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O08999 (LTBP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Latent-transforming growth factor beta-binding protein 2
Short name=LTBP-2
Gene names
Name:Ltbp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1813 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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).

Subunit structure

Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with SDC4 By similarity. Ref.1

Subcellular location

Secreted By similarity. Note: Localized in nuchal ligament and aorta to the fibrillin-containing, microfibrillar component of elastic fibers By similarity.

Tissue specificity

Expressed in the anterior chamber of the eye. Ref.7

Domain

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

Post-translational modification

Contains hydroxylated asparagine residues By similarity.

Sequence similarities

Belongs to the LTBP family.

Contains 20 EGF-like domains.

Contains 4 TB (TGF-beta binding) domains.

Sequence caution

The sequence AAB61611.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC35229.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 18131778Latent-transforming growth factor beta-binding protein 2
PRO_0000007644

Regions

Domain181 – 21333EGF-like 1
Domain381 – 41333EGF-like 2
Domain536 – 58853TB 1
Domain609 – 64941EGF-like 3; calcium-binding Potential
Domain659 – 71153TB 2
Domain835 – 87743EGF-like 4
Domain878 – 92043EGF-like 5; calcium-binding Potential
Domain921 – 96040EGF-like 6; calcium-binding Potential
Domain961 – 100040EGF-like 7; calcium-binding Potential
Domain1001 – 104141EGF-like 8; calcium-binding Potential
Domain1042 – 108342EGF-like 9; calcium-binding Potential
Domain1084 – 112542EGF-like 10; calcium-binding Potential
Domain1126 – 116641EGF-like 11; calcium-binding Potential
Domain1167 – 120842EGF-like 12; calcium-binding Potential
Domain1209 – 125042EGF-like 13; calcium-binding Potential
Domain1251 – 129444EGF-like 14; calcium-binding Potential
Domain1295 – 133642EGF-like 15; calcium-binding Potential
Domain1337 – 137943EGF-like 16; calcium-binding Potential
Domain1403 – 145553TB 3
Domain1477 – 151943EGF-like 17; calcium-binding Potential
Domain1520 – 155940EGF-like 18; calcium-binding Potential
Domain1576 – 162853TB 4
Domain1725 – 176541EGF-like 19; calcium-binding Potential
Domain1766 – 181045EGF-like 20; calcium-binding Potential
Region94 – 11522Heparin-binding By similarity
Region226 – 24318Heparin-binding By similarity
Region329 – 33911Heparin-binding By similarity
Compositional bias847 – 1364518Cys-rich

Amino acid modifications

Modified residue4911Phosphoserine Ref.6
Glycosylation1751N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation6031N-linked (GlcNAc...) Potential
Glycosylation11611N-linked (GlcNAc...) Potential
Glycosylation13011N-linked (GlcNAc...) Potential
Glycosylation14221N-linked (GlcNAc...) Potential
Glycosylation15601N-linked (GlcNAc...) Potential
Disulfide bond185 ↔ 195 By similarity
Disulfide bond189 ↔ 201 By similarity
Disulfide bond203 ↔ 212 By similarity
Disulfide bond385 ↔ 395 By similarity
Disulfide bond389 ↔ 401 By similarity
Disulfide bond403 ↔ 412 By similarity
Disulfide bond613 ↔ 624 By similarity
Disulfide bond619 ↔ 633 By similarity
Disulfide bond635 ↔ 648 By similarity
Disulfide bond839 ↔ 852 By similarity
Disulfide bond847 ↔ 861 By similarity
Disulfide bond863 ↔ 876 By similarity
Disulfide bond882 ↔ 893 By similarity
Disulfide bond887 ↔ 902 By similarity
Disulfide bond904 ↔ 919 By similarity
Disulfide bond925 ↔ 936 By similarity
Disulfide bond931 ↔ 945 By similarity
Disulfide bond947 ↔ 959 By similarity
Disulfide bond965 ↔ 976 By similarity
Disulfide bond971 ↔ 985 By similarity
Disulfide bond988 ↔ 999 By similarity
Disulfide bond1005 ↔ 1016 By similarity
Disulfide bond1011 ↔ 1025 By similarity
Disulfide bond1027 ↔ 1040 By similarity
Disulfide bond1046 ↔ 1057 By similarity
Disulfide bond1052 ↔ 1066 By similarity
Disulfide bond1069 ↔ 1082 By similarity
Disulfide bond1088 ↔ 1099 By similarity
Disulfide bond1094 ↔ 1108 By similarity
Disulfide bond1111 ↔ 1124 By similarity
Disulfide bond1130 ↔ 1142 By similarity
Disulfide bond1137 ↔ 1151 By similarity
Disulfide bond1153 ↔ 1165 By similarity
Disulfide bond1171 ↔ 1183 By similarity
Disulfide bond1177 ↔ 1192 By similarity
Disulfide bond1194 ↔ 1207 By similarity
Disulfide bond1213 ↔ 1224 By similarity
Disulfide bond1219 ↔ 1233 By similarity
Disulfide bond1235 ↔ 1249 By similarity
Disulfide bond1255 ↔ 1268 By similarity
Disulfide bond1263 ↔ 1277 By similarity
Disulfide bond1281 ↔ 1293 By similarity
Disulfide bond1299 ↔ 1311 By similarity
Disulfide bond1305 ↔ 1320 By similarity
Disulfide bond1322 ↔ 1335 By similarity
Disulfide bond1341 ↔ 1353 By similarity
Disulfide bond1348 ↔ 1362 By similarity
Disulfide bond1364 ↔ 1378 By similarity
Disulfide bond1481 ↔ 1494 By similarity
Disulfide bond1489 ↔ 1503 By similarity
Disulfide bond1505 ↔ 1518 By similarity
Disulfide bond1524 ↔ 1534 By similarity
Disulfide bond1529 ↔ 1543 By similarity
Disulfide bond1545 ↔ 1558 By similarity
Disulfide bond1729 ↔ 1740 By similarity
Disulfide bond1735 ↔ 1749 By similarity
Disulfide bond1751 ↔ 1764 By similarity
Disulfide bond1770 ↔ 1785 By similarity
Disulfide bond1780 ↔ 1794 By similarity
Disulfide bond1796 ↔ 1809 By similarity

Experimental info

Sequence conflict141Q → R in BAC35229. Ref.2
Sequence conflict741E → G in BAC35229. Ref.2
Sequence conflict971W → R in BAC35229. Ref.2
Sequence conflict4981H → R in BAC35229. Ref.2
Sequence conflict5531S → E in BAC35229. Ref.2
Sequence conflict580 – 5823Missing in BAC35229. Ref.2
Sequence conflict7781D → L in BAC35229. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O08999 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: D993DF6489AA27D5

FASTA1,813195,829
        10         20         30         40         50         60 
MRAPTTARCS GCIQRVRWRG FLPLVLAVLM GTSHAQRDSI GRYEPASRDA NRLWHPVGSH 

        70         80         90        100        110        120 
PAAAAAKVYS LFREPDAPVP GLSPSEWNQP AQGNPGWLAE AEARRPPRTQ QLRRVQPPVQ 

       130        140        150        160        170        180 
TRRSHPRGQQ QIAARAAPSV ARLETPQRPA AARRGRLTGR NVCGGQCCPG WTTSNSTNHC 

       190        200        210        220        230        240 
IKPVCQPPCQ NRGSCSRPQV CICRSGFRGA RCEEVIPEEE FDPQNARPVP RRSVERAPGP 

       250        260        270        280        290        300 
HRSSEARGSL VTRIQPLVPP PSPPPSRRLS QPWPLQQHSG PSRTVRRYPA TGANGQLMSN 

       310        320        330        340        350        360 
ALPSGLELRD SSPQAAHVNH LSPPWGLNLT EKIKKIKVVF TPTICKQTCA RGRCANSCEK 

       370        380        390        400        410        420 
GDTTTLYSQG GHGHDPKSGF RIYFCQIPCL NGGRCIGRDE CWCPANSTGK FCHLPVPQPD 

       430        440        450        460        470        480 
REPAGRGSRH RTLLEGPLKQ STFTLPLSNQ LASVNPSLVK VQIHHPPEAS VQIHQVARVR 

       490        500        510        520        530        540 
GELDPVLEDN SVETRASHRP HGNLGHSPWA SNSIPARAGE APRPPPVLSR HYGLLGQCYL 

       550        560        570        580        590        600 
STVNGQCANP LGSLTSQEDC CGSVGTFWGV TSCAPCPPRQ EGPAFPVIEN GQLECPQGYK 

       610        620        630        640        650        660 
RLNLSHCQDI NECLTLGLCK DSECVNTRGS YLCTCRPGLM LDPSRSRCVS DKAVSMQQGL 

       670        680        690        700        710        720 
CYRSLGSGTC TLPLVHRITK QICCCSRVGK AWGSTCEQCP LPGTEAFREI CPAGHGYTYS 

       730        740        750        760        770        780 
SSDIRLSMRK AEEEELASPL REQTEQSTAP PPGQAERQPL RAATATWIEA ETLPDKGDSR 

       790        800        810        820        830        840 
AVQITTSAPH LPARVPGDAT GRPAPSLPGQ GIPESPAEEQ VIPSSDVLVT HSPPDFDPCF 

       850        860        870        880        890        900 
AGASNICGPG TCVSLPNGYR CVCSPGYQLH PSQDYCTDDN ECMRNPCEGR GRCVNSVGSY 

       910        920        930        940        950        960 
SCLCYPGYTL VTLGDTQECQ DIDECEQPGV CSGGRCSNTE GSYHCECDRG YIMVRKGHCQ 

       970        980        990       1000       1010       1020 
DINECRHPGT CPDGRCVNSP GSYTCLACEE GYVGQSGSCV DVNECLTPGI CTHGRCINME 

      1030       1040       1050       1060       1070       1080 
GSFRCSCEPG YEVTPDKKGC RDVDECASRA SCPTGLCLNT EGSFTCSACQ SGYWVNEDGT 

      1090       1100       1110       1120       1130       1140 
ACEDLDECAF PGVCPTGVCT NTVGSFSCKD CDQGYRPNPL GNRCEDVDEC EGPQSSCRGG 

      1150       1160       1170       1180       1190       1200 
ECKNTEGSYQ CLCHQGFQLV NGTMCEDVNE CVGEEHCAPH GECLNSLGSF FCLCAPGFAS 

      1210       1220       1230       1240       1250       1260 
AEGGTRCQDV DECAATDPCP GGHCVNTEGS FSCLCETASF QPSPDSGECL DIDECEDRED 

      1270       1280       1290       1300       1310       1320 
PVCGAWRCEN SPGSYRCILD CQPGFYVAPN GDCIDIDECA NDTVCGNHGF CDNTDGSFRC 

      1330       1340       1350       1360       1370       1380 
LCDQGFETSP SGWECVDVNE CELMMAVCGD ALCENVEGSF LCLCASDLEE YDAEEGHCRP 

      1390       1400       1410       1420       1430       1440 
RVAGAQRIPE VRTEDQAPSL IRMECYSEHN GGPPCSQILG QNSTQAECCC TQGARWGKAC 

      1450       1460       1470       1480       1490       1500 
APCPSEDSVE FSQLCPSGQG YIPVEGAWTF GQTMYTDADE CVLFGPALCQ NGRCSNIVPG 

      1510       1520       1530       1540       1550       1560 
YICLCNPGYH YDASSRKCQD HNECQDLACE NGECVNQEGS FHCLCNPPLT LDLSGQRCVN 

      1570       1580       1590       1600       1610       1620 
TTSSTEDFPD HDIHMDICWK KVTNDVCSQP LRGHHTTYTE CCCQDGEAWS QQCALCPPRS 

      1630       1640       1650       1660       1670       1680 
SEVYAQLCNV ARIEAERGAG IHFRPGYEYG PGLDDLPENL YGPDGAPFYN YLGPEDTAPE 

      1690       1700       1710       1720       1730       1740 
PPFSNPASQP GDNTPVLEPP LQPSELQPHY LASHSEPPAS FEGLQAEECG ILNGCENGRC 

      1750       1760       1770       1780       1790       1800 
VRVREGYTCD CFEGFQLDAP TLACVDVNEC EDLNGPARLC AHGHCENTEG SYRCHCSPGY 

      1810 
VAEPGPPHCA AKE

« Hide

References

« Hide 'large scale' references
[1]"8-cysteine TGF-BP structural motifs are the site of covalent binding between mouse LTBP-3, LTBP-2, and latent TGF-beta 1."
Yin W., Fang J., Smiley E., Bonadio J.
Biochim. Biophys. Acta 1383:340-350(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TGFB1.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-778.
Strain: C57BL/6J.
Tissue: Head.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 205-211, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"Latent transforming growth factor-beta binding proteins (LTBPs) --structural extracellular matrix proteins for targeting TGF-beta action."
Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.
Cytokine Growth Factor Rev. 10:99-117(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[5]"The latent transforming growth factor beta binding protein (LTBP) family."
Oklu R., Hesketh R.
Biochem. J. 352:601-610(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, MASS SPECTROMETRY.
Tissue: Melanoma.
[7]"Null mutations in LTBP2 cause primary congenital glaucoma."
Ali M., McKibbin M., Booth A., Parry D.A., Jain P., Riazuddin S.A., Hejtmancik J.F., Khan S.N., Firasat S., Shires M., Gilmour D.F., Towns K., Murphy A.L., Azmanov D., Tournev I., Cherninkova S., Jafri H., Raashid Y. expand/collapse author list , Toomes C., Craig J., Mackey D.A., Kalaydjieva L., Riazuddin S., Inglehearn C.F.
Am. J. Hum. Genet. 84:664-671(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF004874 mRNA. Translation: AAB61611.1. Different initiation.
AK052980 mRNA. Translation: BAC35229.1. Different initiation.
IPIIPI00874393.
RefSeqNP_038617.3. NM_013589.3.
UniGeneMm.3900.

3D structure databases

ProteinModelPortalO08999.
SMRO08999. Positions 146-215, 536-717, 854-1558, 1727-1811.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4100636.

PTM databases

PhosphoSiteO08999.

Proteomic databases

PaxDbO08999.
PRIDEO08999.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID16997.
KEGGmmu:16997.

Organism-specific databases

CTD4053.
MGIMGI:99502. Ltbp2.

Phylogenomic databases

eggNOGNOG318792.
HOGENOMHOG000293153.
HOVERGENHBG052370.
InParanoidO08999.
KOK08023.

Gene expression databases

GenevestigatorO08999.
GermOnlineENSMUSG00000002020. Mus musculus.

Family and domain databases

Gene3D3.90.290.10. 5 hits.
InterProIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF07645. EGF_CA. 15 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTSM00181. EGF. 4 hits.
SM00179. EGF_CA. 16 hits.
[Graphical view]
SUPFAMSSF57581. Fibril-assoc. 4 hits.
SSF57184. Grow_fac_recept. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00010. ASX_HYDROXYL. 12 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 10 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 16 hits.
PS51364. TB. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLTBP2. mouse.
NextBio291100.
SOURCESearch...

Entry information

Entry nameLTBP2_MOUSE
AccessionPrimary (citable) accession number: O08999
Secondary accession number(s): Q8C6W9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: May 29, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents