LTBP1_HUMAN
ID LTBP1_HUMAN Reviewed; 1721 AA.
AC Q14766; A1L3V1; P22064; Q53SD8; Q53SF3; Q53SG1; Q59HF7; Q8TD95;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Latent-transforming growth factor beta-binding protein 1 {ECO:0000303|PubMed:8537398};
DE Short=LTBP-1 {ECO:0000303|PubMed:8537398};
DE AltName: Full=Transforming growth factor beta-1-binding protein 1 {ECO:0000303|PubMed:2350783};
DE Short=TGF-beta1-BP-1 {ECO:0000303|PubMed:2350783};
DE Flags: Precursor;
GN Name=LTBP1 {ECO:0000312|HGNC:HGNC:6714};
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 SHORT), PARTIAL PROTEIN SEQUENCE, AND
RP HYDROXYLATION AT ASN-974 AND ASN-1137.
RC TISSUE=Fibroblast, and Platelet;
RX PubMed=2350783; DOI=10.1016/0092-8674(90)90069-q;
RA Kanzaki T., Olofsson A., Moren A., Wernstedt C., Hellman U., Miyazono K.,
RA Claesson-Welsh L., Heldin C.-H.;
RT "TGF-beta 1 binding protein: a component of the large latent complex of
RT TGF-beta 1 with multiple repeat sequences.";
RL Cell 61:1051-1061(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RA Kwak J.H., Shin K.Y., Kim S.I.;
RT "Major alternative spliced-form of LTBP1 mRNA in human glomerular
RT endothelial cell.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC 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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346.
RC TISSUE=Blood;
RX PubMed=8537398; DOI=10.1074/jbc.270.52.31294;
RA Olofsson A., Ichijo H., Moren A., ten Dijke P., Miyazono K., Heldin C.-H.;
RT "Efficient association of an amino-terminally extended form of human latent
RT transforming growth factor-beta binding protein with the extracellular
RT matrix.";
RL J. Biol. Chem. 270:31294-31297(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 684-875 (ISOFORMS 4 AND 5).
RA Suzuki Y., Yamashita R., Shirota M., Sakakibara Y., Chiba J., Nakai K.,
RA Sugano S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND INTERACTION WITH TGFB1.
RX PubMed=2022183; DOI=10.1002/j.1460-2075.1991.tb08049.x;
RA Miyazono K., Olofsson A., Colosetti P., Heldin C.H.;
RT "A role of the latent TGF-beta 1-binding protein in the assembly and
RT secretion of TGF-beta 1.";
RL EMBO J. 10:1091-1101(1991).
RN [10]
RP FUNCTION, INTERACTION WITH TGFB1, DOMAIN, SUBCELLULAR LOCATION,
RP GLYCOSYLATION AT ASN-1366, DISULFIDE BOND, AND MUTAGENESIS OF ASN-1366.
RX PubMed=8617200; DOI=10.1002/j.1460-2075.1996.tb00355.x;
RA Saharinen J., Taipale J., Keski-Oja J.;
RT "Association of the small latent transforming growth factor-beta with an
RT eight cysteine repeat of its binding protein LTBP-1.";
RL EMBO J. 15:245-253(1996).
RN [11]
RP FUNCTION, INTERACTION WITH TGFB1, DOMAIN, GLYCOSYLATION AT ASN-1366,
RP DISULFIDE BOND, AND MUTAGENESIS OF ASN-1366.
RX PubMed=8939931; DOI=10.1074/jbc.271.47.29891;
RA Gleizes P.E., Beavis R.C., Mazzieri R., Shen B., Rifkin D.B.;
RT "Identification and characterization of an eight-cysteine repeat of the
RT latent transforming growth factor-beta binding protein-1 that mediates
RT bonding to the latent transforming growth factor-beta1.";
RL J. Biol. Chem. 271:29891-29896(1996).
RN [12]
RP REVIEW.
RX PubMed=10743502; DOI=10.1016/s1359-6101(99)00010-6;
RA Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.;
RT "Latent transforming growth factor-beta binding proteins (LTBPs)
RT -- structural extracellular matrix proteins for targeting TGF-beta
RT action.";
RL Cytokine Growth Factor Rev. 10:99-117(1999).
RN [13]
RP REVIEW.
RX PubMed=11104663; DOI=10.1042/bj3520601;
RA Oklu R., Hesketh R.;
RT "The latent transforming growth factor beta binding protein (LTBP)
RT family.";
RL Biochem. J. 352:601-610(2000).
RN [14]
RP GLYCOSYLATION AT ASN-1366.
RX PubMed=10677208; DOI=10.1021/bi9918285;
RA Rudd P.M., Downing A.K., Cadene M., Harvey D.J., Wormald M.R., Weir I.,
RA Dwek R.A., Rifkin D.B., Gleizes P.E.;
RT "Hybrid and complex glycans are linked to the conserved N-glycosylation
RT site of the third eight-cysteine domain of LTBP-1 in insect cells.";
RL Biochemistry 39:1596-1603(2000).
RN [15]
RP INTERACTION WITH TGFB1, AND MUTAGENESIS OF 1385-GLU--PRO-1388.
RX PubMed=10930463; DOI=10.1091/mbc.11.8.2691;
RA Saharinen J., Keski-Oja J.;
RT "Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins,
RT LTBPs, creates a hydrophobic interaction surface for binding of small
RT latent TGF-beta.";
RL Mol. Biol. Cell 11:2691-2704(2000).
RN [16]
RP INTERACTION WITH FBN1 AND FBN2.
RX PubMed=12429738; DOI=10.1074/jbc.m209256200;
RA Isogai Z., Ono R.N., Ushiro S., Keene D.R., Chen Y., Mazzieri R.,
RA Charbonneau N.L., Reinhardt D.P., Rifkin D.B., Sakai L.Y.;
RT "Latent transforming growth factor beta-binding protein 1 interacts with
RT fibrillin and is a microfibril-associated protein.";
RL J. Biol. Chem. 278:2750-2757(2003).
RN [17]
RP FUNCTION.
RX PubMed=15184403; DOI=10.1083/jcb.200312172;
RA Annes J.P., Chen Y., Munger J.S., Rifkin D.B.;
RT "Integrin alphaVbeta6-mediated activation of latent TGF-beta requires the
RT latent TGF-beta binding protein-1.";
RL J. Cell Biol. 165:723-734(2004).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=16157329; DOI=10.1016/j.yexcr.2005.08.008;
RA Koli K., Hyytieainen M., Ryynanen M.J., Keski-Oja J.;
RT "Sequential deposition of latent TGF-beta binding proteins (LTBPs) during
RT formation of the extracellular matrix in human lung fibroblasts.";
RL Exp. Cell Res. 310:370-382(2005).
RN [19]
RP INTERACTION WITH TGFB1, AND MUTAGENESIS OF GLU-1348 AND 1382-ASP--GLU-1385.
RX PubMed=15567420; DOI=10.1016/j.jmb.2004.10.039;
RA Chen Y., Ali T., Todorovic V., O'leary J.M., Kristina Downing A.,
RA Rifkin D.B.;
RT "Amino acid requirements for formation of the TGF-beta-latent TGF-beta
RT binding protein complexes.";
RL J. Mol. Biol. 345:175-186(2005).
RN [20]
RP INTERACTION WITH FBN1, C-TERMINAL REGION DOMAIN, AND TISSUE SPECIFICITY.
RX PubMed=17293099; DOI=10.1016/j.matbio.2006.12.006;
RA Hirani R., Hanssen E., Gibson M.A.;
RT "LTBP-2 specifically interacts with the amino-terminal region of fibrillin-
RT 1 and competes with LTBP-1 for binding to this microfibrillar protein.";
RL Matrix Biol. 26:213-223(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1597, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [22]
RP INTERACTION WITH ADAMTSL2.
RX PubMed=18677313; DOI=10.1038/ng.199;
RA Le Goff C., Morice-Picard F., Dagoneau N., Wang L.W., Perrot C., Crow Y.J.,
RA Bauer F., Flori E., Prost-Squarcioni C., Krakow D., Ge G., Greenspan D.S.,
RA Bonnet D., Le Merrer M., Munnich A., Apte S.S., Cormier-Daire V.;
RT "ADAMTSL2 mutations in geleophysic dysplasia demonstrate a role for ADAMTS-
RT like proteins in TGF-beta bioavailability regulation.";
RL Nat. Genet. 40:1119-1123(2008).
RN [23]
RP FUNCTION, AND INTERACTION WITH TGFB1.
RX PubMed=22278742; DOI=10.1091/mbc.e11-12-1018;
RA Wang R., Zhu J., Dong X., Shi M., Lu C., Springer T.A.;
RT "GARP regulates the bioavailability and activation of TGFbeta.";
RL Mol. Biol. Cell 23:1129-1139(2012).
RN [24]
RP IDENTIFICATION BY MASS 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 [25]
RP PHOSPHORYLATION AT SER-1414.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [26]
RP INTERACTION WITH EFEMP2.
RX PubMed=27339457; DOI=10.1016/j.matbio.2016.06.003;
RA Sasaki T., Hanisch F.G., Deutzmann R., Sakai L.Y., Sakuma T., Miyamoto T.,
RA Yamamoto T., Hannappel E., Chu M.L., Lanig H., von der Mark K.;
RT "Functional consequence of fibulin-4 missense mutations associated with
RT vascular and skeletal abnormalities and cutis laxa.";
RL Matrix Biol. 56:132-149(2016).
RN [27]
RP GLYCOSYLATION AT SER-647; SER-937; SER-1019; SER-1059; SER-1141; SER-1224;
RP SER-1488 AND SER-1687.
RX PubMed=34411563; DOI=10.1016/j.jbc.2021.101055;
RA Williamson D.B., Sohn C.J., Ito A., Haltiwanger R.S.;
RT "POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2,
RT and LTBP1 and promote secretion of fibrillin-1.";
RL J. Biol. Chem. 297:101055-101055(2021).
RN [28]
RP STRUCTURE BY NMR OF 1340-1412, AND DISULFIDE BONDS.
RX PubMed=14607119; DOI=10.1016/j.jmb.2003.09.053;
RA Lack J., O'Leary J.M., Knott V., Yuan X., Rifkin D.B., Handford P.A.,
RA Downing A.K.;
RT "Solution structure of the third TB domain from LTBP1 provides insight into
RT assembly of the large latent complex that sequesters latent TGF-beta.";
RL J. Mol. Biol. 334:281-291(2003).
RN [29]
RP INVOLVEMENT IN ARCL2E, VARIANTS ARCL2E 448-GLN--GLU-1721 DEL AND
RP 1477-CYS--GLU-1721, CHARACTERIZATION OF VARIANTS ARCL2E 448-GLN--GLU-1721
RP DEL AND 1477-CYS--GLU-172, AND INTERACTION WITH FBN1 AND FBN2.
RX PubMed=33991472; DOI=10.1016/j.ajhg.2021.04.016;
RA Pottie L., Adamo C.S., Beyens A., Luetke S., Tapaneeyaphan P.,
RA De Clercq A., Salmon P.L., De Rycke R., Gezdirici A., Gulec E.Y., Khan N.,
RA Urquhart J.E., Newman W.G., Metcalfe K., Efthymiou S., Maroofian R.,
RA Anwar N., Maqbool S., Rahman F., Altweijri I., Alsaleh M., Abdullah S.M.,
RA Al-Owain M., Hashem M., Houlden H., Alkuraya F.S., Sips P., Sengle G.,
RA Callewaert B.;
RT "Bi-allelic premature truncating variants in LTBP1 cause cutis laxa
RT syndrome.";
RL Am. J. Hum. Genet. 108:1095-1114(2021).
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 (PubMed:2022183,
CC PubMed:8617200, PubMed:8939931). Associates specifically via disulfide
CC bonds with the Latency-associated peptide (LAP), which is the
CC regulatory chain of TGF-beta, and regulates integrin-dependent
CC activation of TGF-beta (PubMed:8617200, PubMed:8939931,
CC PubMed:15184403). Outcompeted by LRRC32/GARP for binding to LAP
CC regulatory chain of TGF-beta (PubMed:22278742).
CC {ECO:0000269|PubMed:15184403, ECO:0000269|PubMed:2022183,
CC ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:8617200,
CC ECO:0000269|PubMed:8939931}.
CC -!- SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with the
CC Latency-associated peptide chain (LAP) regulatory chain of TGFB1,
CC leading to regulate activation of TGF-beta-1 (PubMed:10930463,
CC PubMed:2022183, PubMed:8617200, PubMed:15567420, PubMed:8939931,
CC PubMed:22278742). LTBP1 does not bind directly to TGF-beta-1, the
CC active chain of TGFB1 (PubMed:10930463). Interacts (via C-terminal
CC domain) with FBN1 (via N-terminal domain) (PubMed:12429738,
CC PubMed:17293099, PubMed:33991472). Interacts with FBN2
CC (PubMed:12429738, PubMed:33991472). Interacts with ADAMTSL2
CC (PubMed:18677313). Interacts with EFEMP2 (PubMed:27339457).
CC {ECO:0000269|PubMed:10930463, ECO:0000269|PubMed:12429738,
CC ECO:0000269|PubMed:15567420, ECO:0000269|PubMed:17293099,
CC ECO:0000269|PubMed:18677313, ECO:0000269|PubMed:2022183,
CC ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:27339457,
CC ECO:0000269|PubMed:33991472, ECO:0000269|PubMed:8617200,
CC ECO:0000269|PubMed:8939931}.
CC -!- INTERACTION:
CC Q14766-1; P01137: TGFB1; NbExp=4; IntAct=EBI-11173861, EBI-779636;
CC Q14766-2; P35555: FBN1; NbExp=2; IntAct=EBI-11173832, EBI-2505934;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16157329}. Secreted,
CC extracellular space, extracellular matrix {ECO:0000269|PubMed:16157329,
CC ECO:0000269|PubMed:8617200}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=Long; Synonyms=LTBP-1L;
CC IsoId=Q14766-1; Sequence=Displayed;
CC Name=Short; Synonyms=LTBP-1S;
CC IsoId=Q14766-2, P22064-1;
CC Sequence=VSP_036963, VSP_036964;
CC Name=3;
CC IsoId=Q14766-3; Sequence=VSP_036963, VSP_036964, VSP_036965;
CC Name=4;
CC IsoId=Q14766-4; Sequence=VSP_040125;
CC Name=5;
CC IsoId=Q14766-5; Sequence=VSP_036963, VSP_036964, VSP_040125;
CC -!- TISSUE SPECIFICITY: Expressed in the aorta (at protein level)
CC (PubMed:17293099). Isoform Long: Expressed in fibroblasts
CC (PubMed:17293099). {ECO:0000269|PubMed:17293099}.
CC -!- DOMAIN: The 8-Cys3 region in the third TB domain mediates the
CC interchain disulfide bond interaction with the Latency-associated
CC peptide chain (LAP) regulatory chain of TGFB1.
CC {ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931}.
CC -!- PTM: Contains hydroxylated asparagine residues.
CC {ECO:0000269|PubMed:2350783}.
CC -!- PTM: Isoform Short N-terminus is blocked. {ECO:0000269|PubMed:2350783}.
CC -!- PTM: Two intrachain disulfide bonds from the TB3 domain are rearranged
CC upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide,
CC anchoring it to the extracellular matrix.
CC {ECO:0000269|PubMed:14607119}.
CC -!- PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3.
CC {ECO:0000269|PubMed:34411563}.
CC -!- DISEASE: Cutis laxa, autosomal recessive, 2E (ARCL2E) [MIM:619451]: A
CC form of cutis laxa, a disorder characterized by an excessive congenital
CC skin wrinkling, a large fontanelle with delayed closure, a typical
CC facial appearance with downslanting palpebral fissures, and a general
CC connective tissue weakness. ARCL2E patients present with cutis laxa,
CC inguinal hernia, craniofacial dysmorphology, variable heart defects,
CC and prominent skeletal features including craniosynostosis, short
CC stature, brachydactyly, and syndactyly. {ECO:0000269|PubMed:33991472}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92038.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M34057; AAA61160.1; -; mRNA.
DR EMBL; AF489528; AAM03124.1; -; mRNA.
DR EMBL; AB208801; BAD92038.1; ALT_INIT; mRNA.
DR EMBL; AC019195; AAY14953.1; -; Genomic_DNA.
DR EMBL; AC019127; AAY24260.1; -; Genomic_DNA.
DR EMBL; AC020594; AAY15036.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00437.1; -; Genomic_DNA.
DR EMBL; BC130289; AAI30290.1; -; mRNA.
DR EMBL; L48925; AAA96327.1; -; Genomic_DNA.
DR EMBL; BP291349; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS33177.2; -. [Q14766-1]
DR CCDS; CCDS33178.2; -. [Q14766-2]
DR CCDS; CCDS54345.1; -. [Q14766-3]
DR PIR; A35626; A35626.
DR RefSeq; NP_000618.3; NM_000627.3. [Q14766-2]
DR RefSeq; NP_001159736.1; NM_001166264.1.
DR RefSeq; NP_001159737.1; NM_001166265.1. [Q14766-3]
DR RefSeq; NP_001159738.1; NM_001166266.1.
DR RefSeq; NP_996826.2; NM_206943.2. [Q14766-1]
DR RefSeq; XP_011531155.1; XM_011532853.2. [Q14766-4]
DR PDB; 1KSQ; NMR; -; A=1340-1412.
DR PDBsum; 1KSQ; -.
DR AlphaFoldDB; Q14766; -.
DR SASBDB; Q14766; -.
DR SMR; Q14766; -.
DR BioGRID; 110230; 70.
DR DIP; DIP-50011N; -.
DR IntAct; Q14766; 37.
DR MINT; Q14766; -.
DR STRING; 9606.ENSP00000386043; -.
DR GlyConnect; 329; 37 N-Linked glycans (5 sites).
DR GlyGen; Q14766; 25 sites, 52 N-linked glycans (5 sites), 5 O-linked glycans (14 sites).
DR iPTMnet; Q14766; -.
DR PhosphoSitePlus; Q14766; -.
DR BioMuta; LTBP1; -.
DR DMDM; 290457687; -.
DR EPD; Q14766; -.
DR jPOST; Q14766; -.
DR MassIVE; Q14766; -.
DR MaxQB; Q14766; -.
DR PaxDb; Q14766; -.
DR PeptideAtlas; Q14766; -.
DR PRIDE; Q14766; -.
DR ProteomicsDB; 60159; -. [Q14766-1]
DR ProteomicsDB; 60160; -. [Q14766-2]
DR ProteomicsDB; 60161; -. [Q14766-3]
DR ProteomicsDB; 60162; -. [Q14766-4]
DR ProteomicsDB; 60163; -. [Q14766-5]
DR Antibodypedia; 1284; 213 antibodies from 30 providers.
DR DNASU; 4052; -.
DR Ensembl; ENST00000404525.5; ENSP00000385359.1; ENSG00000049323.16. [Q14766-3]
DR Ensembl; ENST00000404816.7; ENSP00000386043.2; ENSG00000049323.16. [Q14766-1]
DR Ensembl; ENST00000407925.5; ENSP00000384091.1; ENSG00000049323.16. [Q14766-2]
DR GeneID; 4052; -.
DR KEGG; hsa:4052; -.
DR MANE-Select; ENST00000404816.7; ENSP00000386043.2; NM_206943.4; NP_996826.3.
DR UCSC; uc002rou.4; human. [Q14766-1]
DR CTD; 4052; -.
DR DisGeNET; 4052; -.
DR GeneCards; LTBP1; -.
DR HGNC; HGNC:6714; LTBP1.
DR HPA; ENSG00000049323; Tissue enhanced (cervix).
DR MIM; 150390; gene.
DR MIM; 619451; phenotype.
DR neXtProt; NX_Q14766; -.
DR OpenTargets; ENSG00000049323; -.
DR Orphanet; 90349; Autosomal recessive cutis laxa type 1.
DR PharmGKB; PA30477; -.
DR VEuPathDB; HostDB:ENSG00000049323; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000155823; -.
DR InParanoid; Q14766; -.
DR OMA; SQRCTKX; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q14766; -.
DR TreeFam; TF317514; -.
DR PathwayCommons; Q14766; -.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q14766; -.
DR SIGNOR; Q14766; -.
DR BioGRID-ORCS; 4052; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; LTBP1; human.
DR EvolutionaryTrace; Q14766; -.
DR GeneWiki; LTBP1_(gene); -.
DR GenomeRNAi; 4052; -.
DR Pharos; Q14766; Tbio.
DR PRO; PR:Q14766; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q14766; protein.
DR Bgee; ENSG00000049323; Expressed in blood vessel layer and 207 other tissues.
DR ExpressionAtlas; Q14766; baseline and differential.
DR Genevisible; Q14766; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0001527; C:microfibril; IDA:AgBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050436; F:microfibril binding; IDA:AgBase.
DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:UniProtKB.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; NAS:UniProtKB.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; IDA:UniProtKB.
DR GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; IDA:UniProtKB.
DR Gene3D; 3.90.290.10; -; 4.
DR InterPro; IPR026823; cEGF.
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; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 13.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00179; EGF_CA; 16.
DR SUPFAM; SSF57184; SSF57184; 5.
DR SUPFAM; SSF57581; SSF57581; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 13.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS01187; EGF_CA; 15.
DR PROSITE; PS51364; TB; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disease variant; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Growth factor binding; Hydroxylation; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1721
FT /note="Latent-transforming growth factor beta-binding
FT protein 1"
FT /id="PRO_0000007635"
FT DOMAIN 187..219
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 399..431
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 557..609
FT /note="TB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 626..663
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 677..729
FT /note="TB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 873..910
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 915..956
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 957..997
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 998..1037
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1038..1078
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1079..1119
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1120..1160
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1161..1201
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1202..1243
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1244..1281
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1286..1328
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1347..1401
FT /note="TB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1424..1466
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1467..1503
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1524..1577
FT /note="TB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1621..1657
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1662..1706
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 64..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1411
FT /note="8-Cys3 region"
FT /evidence="ECO:0000269|PubMed:8617200,
FT ECO:0000269|PubMed:8939931"
FT REGION 1507..1721
FT /note="C-terminal domain"
FT /evidence="ECO:0000269|PubMed:17293099"
FT MOTIF 1174..1176
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 96..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 974
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000269|PubMed:2350783"
FT MOD_RES 1137
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000269|PubMed:2350783"
FT MOD_RES 1414
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 1597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 1616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG19"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
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 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 937
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1019
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1059
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1141
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1224
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10677208,
FT ECO:0000269|PubMed:8617200"
FT /id="CAR_000184"
FT CARBOHYD 1488
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1687
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT DISULFID 191..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 195..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 209..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 403..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 407..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 421..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 559..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 568..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 582..597
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 630..641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 636..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 652..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 679..702
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 689..714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 703..717
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 704..729
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 877..889
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 884..898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 900..913
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 919..931
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 926..940
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 942..955
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 961..972
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 967..981
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 984..996
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1002..1013
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1008..1022
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1025..1036
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1042..1053
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1048..1062
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1064..1077
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1083..1094
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1089..1103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1105..1118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1124..1135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1130..1144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1146..1159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1165..1177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1172..1186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1188..1200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1206..1218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1212..1227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1229..1242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1248..1260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1254..1269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1349..1372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697,
FT ECO:0000269|PubMed:14607119"
FT DISULFID 1359..1384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697,
FT ECO:0000269|PubMed:14607119"
FT DISULFID 1359
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000305|PubMed:14607119"
FT DISULFID 1373..1389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697,
FT ECO:0000269|PubMed:14607119"
FT DISULFID 1374..1401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697,
FT ECO:0000269|PubMed:14607119"
FT DISULFID 1384
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000305|PubMed:14607119"
FT DISULFID 1471..1482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1477..1491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1526..1550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1536..1562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1551..1565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1552..1577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1625..1636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1631..1645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1666..1681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1676..1690
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1692..1705
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..326
FT /note="Missing (in isoform Short, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2350783, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.8"
FT /id="VSP_036963"
FT VAR_SEQ 327..345
FT /note="EGSFPLRYVQDQVAAPFQL -> MDTKLMCLLFFFSLPPLLV (in
FT isoform Short, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2350783, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.8"
FT /id="VSP_036964"
FT VAR_SEQ 724..776
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_036965"
FT VAR_SEQ 839..840
FT /note="PV -> PGI (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_040125"
FT VARIANT 448..1721
FT /note="Missing (in ARCL2E; loss of interaction with FBN1
FT AND FBN2)"
FT /evidence="ECO:0000269|PubMed:33991472"
FT /id="VAR_086071"
FT VARIANT 1477..1721
FT /note="Missing (in ARCL2E; loss of interaction with FBN1
FT AND FBN2)"
FT /evidence="ECO:0000269|PubMed:33991472"
FT /id="VAR_086072"
FT MUTAGEN 1348
FT /note="E->A: Abolishes interaction with the Latency-
FT associated peptide chain (LAP) regulatory chain of TGFB1;
FT when associated with 1382-A--A-1385."
FT /evidence="ECO:0000269|PubMed:15567420"
FT MUTAGEN 1366
FT /note="N->A,Q: Abolishes N-glycosylation at this site
FT without affecting ability to interact with the Latency-
FT associated peptide chain (LAP) regulatory chain of TGFB1."
FT /evidence="ECO:0000269|PubMed:8617200,
FT ECO:0000269|PubMed:8939931"
FT MUTAGEN 1382..1385
FT /note="DNCE->ANCA: Abolishes interaction with the Latency-
FT associated peptide chain (LAP) regulatory chain of TGFB1;
FT when associated with A-1348."
FT /evidence="ECO:0000269|PubMed:15567420"
FT MUTAGEN 1385..1388
FT /note="EIFP->DL: Loss of binding to TGFB1."
FT /evidence="ECO:0000269|PubMed:10930463"
FT CONFLICT 50
FT /note="R -> AS (in Ref. 7; AAA96327)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="H -> Y (in Ref. 1; AAA61160)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="S -> P (in Ref. 8; BP291349)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="Missing (in Ref. 1; AAA61160 and 2; AAM03124)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="R -> M (in Ref. 8; BP291349)"
FT /evidence="ECO:0000305"
FT CONFLICT 792..794
FT /note="PGV -> ARS (in Ref. 1; AAA61160 and 2; AAM03124)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="T -> A (in Ref. 1; AAA61160)"
FT /evidence="ECO:0000305"
FT CONFLICT 1378
FT /note="V -> A (in Ref. 1; AAA61160, 2; AAM03124, 3;
FT BAD92038, 5; EAX00437 and 6; AAI30290)"
FT /evidence="ECO:0000305"
FT CONFLICT 1648
FT /note="F -> L (in Ref. 1; AAA61160 and 2; AAM03124)"
FT /evidence="ECO:0000305"
FT CONFLICT 1661
FT /note="V -> F (in Ref. 1; AAA61160)"
FT /evidence="ECO:0000305"
FT STRAND 1340..1342
FT /evidence="ECO:0007829|PDB:1KSQ"
FT STRAND 1346..1353
FT /evidence="ECO:0007829|PDB:1KSQ"
FT TURN 1355..1358
FT /evidence="ECO:0007829|PDB:1KSQ"
FT STRAND 1366..1368
FT /evidence="ECO:0007829|PDB:1KSQ"
FT HELIX 1369..1374
FT /evidence="ECO:0007829|PDB:1KSQ"
FT STRAND 1378..1382
FT /evidence="ECO:0007829|PDB:1KSQ"
FT STRAND 1385..1388
FT /evidence="ECO:0007829|PDB:1KSQ"
FT STRAND 1392..1394
FT /evidence="ECO:0007829|PDB:1KSQ"
FT HELIX 1395..1400
FT /evidence="ECO:0007829|PDB:1KSQ"
FT STRAND 1408..1410
FT /evidence="ECO:0007829|PDB:1KSQ"
SQ SEQUENCE 1721 AA; 186796 MW; 432489CAC3023754 CRC64;
MAGAWLRWGL LLWAGLLASS AHGRLRRITY VVHPGPGLAA GALPLSGPPR SRTFNVALNA
RYSRSSAAAG APSRASPGVP SERTRRTSKP GGAALQGLRP PPPPPPEPAR PAVPGGQLHP
NPGGHPAAAP FTKQGRQVVR SKVPQETQSG GGSRLQVHQK QQLQGVNVCG GRCCHGWSKA
PGSQRCTKPS CVPPCQNGGM CLRPQLCVCK PGTKGKACET IAAQDTSSPV FGGQSPGAAS
SWGPPEQAAK HTSSKKADTL PRVSPVAQMT LTLKPKPSVG LPQQIHSQVT PLSSQSVVIH
HGQTQEYVLK PKYFPAQKGI SGEQSTEGSF PLRYVQDQVA APFQLSNHTG RIKVVFTPSI
CKVTCTKGSC QNSCEKGNTT TLISENGHAA DTLTATNFRV VICHLPCMNG GQCSSRDKCQ
CPPNFTGKLC QIPVHGASVP KLYQHSQQPG KALGTHVIHS THTLPLTVTS QQGVKVKFPP
NIVNIHVKHP PEASVQIHQV SRIDGPTGQK TKEAQPGQSQ VSYQGLPVQK TQTIHSTYSH
QQVIPHVYPV AAKTQLGRCF QETIGSQCGK ALPGLSKQED CCGTVGTSWG FNKCQKCPKK
PSYHGYNQMM ECLPGYKRVN NTFCQDINEC QLQGVCPNGE CLNTMGSYRC TCKIGFGPDP
TFSSCVPDPP VISEEKGPCY RLVSSGRQCM HPLSVHLTKQ LCCCSVGKAW GPHCEKCPLP
GTAAFKEICP GGMGYTVSGV HRRRPIHHHV GKGPVFVKPK NTQPVAKSTH PPPLPAKEEP
VEALTFSREH GPGVAEPEVA TAPPEKEIPS LDQEKTKLEP GQPQLSPGIS TIHLHPQFPV
VIEKTSPPVP VEVAPEASTS SASQVIAPTQ VTEINECTVN PDICGAGHCI NLPVRYTCIC
YEGYRFSEQQ RKCVDIDECT QVQHLCSQGR CENTEGSFLC ICPAGFMASE EGTNCIDVDE
CLRPDVCGEG HCVNTVGAFR CEYCDSGYRM TQRGRCEDID ECLNPSTCPD EQCVNSPGSY
QCVPCTEGFR GWNGQCLDVD ECLEPNVCAN GDCSNLEGSY MCSCHKGYTR TPDHKHCRDI
DECQQGNLCV NGQCKNTEGS FRCTCGQGYQ LSAAKDQCED IDECQHRHLC AHGQCRNTEG
SFQCVCDQGY RASGLGDHCE DINECLEDKS VCQRGDCINT AGSYDCTCPD GFQLDDNKTC
QDINECEHPG LCGPQGECLN TEGSFHCVCQ QGFSISADGR TCEDIDECVN NTVCDSHGFC
DNTAGSFRCL CYQGFQAPQD GQGCVDVNEC ELLSGVCGEA FCENVEGSFL CVCADENQEY
SPMTGQCRSR TSTDLDVDVD QPKEEKKECY YNLNDASLCD NVLAPNVTKQ ECCCTSGVGW
GDNCEIFPCP VLGTAEFTEM CPKGKGFVPA GESSSEAGGE NYKDADECLL FGQEICKNGF
CLNTRPGYEC YCKQGTYYDP VKLQCFDMDE CQDPSSCIDG QCVNTEGSYN CFCTHPMVLD
ASEKRCIRPA ESNEQIEETD VYQDLCWEHL SDEYVCSRPL VGKQTTYTEC CCLYGEAWGM
QCALCPLKDS DDYAQLCNIP VTGRRQPYGR DALVDFSEQY TPEADPYFIQ DRFLNSFEEL
QAEECGILNG CENGRCVRVQ EGYTCDCFDG YHLDTAKMTC VDVNECDELN NRMSLCKNAK
CINTDGSYKC LCLPGYVPSD KPNYCTPLNT ALNLEKDSDL E
