783572.2; NM_175641.2. [Q8K4G1-1]
DR AlphaFoldDB; Q8K4G1; -.
DR IntAct; Q8K4G1; 1.
DR STRING; 10090.ENSMUSP00000037536; -.
DR GlyGen; Q8K4G1; 5 sites.
DR iPTMnet; Q8K4G1; -.
DR PhosphoSitePlus; Q8K4G1; -.
DR CPTAC; non-CPTAC-3427; -.
DR MaxQB; Q8K4G1; -.
DR PaxDb; Q8K4G1; -.
DR PeptideAtlas; Q8K4G1; -.
DR PRIDE; Q8K4G1; -.
DR ProteomicsDB; 292127; -. [Q8K4G1-1]
DR ProteomicsDB; 292128; -. [Q8K4G1-2]
DR ProteomicsDB; 292129; -. [Q8K4G1-3]
DR Antibodypedia; 4199; 85 antibodies from 17 providers.
DR DNASU; 108075; -.
DR Ensembl; ENSMUST00000038618; ENSMUSP00000037536; ENSMUSG00000040488. [Q8K4G1-1]
DR Ensembl; ENSMUST00000121175; ENSMUSP00000113674; ENSMUSG00000040488. [Q8K4G1-2]
DR GeneID; 108075; -.
DR KEGG; mmu:108075; -.
DR UCSC; uc009fvs.2; mouse. [Q8K4G1-2]
DR UCSC; uc009fvt.2; mouse. [Q8K4G1-1]
DR CTD; 8425; -.
DR MGI; MGI:1321395; Ltbp4.
DR VEuPathDB; HostDB:ENSMUSG00000040488; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000158234; -.
DR HOGENOM; CLU_001884_0_0_1; -.
DR InParanoid; Q8K4G1; -.
DR OMA; LCDQYEG; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q8K4G1; -.
DR TreeFam; TF317514; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR BioGRID-ORCS; 108075; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ltbp4; mouse.
DR PRO; PR:Q8K4G1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K4G1; protein.
DR Bgee; ENSMUSG00000040488; Expressed in lip and 209 other tissues.
DR ExpressionAtlas; Q8K4G1; baseline and differential.
DR Genevisible; Q8K4G1; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0001527; C:microfibril; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR GO; GO:0048251; P:elastic fiber assembly; IMP:UniProtKB.
DR GO; GO:0046879; P:hormone secretion; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR Gene3D; 3.90.290.10; -; 4.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR Pfam; PF07645; EGF_CA; 17.
DR Pfam; PF00683; TB; 3.
DR SMART; SM00181; EGF; 20.
DR SMART; SM00179; EGF_CA; 19.
DR SUPFAM; SSF57184; SSF57184; 5.
DR SUPFAM; SSF57581; SSF57581; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 14.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 12.
DR PROSITE; PS50026; EGF_3; 16.
DR PROSITE; PS01187; EGF_CA; 17.
DR PROSITE; PS51364; TB; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Growth factor binding; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1666
FT /note="Latent-transforming growth factor beta-binding
FT protein 4"
FT /id="PRO_0000007648"
FT DOMAIN 148..180
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 286..338
FT /note="TB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 356..396
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 406..458
FT /note="TB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 588..629
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 630..671
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 672..713
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 714..751
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 753..794
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 795..836
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 877..919
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 920..961
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 962..1002
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1091..1132
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1223..1277
FT /note="TB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1295..1337
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1338..1379
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1391..1444
FT /note="TB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1575..1615
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1616..1660
FT /note="EGF-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 473..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..512
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..577
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1564
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1097
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 152..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 156..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 170..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 288..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 297..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 311..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 360..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 366..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 382..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 408..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 417..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 431..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 432..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 592..604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 599..613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 615..628
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 634..646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 641..655
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 657..670
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 676..688
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 683..697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 699..712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 718..730
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 725..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 741..750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 757..769
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 764..778
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 780..793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 799..811
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 806..820
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 822..835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 881..893
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 887..902
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 904..918
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 924..936
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 930..945
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 947..960
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 966..977
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 972..986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 988..1001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1095..1107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1101..1116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1118..1131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1225..1248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1235..1260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1235
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT DISULFID 1249..1265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1250..1277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1260
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT DISULFID 1299..1312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1307..1321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1323..1336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1342..1354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1349..1363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1365..1378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1393..1417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1403..1429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1418..1432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1419..1444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1579..1590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1585..1599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1601..1614
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1620..1635
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1630..1644
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1646..1659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12208849"
FT /id="VSP_009248"
FT VAR_SEQ 60..150
FT /note="KSSRCTRASCRVRNCPPAKCTGLEGCLTPTPSVPSPSRSPVEKSQVSLNWQP
FT LTLQEARALLRQRRPRGPWARALLKRRPPHRAPAGQARV -> RHEAALQPWRAARSCS
FT GCRYWCCWRSWGRSPYWADPESVFACASPPLCAACVASTGPLAPAVPRPARPATPPVDS
FT GAPGGAAPGGPGFRAF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009249"
FT VAR_SEQ 67..150
FT /note="ASCRVRNCPPAKCTGLEGCLTPTPSVPSPSRSPVEKSQVSLNWQPLTLQEAR
FT ALLRQRRPRGPWARALLKRRPPHRAPAGQARV -> MAGGAQLLWVSLLVLLAQLGPQP
FT VLGRPRERLRVRFTPAVCGLRCIHGPTGSRCTPTCAPRNATSVDSGAPGGAAPGGPGFR
FT AF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12208849"
FT /id="VSP_009250"
FT CONFLICT 361
FT /note="A -> S (in Ref. 3; AAH59016)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="G -> D (in Ref. 1; AAN04661)"
FT /evidence="ECO:0000305"
FT CONFLICT 1631
FT /note="V -> I (in Ref. 1; AAN04661/AAN04662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1666 AA; 178642 MW; 3784110C2B714E7D CRC64;
MRRPGLGGPC PLLLLLLLPA ATSASGSSPS PSPSPIEKAV VPSHQAGVAA CHCCLDQTPK
SSRCTRASCR VRNCPPAKCT GLEGCLTPTP SVPSPSRSPV EKSQVSLNWQ PLTLQEARAL
LRQRRPRGPW ARALLKRRPP HRAPAGQARV LCPLICHNGG VCVKPDRCLC PPDFAGKFCQ
LHSSGARPPA PAMPGLTRSV YTMPLANHRD DEHGVASMVS VHVEHPQEAS VVVHQVERVS
GPWEEANPEA LARAEAAARA EAAAPYTVLA QSAPREDGYS DASGFGYCFR ELRGSECASP
LPGLRTQEVC CRGEGLAWGV HDCHPCAEHL RNSNQVSGPN GPCPPGFERV NGSCVDVDEC
ATGGRCQHGE CANTRGGYTC VCPDGFLLDS SRSSCISQHV ISEAKGPCYR VLHDGGCSLP
ILRNITKQIC CCSRVGKAWG RGCQLCPPYG SEGFREICPA GPGYHYSASD LRYNTRPLNQ
DPPRVTFNQP RVPPATPRPP TGFLPTRRPE PRPDPGPQPE PRPRPEPRPR PESRPRPEPR
PRPEPRPQPE SQPRPESRPR PESQPWPEFP LPSIPAWTGP EIPESGPSSS MCQRNPQVCG
PGRCVPRPSG YTCACDPGFR LGPQGTRCID IDECRRVPTP CAPGRCENTP GSFRCVCGTG
FQAGPRATEC LDVDECRRVP PPCDRGRCEN TPGSFLCVCP AGYQAAPHGA SCQDVDECTQ
SPGLCGRGVC ENLPGSFRCV CPAGFRGSAC EEDVDECAQQ PPPCGPGRCD NTAGSFHCAC
PAGFRSRGPG APCQDVDECS RSPSPCAYGR CENTEGSFKC VCPTGFQPNA AGSECEDVDE
CENRLACPGQ ECVNSPGSFQ CRACPVGHHL HRGRCTDVDE CSSGTPCGLH GQCTNTKGSF
HCSCSTGYRA PSGQPGPCAD INECLEGDFC FPHGECLNTD GSFTCTCAPG YRPGPRGASC
LDVDECSEED LCQSGICTNT DGSFECICPP GHRAGPDLAS CLDIDECRER GPALCGSQRC
ENSPGSYRCV RDCDPGYHPG PEGTCDDIDE CREYGSAICG AQRCENTPGS YRCTPACDPG
YQPTPGGGCQ DVDECRNRSF CGAHAMCQNL PGSFQCVCDQ GYEGARDGRH CVDVNECETL
QGVCGSALCE NVEGSFLCVC PNSPEEFDPM TGRCVPPRAP AGTFPGSQPQ APASPSLPAR
PPAPPPPRRP SPPRQGPVSS GRRECYFDTA APDACDNILA RNVTWQECCC TVGEGWGSGC
RIQQCPGTET AEYQSLCPHG RGYLVPSGDL SARRDVDECQ LFQDQVCKSG VCVNTAPGYS
CYCSNGFYYH AHRLECVDND ECADEEPACE GGRCVNTVGS YHCTCEPPLV LDGSRRRCVS
NESQSLDDNL GVCWQEVGPD LVCSRPRLDR QATYTECCCL YGEAWGMDCA LCPAQDSDDF
EALCNVLRPP AYGPPRPGGF GIPYEYGPDI GPPYQSLPYG PDLYPPPVLP YDPYPPPPGP
FARREAPYGA PPFDMPDFED DGGPYGESET PDPPSRGTGW PYRSRDTRGS FPEPEESSER
GSYTGALSEP YEGLEAEECG ILDGCPHGRC VRVPEGFTCD CFDGYRLDIT RMSCVDVNEC
DEAEATSPLC VNARCVNTDG SFRCICRPGF APTHQPHHCA PARPRA
