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UniProtKB - Q00918 (LTBP1_RAT)

Entry version 156 (10 Feb 2021)
Sequence version 1 (01 Jul 1993)
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Protein

Latent-transforming growth factor beta-binding protein 1

Gene

Ltbp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:7593177). Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta (By similarity). Outcompeted by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta (By similarity).By similarity1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGrowth factor binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-2129379, Molecules associated with elastic fibres
R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-RNO-8957275, Post-translational protein phosphorylation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Latent-transforming growth factor beta-binding protein 1
Short name:
LTBP-1
Alternative name(s):
Transforming growth factor beta-1-binding protein 1
Short name:
TGF-beta-1-BP-1
Transforming growth factor beta-1-masking protein large subunit
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ltbp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		68379, Ltbp1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000044555521 – 1712Latent-transforming growth factor beta-binding protein 1Add BLAST1692

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi185 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 201PROSITE-ProRule annotation
Disulfide bondi203 ↔ 212PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi339N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi370N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi395 ↔ 405PROSITE-ProRule annotation
Disulfide bondi399 ↔ 411PROSITE-ProRule annotation
Disulfide bondi413 ↔ 422PROSITE-ProRule annotation
Glycosylationi416N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi551 ↔ 573PROSITE-ProRule annotation
Disulfide bondi560 ↔ 586PROSITE-ProRule annotation
Disulfide bondi574 ↔ 589PROSITE-ProRule annotation
Glycosylationi612N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi622 ↔ 633PROSITE-ProRule annotation
Disulfide bondi628 ↔ 642PROSITE-ProRule annotation
Disulfide bondi644 ↔ 657PROSITE-ProRule annotation
Disulfide bondi671 ↔ 694PROSITE-ProRule annotation
Disulfide bondi681 ↔ 706PROSITE-ProRule annotation
Disulfide bondi695 ↔ 709PROSITE-ProRule annotation
Disulfide bondi696 ↔ 721PROSITE-ProRule annotation
Disulfide bondi869 ↔ 881PROSITE-ProRule annotation
Disulfide bondi876 ↔ 890PROSITE-ProRule annotation
Disulfide bondi892 ↔ 905PROSITE-ProRule annotation
Disulfide bondi911 ↔ 923PROSITE-ProRule annotation
Disulfide bondi918 ↔ 932PROSITE-ProRule annotation
Disulfide bondi934 ↔ 947PROSITE-ProRule annotation
Disulfide bondi953 ↔ 964PROSITE-ProRule annotation
Disulfide bondi959 ↔ 973PROSITE-ProRule annotation
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei966(3R)-3-hydroxyasparagineBy similarity1
Disulfide bondi976 ↔ 988PROSITE-ProRule annotation
Disulfide bondi994 ↔ 1005PROSITE-ProRule annotation
Disulfide bondi1000 ↔ 1014PROSITE-ProRule annotation
Disulfide bondi1017 ↔ 1028PROSITE-ProRule annotation
Disulfide bondi1034 ↔ 1045PROSITE-ProRule annotation
Disulfide bondi1040 ↔ 1054PROSITE-ProRule annotation
Glycosylationi1042N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1056 ↔ 1069PROSITE-ProRule annotation
Disulfide bondi1075 ↔ 1086PROSITE-ProRule annotation
Disulfide bondi1081 ↔ 1095PROSITE-ProRule annotation
Disulfide bondi1097 ↔ 1110PROSITE-ProRule annotation
Disulfide bondi1116 ↔ 1127PROSITE-ProRule annotation
Disulfide bondi1122 ↔ 1136PROSITE-ProRule annotation
Modified residuei1129(3R)-3-hydroxyasparagineBy similarity1
Disulfide bondi1138 ↔ 1151PROSITE-ProRule annotation
Disulfide bondi1157 ↔ 1169PROSITE-ProRule annotation
Disulfide bondi1164 ↔ 1178PROSITE-ProRule annotation
Disulfide bondi1180 ↔ 1192PROSITE-ProRule annotation
Disulfide bondi1198 ↔ 1210PROSITE-ProRule annotation
Disulfide bondi1204 ↔ 1219PROSITE-ProRule annotation
Disulfide bondi1221 ↔ 1234PROSITE-ProRule annotation
Disulfide bondi1240 ↔ 1252PROSITE-ProRule annotation
Glycosylationi1242N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1246 ↔ 1261PROSITE-ProRule annotation
Disulfide bondi1263 ↔ 1276PROSITE-ProRule annotation
Disulfide bondi1282 ↔ 1294PROSITE-ProRule annotation
Disulfide bondi1289 ↔ 1303PROSITE-ProRule annotation
Disulfide bondi1305 ↔ 1319PROSITE-ProRule annotation
Disulfide bondi1340 ↔ 1363PROSITE-ProRule annotation
Disulfide bondi1350 ↔ 1375PROSITE-ProRule annotation
Disulfide bondi1350Interchain (with C-33 in TGFB1); in linked formBy similarity
Glycosylationi1357N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi1364 ↔ 1380PROSITE-ProRule annotation
Disulfide bondi1365 ↔ 1392PROSITE-ProRule annotation
Disulfide bondi1375Interchain (with C-33 in TGFB1); in linked formBy similarity
Modified residuei1405PhosphoserineBy similarity1
Disulfide bondi1419 ↔ 1432PROSITE-ProRule annotation
Disulfide bondi1427 ↔ 1441PROSITE-ProRule annotation
Disulfide bondi1443 ↔ 1456PROSITE-ProRule annotation
Disulfide bondi1462 ↔ 1473PROSITE-ProRule annotation
Disulfide bondi1468 ↔ 1482PROSITE-ProRule annotation
Disulfide bondi1484 ↔ 1497PROSITE-ProRule annotation
Disulfide bondi1517 ↔ 1541PROSITE-ProRule annotation
Disulfide bondi1527 ↔ 1553PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1556PROSITE-ProRule annotation
Disulfide bondi1543 ↔ 1568PROSITE-ProRule annotation
Modified residuei1588PhosphoserineBy similarity1
Modified residuei1607PhosphoserineBy similarity1
Disulfide bondi1616 ↔ 1627PROSITE-ProRule annotation
Disulfide bondi1622 ↔ 1636PROSITE-ProRule annotation
Disulfide bondi1638 ↔ 1651PROSITE-ProRule annotation
Disulfide bondi1657 ↔ 1672PROSITE-ProRule annotation
Disulfide bondi1667 ↔ 1681PROSITE-ProRule annotation
Disulfide bondi1683 ↔ 1696PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Contains hydroxylated asparagine residues.By similarity
Two intrachain disulfide bonds from the TB3 domain are rearranged upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide, anchoring it to the extracellular matrix.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei736 – 737CleavageSequence analysis2
Sitei1577 – 1578CleavageSequence analysis2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q00918

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		Q00918

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q00918, 7 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q00918

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q00918

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with TGFB1; associates via disulfide bonds with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1, leading to regulate activation of TGF-beta-1. LTBP1 does not bind directly to TGF-beta-1, the active chain of TGFB1.

Interacts (via C-terminal domain) with FBN1 (via N-terminal domain).

Interacts with FBN2.

Interacts with ADAMTSL2.

Interacts with EFEMP2 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		Q00918, 1 interactor

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000040099

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q00918

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini181 – 213EGF-like 1PROSITE-ProRule annotationAdd BLAST33
Domaini391 – 423EGF-like 2PROSITE-ProRule annotationAdd BLAST33
Domaini549 – 601TB 1PROSITE-ProRule annotationAdd BLAST53
Domaini618 – 658EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini669 – 721TB 2PROSITE-ProRule annotationAdd BLAST53
Domaini865 – 906EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini907 – 948EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini949 – 989EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini990 – 1029EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1030 – 1070EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1071 – 1111EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1112 – 1152EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1153 – 1193EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1194 – 1235EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1236 – 1277EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1278 – 1320EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1338 – 1392TB 3PROSITE-ProRule annotationAdd BLAST55
Domaini1415 – 1457EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1458 – 1498EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1515 – 1568TB 4PROSITE-ProRule annotationAdd BLAST54
Domaini1612 – 1652EGF-like 17PROSITE-ProRule annotationAdd BLAST41
Domaini1653 – 1697EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1335 – 14028-Cys3 regionBy similarityAdd BLAST68
Regioni1498 – 1712C-terminal domainBy similarityAdd BLAST215

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi96 – 124Pro-richAdd BLAST29

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The 8-Cys3 region in the third TB domain mediates the interchain disulfide bond interaction with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the LTBP family.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1217, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q00918

Database of Orthologous Groups

More...OrthoDBi		1174178at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q00918

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.290.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR026823, cEGF
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR017878, TB_dom
IPR036773, TB_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12662, cEGF, 1 hit
PF07645, EGF_CA, 13 hits
PF00683, TB, 4 hits

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00181, EGF, 18 hits
SM00179, EGF_CA, 16 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57184, SSF57184, 4 hits
SSF57581, SSF57581, 4 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00010, ASX_HYDROXYL, 13 hits
PS00022, EGF_1, 2 hits
PS01186, EGF_2, 10 hits
PS50026, EGF_3, 14 hits
PS01187, EGF_CA, 15 hits
PS51364, TB, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q00918-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGAWLRWGL LLWAGLLAWS AHGRVRRITY VVRPGPGLPA GTLPLAGPPR 
        60         70         80         90        100
TFNVALDARY SRSSTATSSR SLAGPPAERT RRTSQPGGAA LPGLRSPLPP 
       110        120        130        140        150
EPARPGAPSR QLHSKAGAQT AVTRFAKHGR QVVRSKVQQD TQSSGGSRLQ 
       160        170        180        190        200
VQQKQQLQGI NVCGGQCCHG WSKAPGSQRC TKPSCVPPCQ NGGMCLRPQF 
       210        220        230        240        250
CVCKPGTKGK ACEITAAQDT MSPVFGGQNP GSSWVPPEPA AKRTSTKKAD 
       260        270        280        290        300
TLPRVSPVAQ MTLTLKPKPS MGLSQQIHSQ VAPLSSQNVM IRHGQTQEYV 
       310        320        330        340        350
LKPKYFPAPK VVSGEQSTEG SFSLRYGQEQ GTAPFQVSNH TGRIKVVFTP 
       360        370        380        390        400
SICKVTCTKG NCHNSCQKGN TTTLISENGH AADTLTATNF RVVICHLPCM 
       410        420        430        440        450
NGGQCSSRDK CQCPPNFTGK LCQIPVLGAS MPKLYQHAQQ PGKALGSHVI 
       460        470        480        490        500
HSTHTLPLTM TNQQGVKVKF PPNIVNIHVK HPPEASVQIH QVSRIDGPVG 
       510        520        530        540        550
QRVKEVQPGQ SQVSYQGLPV QKTQTVHSTY SHQQVIPHVY PVAAKTQLGR 
       560        570        580        590        600
CFQETIGSQC GKALPGLSKQ EDCCGTVGTS WGFNKCQKCP KKQSYHGYTQ 
       610        620        630        640        650
MMECLQGYKR VNNTFCQDIN ECQLQGVCPN GECLNTMGSY RCSCKMGFGP 
       660        670        680        690        700
DPTFSSCVPD PPMISEEKGP CYRLVSPGRQ CMHPLSVHLT KQICCCSVGK 
       710        720        730        740        750
AWGPQCEKCP LPGTAAFKEI CPGGMGYTVS GIHRRRPIHQ HIGKEAVFVK 
       760        770        780        790        800
PKNTQPVAKS THPPPLPAKE EPVEALTSSR EHGPGVAEPE VVTAPPEKEI 
       810        820        830        840        850
PSLDQEKTRL EPGQPQLSPG VSTIHLHPQF PVVVEKTSPP VPVEVAPEGS 
       860        870        880        890        900
TSSASQVIAP TQVTEINECT VNPDICGAGH CINLPVRYTC ICYEGYKFSE 
       910        920        930        940        950
QQRKCIDIDE CAQAQHLCSQ GRCENTEGSF LCICPAGFIA SEEGSNCIDV 
       960        970        980        990       1000
DECLRPDVCR DGRCINTAGA FRCEYCDSGY RMSRRGHCED IDECLTPSTC 
      1010       1020       1030       1040       1050
PEEQCVNSPG SYQCVPCTEG FRGWNGQCLD VDECLQPKVC TNGSCTNLEG 
      1060       1070       1080       1090       1100
SYMCSCHKGY SPTPDHRHCQ DIDECQQGNL CMNGQCKNTD GSFRCTCGQG 
      1110       1120       1130       1140       1150
YQLSAAKDQC EDIDECEHRH LCSHGQCRNT EGSFQCLCNQ GYRASVLGDH 
      1160       1170       1180       1190       1200
CEDINECLED SSVCQGGDCI NTAGSYDCTC PDGLQLNDNK GCQDINECAQ 
      1210       1220       1230       1240       1250
PGLCAPHGEC LNTQGSFHCV CEQGFSISAD GRTCEDIDEC VNNTVCDSHG 
      1260       1270       1280       1290       1300
FCDNTAGSFR CLCYQGFQAP QDGQGCVDVN ECELLSGVCG EAFCENVEGS 
      1310       1320       1330       1340       1350
FLCVCADENQ EYSPMTGQCR SRATEDSGVD RQPKEEKKEC YYNLNDASLC 
      1360       1370       1380       1390       1400
DNVLAPNVTK QECCCTSGAG WGDNCEIFPC PVQGTAEFSE MCPRGKGFVP 
      1410       1420       1430       1440       1450
AGESSYETGG ENYKDADECL LFGEEICKNG YCLNTQPGYE CYCKEGTYYD 
      1460       1470       1480       1490       1500
PVKLQCFDMD ECQDPNSCID GQCVNTEGSY NCFCTHPMVL DASEKRCVQP 
      1510       1520       1530       1540       1550
TESNEQIEET DVYQDLCWEH LSEEYVCSRP LVGKQTTYTE CCCLYGEAWG 
      1560       1570       1580       1590       1600
MQCALCPMKD SDDYAQLCNI PVTGRRRPYG RDALVDFSEQ YGPETDPYFI 
      1610       1620       1630       1640       1650
QDRFLNSFEE LQAEECGILN GCENGRCVRV QEGYTCDCFD GYHLDMAKMT 
      1660       1670       1680       1690       1700
CVDVNECSEL NNRMSLCKNA KCINTEGSYK CVCLPGYVPS DKPNYCTPLN 
      1710 
TALNLDKDSD LE
Length:1,712
Mass (Da):186,599
Last modified:July 1, 1993 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i650BCEAA691FD134
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3ZAA3D3ZAA3_RAT
Latent-transforming growth factor b...
Ltbp1 rCG_61456
1,712Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M55431 mRNA Translation: AAA42235.1

Protein sequence database of the Protein Information Resource

More...PIRi		A38261

NCBI Reference Sequences

More...RefSeqi		NP_067598.1, NM_021587.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		59107

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:59107

UCSC genome browser

More...UCSCi		RGD:68379, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55431 mRNA Translation: AAA42235.1
PIRiA38261
RefSeqiNP_067598.1, NM_021587.1

3D structure databases

SMRiQ00918
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ00918, 1 interactor
STRINGi10116.ENSRNOP00000040099

PTM databases

CarbonylDBiQ00918
GlyGeniQ00918, 7 sites
iPTMnetiQ00918
PhosphoSitePlusiQ00918

Proteomic databases

PaxDbiQ00918

Genome annotation databases

GeneIDi59107
KEGGirno:59107
UCSCiRGD:68379, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4052
RGDi68379, Ltbp1

Phylogenomic databases

eggNOGiKOG1217, Eukaryota
InParanoidiQ00918
OrthoDBi1174178at2759
PhylomeDBiQ00918

Enzyme and pathway databases

ReactomeiR-RNO-2129379, Molecules associated with elastic fibres
R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-RNO-8957275, Post-translational protein phosphorylation

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q00918

Family and domain databases

Gene3Di3.90.290.10, 4 hits
InterProiView protein in InterPro
IPR026823, cEGF
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR017878, TB_dom
IPR036773, TB_dom_sf
PfamiView protein in Pfam
PF12662, cEGF, 1 hit
PF07645, EGF_CA, 13 hits
PF00683, TB, 4 hits
SMARTiView protein in SMART
SM00181, EGF, 18 hits
SM00179, EGF_CA, 16 hits
SUPFAMiSSF57184, SSF57184, 4 hits
SSF57581, SSF57581, 4 hits
PROSITEiView protein in PROSITE
PS00010, ASX_HYDROXYL, 13 hits
PS00022, EGF_1, 2 hits
PS01186, EGF_2, 10 hits
PS50026, EGF_3, 14 hits
PS01187, EGF_CA, 15 hits
PS51364, TB, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLTBP1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q00918
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 10, 2021
This is version 156 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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