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Protein

Latent-transforming growth factor beta-binding protein 2

Gene

LTBP2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play an integral structural role in elastic-fiber architectural organization and/or assembly. May be involved in the assembly, secretion and targeting of TGF- beta to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGF-beta. May have a structural role in the extra cellular matrix (ECM) (By similarity).By similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • heparin binding Source: UniProtKB-KW
  • microfibril binding Source: AgBase
Complete GO annotation...

Keywords - Ligandi

Growth factor binding, Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Latent-transforming growth factor beta-binding protein 2
Short name:
LTBP-2
Gene namesi
Name:LTBP2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • elastic fiber Source: AgBase
  • microfibril Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35By similarityAdd BLAST35
ChainiPRO_000000764236 – 1842Latent-transforming growth factor beta-binding protein 2Add BLAST1807

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi175N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi185 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 201PROSITE-ProRule annotation
Disulfide bondi203 ↔ 212PROSITE-ProRule annotation
Glycosylationi331N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi388 ↔ 398PROSITE-ProRule annotation
Disulfide bondi392 ↔ 404PROSITE-ProRule annotation
Disulfide bondi406 ↔ 415PROSITE-ProRule annotation
Glycosylationi409N-linked (GlcNAc...)Sequence analysis1
Modified residuei494PhosphoserineBy similarity1
Disulfide bondi542 ↔ 564PROSITE-ProRule annotation
Disulfide bondi551 ↔ 577PROSITE-ProRule annotation
Disulfide bondi565 ↔ 580PROSITE-ProRule annotation
Glycosylationi604N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi614 ↔ 625PROSITE-ProRule annotation
Disulfide bondi620 ↔ 634PROSITE-ProRule annotation
Disulfide bondi636 ↔ 649PROSITE-ProRule annotation
Disulfide bondi662 ↔ 684PROSITE-ProRule annotation
Disulfide bondi671 ↔ 697PROSITE-ProRule annotation
Disulfide bondi685 ↔ 700PROSITE-ProRule annotation
Disulfide bondi686 ↔ 712PROSITE-ProRule annotation
Glycosylationi749N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi840 ↔ 853PROSITE-ProRule annotation
Disulfide bondi848 ↔ 862PROSITE-ProRule annotation
Disulfide bondi864 ↔ 877PROSITE-ProRule annotation
Disulfide bondi883 ↔ 894PROSITE-ProRule annotation
Disulfide bondi888 ↔ 903PROSITE-ProRule annotation
Disulfide bondi905 ↔ 920PROSITE-ProRule annotation
Disulfide bondi926 ↔ 937PROSITE-ProRule annotation
Disulfide bondi932 ↔ 946PROSITE-ProRule annotation
Disulfide bondi948 ↔ 960PROSITE-ProRule annotation
Disulfide bondi966 ↔ 977PROSITE-ProRule annotation
Disulfide bondi972 ↔ 986PROSITE-ProRule annotation
Disulfide bondi989 ↔ 1000PROSITE-ProRule annotation
Disulfide bondi1006 ↔ 1017PROSITE-ProRule annotation
Disulfide bondi1012 ↔ 1026PROSITE-ProRule annotation
Disulfide bondi1028 ↔ 1041PROSITE-ProRule annotation
Disulfide bondi1047 ↔ 1058PROSITE-ProRule annotation
Disulfide bondi1053 ↔ 1067PROSITE-ProRule annotation
Disulfide bondi1070 ↔ 1083PROSITE-ProRule annotation
Disulfide bondi1089 ↔ 1100PROSITE-ProRule annotation
Disulfide bondi1095 ↔ 1109PROSITE-ProRule annotation
Disulfide bondi1112 ↔ 1125PROSITE-ProRule annotation
Disulfide bondi1131 ↔ 1143PROSITE-ProRule annotation
Disulfide bondi1138 ↔ 1152PROSITE-ProRule annotation
Disulfide bondi1154 ↔ 1166PROSITE-ProRule annotation
Glycosylationi1162N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1172 ↔ 1184PROSITE-ProRule annotation
Disulfide bondi1178 ↔ 1193PROSITE-ProRule annotation
Disulfide bondi1195 ↔ 1208PROSITE-ProRule annotation
Disulfide bondi1214 ↔ 1225PROSITE-ProRule annotation
Disulfide bondi1220 ↔ 1234PROSITE-ProRule annotation
Disulfide bondi1236 ↔ 1249PROSITE-ProRule annotation
Disulfide bondi1255 ↔ 1268PROSITE-ProRule annotation
Disulfide bondi1263 ↔ 1277PROSITE-ProRule annotation
Disulfide bondi1281 ↔ 1293PROSITE-ProRule annotation
Disulfide bondi1299 ↔ 1311PROSITE-ProRule annotation
Glycosylationi1301N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1305 ↔ 1320PROSITE-ProRule annotation
Disulfide bondi1322 ↔ 1335PROSITE-ProRule annotation
Disulfide bondi1341 ↔ 1353PROSITE-ProRule annotation
Disulfide bondi1348 ↔ 1362PROSITE-ProRule annotation
Disulfide bondi1364 ↔ 1378PROSITE-ProRule annotation
Disulfide bondi1405 ↔ 1428PROSITE-ProRule annotation
Disulfide bondi1415 ↔ 1440PROSITE-ProRule annotation
Glycosylationi1422N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1429 ↔ 1443PROSITE-ProRule annotation
Disulfide bondi1430 ↔ 1455PROSITE-ProRule annotation
Disulfide bondi1481 ↔ 1494PROSITE-ProRule annotation
Disulfide bondi1489 ↔ 1503PROSITE-ProRule annotation
Disulfide bondi1505 ↔ 1518PROSITE-ProRule annotation
Disulfide bondi1524 ↔ 1534PROSITE-ProRule annotation
Disulfide bondi1529 ↔ 1543PROSITE-ProRule annotation
Disulfide bondi1545 ↔ 1558PROSITE-ProRule annotation
Glycosylationi1560N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1578 ↔ 1601PROSITE-ProRule annotation
Disulfide bondi1587 ↔ 1613PROSITE-ProRule annotation
Disulfide bondi1602 ↔ 1616PROSITE-ProRule annotation
Disulfide bondi1603 ↔ 1628PROSITE-ProRule annotation
Disulfide bondi1758 ↔ 1769PROSITE-ProRule annotation
Disulfide bondi1764 ↔ 1778PROSITE-ProRule annotation
Disulfide bondi1780 ↔ 1793PROSITE-ProRule annotation
Disulfide bondi1799 ↔ 1814PROSITE-ProRule annotation
Disulfide bondi1809 ↔ 1823PROSITE-ProRule annotation
Disulfide bondi1825 ↔ 1838PROSITE-ProRule annotation

Post-translational modificationi

Contains hydroxylated asparagine residues.By similarity
N-Glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiQ28019.
PRIDEiQ28019.

Expressioni

Tissue specificityi

Localized in nuchal ligament and aorta to the fibrillin-containing, microfibrillar component of elastic fibers (at protein level).1 Publication

Interactioni

Subunit structurei

Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with SDC4. Interacts (via C-terminal domain) with FBN1 (via N-terminal domain) in a Ca(+2)-dependent manner.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000029274.

Structurei

3D structure databases

ProteinModelPortaliQ28019.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini181 – 213EGF-like 1PROSITE-ProRule annotationAdd BLAST33
Domaini384 – 416EGF-like 2PROSITE-ProRule annotationAdd BLAST33
Domaini540 – 592TB 1PROSITE-ProRule annotationAdd BLAST53
Domaini610 – 650EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini660 – 712TB 2PROSITE-ProRule annotationAdd BLAST53
Domaini836 – 878EGF-like 4PROSITE-ProRule annotationAdd BLAST43
Domaini879 – 921EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini922 – 961EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini962 – 1001EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1002 – 1042EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1043 – 1084EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1085 – 1126EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1127 – 1167EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1168 – 1209EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1210 – 1250EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1251 – 1294EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini1295 – 1336EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1337 – 1379EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1403 – 1455TB 3PROSITE-ProRule annotationAdd BLAST53
Domaini1477 – 1519EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1520 – 1559EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1576 – 1628TB 4PROSITE-ProRule annotationAdd BLAST53
Domaini1754 – 1794EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1795 – 1839EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 114Heparin-bindingBy similarityAdd BLAST22
Regioni226 – 243Heparin-bindingBy similarityAdd BLAST18
Regioni332 – 342Heparin-bindingBy similarityAdd BLAST11
Regioni1631 – 1842C-terminal domainBy similarityAdd BLAST212

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi363 – 365Cell attachment siteSequence analysis3

Domaini

Associates covalently with small latent TGF-beta complex via Repeat B and Repeat C.By similarity

Sequence similaritiesi

Belongs to the LTBP family.Curated
Contains 20 EGF-like domains.PROSITE-ProRule annotation
Contains 4 TB (TGF-beta binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ28019.
KOiK08023.

Family and domain databases

Gene3Di3.90.290.10. 4 hits.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF07645. EGF_CA. 16 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 20 hits.
SM00179. EGF_CA. 18 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57581. SSF57581. 5 hits.
PROSITEiPS00010. ASX_HYDROXYL. 13 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 16 hits.
PS51364. TB. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q28019-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPPTTARCP GRVLQNPWRS FWPLTLALFV GMGQAQRDPV GRYEPAGRDA
60 70 80 90 100
SRLRRPGGSP VVATAKVYSL FREQDAPVRG SPPAELVQPS WGSPRRSTEA
110 120 130 140 150
EARRPPRAQQ PRRVQPPAQT WRSRPSGQQQ SAPRARAAPA LPRLETVQRP
160 170 180 190 200
RAARGRLTGR NVCGGQCCPG WTTANSTNHC IKPVCQPPCQ NRGSCSRPQL
210 220 230 240 250
CVCRSGFRGA RCEEVIPEEE FDPQNSRPAP RRSAEGPPSL RRSSVAREST
260 270 280 290 300
TARVRPPAPQ LQRARTLSGL SQTRSSQQHV GLSQTTRLYP APAASGQLTS
310 320 330 340 350
NALPMGPGPE RRDGAPQAAY LDRPSSSWGL NLTEKIKKIK IVFTPTICKQ
360 370 380 390 400
TCARGRCANS CERGDTTTLY SQSGHGHDPK SGFRIYFCQI PCLNGGRCIG
410 420 430 440 450
RDECWCPANS TGKFCHLPAP RLDQEPPERG PRHRAPLEGP LKQSTFTLPL
460 470 480 490 500
SNQLASVNPS LVNVHIRHPP EASVQIHQVA RVRGEAEEAP EENSVETRPS
510 520 530 540 550
PRLPAGPGPG RWDSNRIPAR SGEAPRLPPP VVPRTPALLG RCYLSTLNGQ
560 570 580 590 600
CANPLPELTA HEDCCGSVGA FWGVTSCAPC PPRPASPVIE NGQLECPQGY
610 620 630 640 650
KRLNLTHCED VNECLTLGLC EDSECVNTRG SYLCTCRPGL LLDPSRSRCV
660 670 680 690 700
SDKAVSMQQG LCYRLLGPGT CALPLAQRIT KQICCCSRVG KAWGSLCEKC
710 720 730 740 750
PLPGTEAFRE ICPAGHGYTY SSSDIRLSMR KAEEEELARP SRDRGPKRNG
760 770 780 790 800
TLPRPAERQP LRAATGTWVE AETIPDKGDS QASQVTTSVT QLSTWVPGGA
810 820 830 840 850
LGTPTPSVPE QGIPEAREEA QVTAPTNVLV TPAPSGIDRC AAGATNICGP
860 870 880 890 900
GTCVNLPDGY RCICSPGYRL HPSQAYCTDD NECLRDPCKG RGRCVNRVGS
910 920 930 940 950
YSCFCYPGYK LATSGATQEC QDIDECEQPG VCSRGRCTNT EGSYHCECDQ
960 970 980 990 1000
GYIMVRKGHC QDINECRHPG TCPDGKCVNS PGSYTCLPCE EGYRGQGGSC
1010 1020 1030 1040 1050
VDVNECLTPG VCTHGTCINL EGSFRCSCEQ GYEVTPDEKG CKDVDECAIR
1060 1070 1080 1090 1100
ASCPTGLCLN TEGSFTCSAC ESGYWVNEDG TACEDLDECA FPGVCPSGVC
1110 1120 1130 1140 1150
TNTAGSFSCR DCEAGYQPSA LGHTCEDVDE CEDPQSSCLG GECKNTAGSY
1160 1170 1180 1190 1200
QCLCPPGFQL ANGTVCEDVD ECVGEEYCAP RGECLNSHGS FFCLCADGFV
1210 1220 1230 1240 1250
SADGGTSCQD VDECAVTDRC VGGQCVNTDG SFNCVCETGF QPSPESGECV
1260 1270 1280 1290 1300
DIDECEDLGE PICGAWRCEN SPGSYRCVLG CQPGFHMAPT GDCIDIDECA
1310 1320 1330 1340 1350
NDTVCGSHGF CDNTDGAFRC LCDQGFETSP SGWDCVDVNE CELMLAVCGA
1360 1370 1380 1390 1400
ALCENVEGSF LCLCASDLEE YDAQEGRCRP RGAGGPSVPE ARPGAHPPGP
1410 1420 1430 1440 1450
VRMECYSGQK DQTPCSSLLG RNTTQAECCC TQGTGWGDAC DLCPDEDSVE
1460 1470 1480 1490 1500
FSEICPSGKG YIPVEGAWMF GQTTYTDADE CVMFGPGLCR NGRCLNTVPG
1510 1520 1530 1540 1550
YICLCNPGYH YNAASRKCED HDECQDMACE NGECVNTEGS FHCFCSPPLT
1560 1570 1580 1590 1600
LDLSQQRCVN STSGVEDLPD HDIHMDICWK RVTNYVCSHP LHGRRTTYTE
1610 1620 1630 1640 1650
CCCQDGEAWS QQCALCPPRS SEVYAQLCNV ARIEAEREAG IHFRPGYEYS
1660 1670 1680 1690 1700
PGPDDLHYSL YGPDGVPFYN YLGPEDAIPE PLFPSTAGRP GDRIPLPEPP
1710 1720 1730 1740 1750
LQPSELQPHY VASHPGLCCC KNGEEVGSEA VSLPSSPSAH HCQQEHQAGF
1760 1770 1780 1790 1800
EGLQAEECGI LNGCENGRCV RVREGYTCDC FEGFQLDTAH MACVDVNECD
1810 1820 1830 1840
DLNGPAALCV HGHCDNTEGS YRCHCLPGYV AEAGPPHCTA KE
Length:1,842
Mass (Da):198,410
Last modified:January 16, 2004 - v2
Checksum:i5C06161EA29AB6AA
GO

Sequence cautioni

The sequence AAA91455 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35363 mRNA. Translation: AAA91455.1. Different initiation.
RefSeqiNP_776810.1. NM_174385.2.
UniGeneiBt.5011.

Genome annotation databases

GeneIDi281905.
KEGGibta:281905.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35363 mRNA. Translation: AAA91455.1. Different initiation.
RefSeqiNP_776810.1. NM_174385.2.
UniGeneiBt.5011.

3D structure databases

ProteinModelPortaliQ28019.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000029274.

Proteomic databases

PaxDbiQ28019.
PRIDEiQ28019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281905.
KEGGibta:281905.

Organism-specific databases

CTDi4053.

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ28019.
KOiK08023.

Family and domain databases

Gene3Di3.90.290.10. 4 hits.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF07645. EGF_CA. 16 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 20 hits.
SM00179. EGF_CA. 18 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57581. SSF57581. 5 hits.
PROSITEiPS00010. ASX_HYDROXYL. 13 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 16 hits.
PS51364. TB. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLTBP2_BOVIN
AccessioniPrimary (citable) accession number: Q28019
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: November 2, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.