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Reviewed, UniProtKB/Swiss-Prot Q61810 (LTBP3_MOUSE)

Last modified June 16, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Latent-transforming growth factor beta-binding protein 3
      Short name=LTBP-3
Gene names
Name: Ltbp3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1268 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May be involved in the assembly, secretion and targeting of TGF- beta1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGF-beta1. May have a structural role in the extra cellular matrix (ECM).

Subunit structure

Forms part of the large latent transforming growth factor beta (TGFB1) precursor complex; removal is essential for activation of complex.

Subcellular location

Secreted. Note: Secretion occurs after coexpression with TGFB1 and requires complexing with 'Cys-33' of the TGFB1 propeptide.

Developmental stage

At 8.5-9.0 dpc highly expressed in liver. Significant expression was also seen in the developing central nervous, somites and cardiovascular tissue. At 13.5-16.5 dpc expression was seen in osteoblasts, respiratory epithelial cells, and nephrons and dermal connective tissue.

Domain

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

Post-translational modification

Contains hydroxylated asparagine residues By similarity.

Sequence similarities

Belongs to the LTBP family.

Contains 13 EGF-like domains.

Contains 3 TB (TGF-beta binding) domains.

Sequence caution

The sequence AAB53015.1 differs from that shown. Reason: Frameshift at positions 6, 38, 56, 155, 158, 160, 480 and 775.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q61810-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q61810-2)

The sequence of this isoform differs from the canonical sequence as follows:
     860-882: KKDIDECSQDPGLCLPHACENLQ → QGMRSWPGILKGEAGQCDLFDTL
     883-1268: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Potential
Chain39 – 12681230Latent-transforming growth factor beta-binding protein 3
PRO_0000007647

Regions

Domain106 – 13833EGF-like 1
Domain274 – 32855TB 1
Domain352 – 39241EGF-like 2; calcium-binding Potential
Domain400 – 45253TB 2
Domain570 – 61142EGF-like 3
Domain612 – 65544EGF-like 4; calcium-binding Potential
Domain656 – 69843EGF-like 5; calcium-binding Potential
Domain740 – 77940EGF-like 6; calcium-binding Potential
Domain780 – 82041EGF-like 7; calcium-binding Potential
Domain821 – 86040EGF-like 8; calcium-binding Potential
Domain862 – 90342EGF-like 9; calcium-binding Potential
Domain912 – 96655TB 3
Domain988 – 103043EGF-like 10; calcium-binding Potential
Domain1031 – 107040EGF-like 11; calcium-binding Potential
Domain1201 – 124646EGF-like 12; calcium-binding Potential
Compositional bias21 – 3212Poly-Leu
Compositional bias47 – 526Poly-Gly
Compositional bias191 – 292102Pro-rich
Compositional bias480 – 55677Pro-rich
Compositional bias574 – 889316Cys-rich

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation3461N-linked (GlcNAc...) Potential
Glycosylation8401N-linked (GlcNAc...) Potential
Glycosylation9311N-linked (GlcNAc...) Potential
Glycosylation12221N-linked (GlcNAc...) Potential
Disulfide bond110 ↔ 120 By similarity
Disulfide bond114 ↔ 126 By similarity
Disulfide bond128 ↔ 137 By similarity
Disulfide bond356 ↔ 367 By similarity
Disulfide bond363 ↔ 376 By similarity
Disulfide bond378 ↔ 391 By similarity
Disulfide bond574 ↔ 586 By similarity
Disulfide bond581 ↔ 595 By similarity
Disulfide bond597 ↔ 610 By similarity
Disulfide bond616 ↔ 628 By similarity
Disulfide bond621 ↔ 637 By similarity
Disulfide bond639 ↔ 654 By similarity
Disulfide bond660 ↔ 672 By similarity
Disulfide bond666 ↔ 681 By similarity
Disulfide bond683 ↔ 697 By similarity
Disulfide bond744 ↔ 755 By similarity
Disulfide bond750 ↔ 764 By similarity
Disulfide bond766 ↔ 778 By similarity
Disulfide bond784 ↔ 795 By similarity
Disulfide bond790 ↔ 804 By similarity
Disulfide bond806 ↔ 819 By similarity
Disulfide bond825 ↔ 836 By similarity
Disulfide bond831 ↔ 845 By similarity
Disulfide bond847 ↔ 859 By similarity
Disulfide bond866 ↔ 878 By similarity
Disulfide bond873 ↔ 887 By similarity
Disulfide bond889 ↔ 902 By similarity
Disulfide bond992 ↔ 1005 By similarity
Disulfide bond1000 ↔ 1014 By similarity
Disulfide bond1016 ↔ 1029 By similarity
Disulfide bond1035 ↔ 1046 By similarity
Disulfide bond1041 ↔ 1055 By similarity
Disulfide bond1057 ↔ 1070 By similarity
Disulfide bond1205 ↔ 1220 By similarity
Disulfide bond1215 ↔ 1229 By similarity
Disulfide bond1231 ↔ 1245 By similarity

Natural variations

Alternative sequence860 – 88223KKDID…CENLQ → QGMRSWPGILKGEAGQCDLF DTL in isoform 2.
VSP_009242
Alternative sequence883 – 1268386Missing in isoform 2.
VSP_009243

Experimental info

Sequence conflict161H → R in AAB53015. Ref.1
Sequence conflict201A → G in AAB53015. Ref.1
Sequence conflict351Missing in AAB53015. Ref.1
Sequence conflict451E → Q in AAB53015. Ref.1
Sequence conflict1041A → G in BAC38053. Ref.2
Sequence conflict1721E → Q in BAC38053. Ref.2
Sequence conflict2631P → Q in BAC38053. Ref.2
Sequence conflict3281V → G in BAC38053. Ref.2
Sequence conflict361 – 3633NVC → MCR in BAC38053. Ref.2
Sequence conflict387 – 3893LAA → SRT in BAC38053. Ref.2
Sequence conflict4531P → PA in BAC38053. Ref.2
Sequence conflict6611A → T in BAC38053. Ref.2
Sequence conflict7681Q → QG in BAC38053. Ref.2
Sequence conflict8491L → Q in BAC38053. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 16, 2004. Version 3.
Checksum: 98F632F249ACB4DD

FASTA1,268135,702
        10         20         30         40         50         60 
MPGPRGAAHG LAPAMHQAGA LGLLALLLLA LLGPGGGAEG GPAGERGTGG GGALARERFK 

        70         80         90        100        110        120 
VVFAPVICKR TCLKGQCRDS CQQGSNMTLI GENGHSTDTL TGSAFRVVVC PLPCMNGGQC 

       130        140        150        160        170        180 
SSRNQCLCPP DFTGRFCQVP AAGTGAGTGS SGPGLARTGA MSTGPLPPLA PEGESVASKH 

       190        200        210        220        230        240 
AIYAVQVIAD PPGPGEGPPA QHAAFLVPLG PGQISAEVQA PPPVVNVRVH HPPEASVQVH 

       250        260        270        280        290        300 
RIEGPNAEGP ASSQHLLPHP KPPHPRPPTQ KPLGRCFQDT LPKQPCGSNP LPGLTKQEDC 

       310        320        330        340        350        360 
CGSIGTAWGQ SKCHKCPQLQ YTGVQKPVPV RGEVGADCPQ GYKRLNSTHC QDINECAMPG 

       370        380        390        400        410        420 
NVCHGDCLNN PGSYRCVCPP GHSLGPLAAQ CIADKPEEKS LCFRLVSTEH QCQHPLTTRL 

       430        440        450        460        470        480 
TRQLCCCSVG KAWGARCQRC PADGTAAFKE ICPGKGYHIL TSHQTLTIQG ESDFSLFLHP 

       490        500        510        520        530        540 
DGPPKPQQLP ESPSRAPPLE DTEEERGVTM DPPVSEERSV QQSHPTTTTS PPRPYPELIS 

       550        560        570        580        590        600 
RPSPPTFHRF LPDLPPSRSA VEIAPTQVTE TDECRLNQNI CGHGQCVPGP SDYSCHCNAG 

       610        620        630        640        650        660 
YRSHPQHRYC VDVNECEAEP CGPGKGICMN TGGSYNCHCN RGYRLHVGAG GRSCVDLNEC 

       670        680        690        700        710        720 
AKPHLCGDGG FCINFPGHYK CNCYPGYRLK ASRPPICEDI DECRDPSTCP DGKCENKPGS 

       730        740        750        760        770        780 
FKCIACQPGY RSQGGGACRD VNECSEGTPC SPGWCENLPG SYRCTCAQYE PAQDGLSCID 

       790        800        810        820        830        840 
VDECEAGKVC QDGICTNTPG SFQCQCLSGY HLSRDRSRCE DIDECDFPAA CIGGDCINTN 

       850        860        870        880        890        900 
GSYRCLCPLG HRLVGGRKCK KDIDECSQDP GLCLPHACEN LQGSYVCVCD EGFTLTQDQH 

       910        920        930        940        950        960 
GCEEVEQPHH KKECYLNFDD TVFCDSVLAT NVTQQECCCS LGAGWGDHCE IYPCPVYSSA 

       970        980        990       1000       1010       1020 
EFHSLVPDGK RLHSGQQHCE LCIPAHRDID ECILFGAEIC KEGKCVNTQP GYECYCKQGF 

      1030       1040       1050       1060       1070       1080 
YYDGNLLECV DVDECLDESN CRNGVCENTR GGYRCACTPP AEYSPAQAQC LIPERWSTPQ 

      1090       1100       1110       1120       1130       1140 
RDVKCAGASE ERTACVWGPW AGPALTFDDC CCRQPRLGTQ CRPCPPRGTG SQCPTSQSES 

      1150       1160       1170       1180       1190       1200 
NSFWDTSPLL LGKSPRDEDS SEEDSDECRC VSGRCVPRPG GAVCECPGGF QLDASRARCV 

      1210       1220       1230       1240       1250       1260 
DIDECRELNQ RGLLCKSERC VNTSGSFRCV CKAGFTRSRP HGPACLSAAA DDAAIAHTSV 


IDHRGYFH 

« Hide

Isoform 2.

Checksum: C5D95F4994A2E776
Show »

FASTA88293,355

References

« Hide 'large scale' references
[1]"Isolation of a novel latent transforming growth factor-beta binding protein gene (LTBP-3)."
Yin W., Smiley E., Germiller J., Mecham R.P., Florer J.B., Wenstrup R.J., Bonadio J.
J. Biol. Chem. 270:10147-10160(1995) [PubMed: 7730318] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Adipose tissue.
[3]"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: 9602168] [Abstract]
Cited for: INTERACTION WITH TGFB1.
[4]"Latent TGF-beta binding protein-3 (LTBP-3) requires binding to TGF-beta for secretion."
Chen Y., Dabovic B., Annes J.P., Rifkin D.B.
FEBS Lett. 517:277-280(2002) [PubMed: 12062452] [Abstract]
Cited for: INTERACTION WITH TGFB1.
[5]"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: 10743502] [Abstract]
Cited for: REVIEW.
[6]"The latent transforming growth factor beta binding protein (LTBP) family."
Oklu R., Hesketh R.
Biochem. J. 352:601-610(2000) [PubMed: 11104663] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

L40459 mRNA. Translation: AAB53015.1. Sequence problems.
AK080869 mRNA. Translation: BAC38053.1.
IPIIPI00407364.
IPI00828508.
PIRA57293.
RefSeqNP_032546.2.
UniGeneMm.182396

3D structure databases

HSSPHSSP built from PDB template 1BF9 based on UniProtKB P08709.
ModBaseSearch...

PTM databases

PhosphoSiteQ61810.

Genome annotation databases

EnsemblENSMUSG00000024940. Mus musculus. [Contig view]
GeneID16998.
KEGGmmu:16998.

Organism-specific databases

MGIMGI:1101355. Ltbp3.

Phylogenomic databases

HOGENOMQ61810.
HOVERGENQ61810.

Gene expression databases

ArrayExpressQ61810.
BgeeQ61810.
GermOnlineENSMUSG00000024940. Mus musculus.

Family and domain databases

InterProIPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR002212. Fibril-assoc.
IPR017878. TFG_b-bd.
[Graphical view]
Gene3DG3DSA:3.90.290.10. Fibril-assoc. 2 hits.
PfamPF00008. EGF. 1 hit.
PF07645. EGF_CA. 11 hits.
PF00683. TB. 3 hits.
[Graphical view]
SMARTSM00181. EGF. 2 hits.
SM00179. EGF_CA. 12 hits.
[Graphical view]
PROSITEPS00010. ASX_HYDROXYL. 10 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 5 hits.
PS50026. EGF_3. 12 hits.
PS01187. EGF_CA. 11 hits.
PS51364. TB. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio291104.
SOURCESearch...

Entry information

Entry nameLTBP3_MOUSE
AccessionPrimary (citable) accession number: Q61810
Secondary accession number(s): Q8BNQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: June 16, 2009
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents