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Protein

Latent-transforming growth factor beta-binding protein 3

Gene

Ltbp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).

GO - Molecular functioni

GO - Biological processi

  • bone morphogenesis Source: MGI
  • bone remodeling Source: MGI
  • lung saccule development Source: MGI
  • negative regulation of bone mineralization Source: MGI
  • negative regulation of chondrocyte differentiation Source: MGI
  • positive regulation of bone resorption Source: MGI
  • positive regulation of mesenchymal stem cell differentiation Source: MGI
  • positive regulation of mesenchymal stem cell proliferation Source: MGI
  • skeletal system development Source: MGI
  • transforming growth factor beta activation Source: MGI
  • transforming growth factor beta receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Ligandi

Growth factor binding

Names & Taxonomyi

Protein namesi
Recommended name:
Latent-transforming growth factor beta-binding protein 3
Short name:
LTBP-3
Gene namesi
Name:Ltbp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1101355. Ltbp3.

Subcellular locationi

  • Secreted

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838Sequence analysisAdd
BLAST
Chaini39 – 12681230Latent-transforming growth factor beta-binding protein 3PRO_0000007647Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi110 ↔ 120PROSITE-ProRule annotation
Disulfide bondi114 ↔ 126PROSITE-ProRule annotation
Disulfide bondi128 ↔ 137PROSITE-ProRule annotation
Disulfide bondi276 ↔ 300PROSITE-ProRule annotation
Disulfide bondi286 ↔ 313PROSITE-ProRule annotation
Disulfide bondi301 ↔ 316PROSITE-ProRule annotation
Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence analysis
Disulfide bondi356 ↔ 367PROSITE-ProRule annotation
Disulfide bondi363 ↔ 376PROSITE-ProRule annotation
Disulfide bondi378 ↔ 391PROSITE-ProRule annotation
Disulfide bondi402 ↔ 425PROSITE-ProRule annotation
Disulfide bondi412 ↔ 437PROSITE-ProRule annotation
Disulfide bondi426 ↔ 440PROSITE-ProRule annotation
Disulfide bondi427 ↔ 452PROSITE-ProRule annotation
Disulfide bondi574 ↔ 586PROSITE-ProRule annotation
Disulfide bondi581 ↔ 595PROSITE-ProRule annotation
Disulfide bondi597 ↔ 610PROSITE-ProRule annotation
Disulfide bondi616 ↔ 628PROSITE-ProRule annotation
Disulfide bondi621 ↔ 637PROSITE-ProRule annotation
Disulfide bondi639 ↔ 654PROSITE-ProRule annotation
Disulfide bondi660 ↔ 672PROSITE-ProRule annotation
Disulfide bondi666 ↔ 681PROSITE-ProRule annotation
Disulfide bondi683 ↔ 697PROSITE-ProRule annotation
Disulfide bondi744 ↔ 755PROSITE-ProRule annotation
Disulfide bondi750 ↔ 764PROSITE-ProRule annotation
Disulfide bondi766 ↔ 778PROSITE-ProRule annotation
Disulfide bondi784 ↔ 795PROSITE-ProRule annotation
Disulfide bondi790 ↔ 804PROSITE-ProRule annotation
Disulfide bondi806 ↔ 819PROSITE-ProRule annotation
Disulfide bondi825 ↔ 836PROSITE-ProRule annotation
Disulfide bondi831 ↔ 845PROSITE-ProRule annotation
Glycosylationi840 – 8401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi847 ↔ 859PROSITE-ProRule annotation
Disulfide bondi866 ↔ 878PROSITE-ProRule annotation
Disulfide bondi873 ↔ 887PROSITE-ProRule annotation
Disulfide bondi889 ↔ 902PROSITE-ProRule annotation
Disulfide bondi914 ↔ 937PROSITE-ProRule annotation
Disulfide bondi924 ↔ 949PROSITE-ProRule annotation
Glycosylationi931 – 9311N-linked (GlcNAc...)Sequence analysis
Disulfide bondi938 ↔ 954PROSITE-ProRule annotation
Disulfide bondi992 ↔ 1005PROSITE-ProRule annotation
Disulfide bondi1000 ↔ 1014PROSITE-ProRule annotation
Disulfide bondi1016 ↔ 1029PROSITE-ProRule annotation
Disulfide bondi1035 ↔ 1046PROSITE-ProRule annotation
Disulfide bondi1041 ↔ 1055PROSITE-ProRule annotation
Disulfide bondi1057 ↔ 1070PROSITE-ProRule annotation
Disulfide bondi1205 ↔ 1220PROSITE-ProRule annotation
Disulfide bondi1215 ↔ 1229PROSITE-ProRule annotation
Glycosylationi1222 – 12221N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1231 ↔ 1245PROSITE-ProRule annotation

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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61810.
PaxDbiQ61810.
PeptideAtlasiQ61810.
PRIDEiQ61810.

PTM databases

iPTMnetiQ61810.
PhosphoSiteiQ61810.

Expressioni

Developmental stagei

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.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201221. 1 interaction.
DIPiDIP-48641N.
IntActiQ61810. 1 interaction.
STRINGi10090.ENSMUSP00000080214.

Structurei

3D structure databases

ProteinModelPortaliQ61810.
SMRiQ61810. Positions 911-970.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini106 – 13833EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini274 – 32855TB 1PROSITE-ProRule annotationAdd
BLAST
Domaini352 – 39241EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini400 – 45253TB 2PROSITE-ProRule annotationAdd
BLAST
Domaini570 – 61142EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini612 – 65544EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini656 – 69843EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini740 – 77940EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini780 – 82041EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini821 – 86040EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini862 – 90342EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini912 – 96655TB 3PROSITE-ProRule annotationAdd
BLAST
Domaini988 – 103043EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1031 – 107040EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1201 – 124646EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi21 – 3212Poly-LeuAdd
BLAST
Compositional biasi47 – 526Poly-Gly
Compositional biasi191 – 292102Pro-richAdd
BLAST
Compositional biasi480 – 55677Pro-richAdd
BLAST
Compositional biasi574 – 889316Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the LTBP family.Curated
Contains 12 EGF-like domains.PROSITE-ProRule annotation
Contains 3 TB (TGF-beta binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR6V. Eukaryota.
ENOG4110G15. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ61810.
KOiK08023.
PhylomeDBiQ61810.

Family and domain databases

Gene3Di3.90.290.10. 3 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]
PfamiPF07645. EGF_CA. 11 hits.
PF00683. TB. 3 hits.
[Graphical view]
SMARTiSM00181. EGF. 14 hits.
SM00179. EGF_CA. 13 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57581. SSF57581. 3 hits.
PROSITEiPS00010. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q61810-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPGPRGAAHG LAPAMHQAGA LGLLALLLLA LLGPGGGAEG GPAGERGTGG
60 70 80 90 100
GGALARERFK VVFAPVICKR TCLKGQCRDS CQQGSNMTLI GENGHSTDTL
110 120 130 140 150
TGSAFRVVVC PLPCMNGGQC SSRNQCLCPP DFTGRFCQVP AAGTGAGTGS
160 170 180 190 200
SGPGLARTGA MSTGPLPPLA PEGESVASKH AIYAVQVIAD PPGPGEGPPA
210 220 230 240 250
QHAAFLVPLG PGQISAEVQA PPPVVNVRVH HPPEASVQVH RIEGPNAEGP
260 270 280 290 300
ASSQHLLPHP KPPHPRPPTQ KPLGRCFQDT LPKQPCGSNP LPGLTKQEDC
310 320 330 340 350
CGSIGTAWGQ SKCHKCPQLQ YTGVQKPVPV RGEVGADCPQ GYKRLNSTHC
360 370 380 390 400
QDINECAMPG NVCHGDCLNN PGSYRCVCPP GHSLGPLAAQ CIADKPEEKS
410 420 430 440 450
LCFRLVSTEH QCQHPLTTRL TRQLCCCSVG KAWGARCQRC PADGTAAFKE
460 470 480 490 500
ICPGKGYHIL TSHQTLTIQG ESDFSLFLHP DGPPKPQQLP ESPSRAPPLE
510 520 530 540 550
DTEEERGVTM DPPVSEERSV QQSHPTTTTS PPRPYPELIS RPSPPTFHRF
560 570 580 590 600
LPDLPPSRSA VEIAPTQVTE TDECRLNQNI CGHGQCVPGP SDYSCHCNAG
610 620 630 640 650
YRSHPQHRYC VDVNECEAEP CGPGKGICMN TGGSYNCHCN RGYRLHVGAG
660 670 680 690 700
GRSCVDLNEC AKPHLCGDGG FCINFPGHYK CNCYPGYRLK ASRPPICEDI
710 720 730 740 750
DECRDPSTCP DGKCENKPGS FKCIACQPGY RSQGGGACRD VNECSEGTPC
760 770 780 790 800
SPGWCENLPG SYRCTCAQYE PAQDGLSCID VDECEAGKVC QDGICTNTPG
810 820 830 840 850
SFQCQCLSGY HLSRDRSRCE DIDECDFPAA CIGGDCINTN GSYRCLCPLG
860 870 880 890 900
HRLVGGRKCK KDIDECSQDP GLCLPHACEN LQGSYVCVCD EGFTLTQDQH
910 920 930 940 950
GCEEVEQPHH KKECYLNFDD TVFCDSVLAT NVTQQECCCS LGAGWGDHCE
960 970 980 990 1000
IYPCPVYSSA EFHSLVPDGK RLHSGQQHCE LCIPAHRDID ECILFGAEIC
1010 1020 1030 1040 1050
KEGKCVNTQP GYECYCKQGF YYDGNLLECV DVDECLDESN CRNGVCENTR
1060 1070 1080 1090 1100
GGYRCACTPP AEYSPAQAQC LIPERWSTPQ RDVKCAGASE ERTACVWGPW
1110 1120 1130 1140 1150
AGPALTFDDC CCRQPRLGTQ CRPCPPRGTG SQCPTSQSES NSFWDTSPLL
1160 1170 1180 1190 1200
LGKSPRDEDS SEEDSDECRC VSGRCVPRPG GAVCECPGGF QLDASRARCV
1210 1220 1230 1240 1250
DIDECRELNQ RGLLCKSERC VNTSGSFRCV CKAGFTRSRP HGPACLSAAA
1260
DDAAIAHTSV IDHRGYFH
Length:1,268
Mass (Da):135,702
Last modified:January 16, 2004 - v3
Checksum:i98F632F249ACB4DD
GO
Isoform 2 (identifier: Q61810-2) [UniParc]FASTAAdd to basket

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

Show »
Length:882
Mass (Da):93,355
Checksum:iC5D95F4994A2E776
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161H → R in AAB53015 (PubMed:7730318).Curated
Sequence conflicti20 – 201A → G in AAB53015 (PubMed:7730318).Curated
Sequence conflicti35 – 351Missing in AAB53015 (PubMed:7730318).Curated
Sequence conflicti45 – 451E → Q in AAB53015 (PubMed:7730318).Curated
Sequence conflicti104 – 1041A → G in BAC38053 (PubMed:16141072).Curated
Sequence conflicti172 – 1721E → Q in BAC38053 (PubMed:16141072).Curated
Sequence conflicti263 – 2631P → Q in BAC38053 (PubMed:16141072).Curated
Sequence conflicti328 – 3281V → G in BAC38053 (PubMed:16141072).Curated
Sequence conflicti361 – 3633NVC → MCR in BAC38053 (PubMed:16141072).Curated
Sequence conflicti387 – 3893LAA → SRT in BAC38053 (PubMed:16141072).Curated
Sequence conflicti453 – 4531P → PA in BAC38053 (PubMed:16141072).Curated
Sequence conflicti661 – 6611A → T in BAC38053 (PubMed:16141072).Curated
Sequence conflicti768 – 7681Q → QG in BAC38053 (PubMed:16141072).Curated
Sequence conflicti849 – 8491L → Q in BAC38053 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei860 – 88223KKDID…CENLQ → QGMRSWPGILKGEAGQCDLF DTL in isoform 2. 1 PublicationVSP_009242Add
BLAST
Alternative sequencei883 – 1268386Missing in isoform 2. 1 PublicationVSP_009243Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40459 mRNA. Translation: AAB53015.1. Sequence problems.
AK080869 mRNA. Translation: BAC38053.1.
PIRiA57293.
RefSeqiNP_032546.2. NM_008520.2.
UniGeneiMm.182396.

Genome annotation databases

GeneIDi16998.
KEGGimmu:16998.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40459 mRNA. Translation: AAB53015.1. Sequence problems.
AK080869 mRNA. Translation: BAC38053.1.
PIRiA57293.
RefSeqiNP_032546.2. NM_008520.2.
UniGeneiMm.182396.

3D structure databases

ProteinModelPortaliQ61810.
SMRiQ61810. Positions 911-970.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201221. 1 interaction.
DIPiDIP-48641N.
IntActiQ61810. 1 interaction.
STRINGi10090.ENSMUSP00000080214.

PTM databases

iPTMnetiQ61810.
PhosphoSiteiQ61810.

Proteomic databases

MaxQBiQ61810.
PaxDbiQ61810.
PeptideAtlasiQ61810.
PRIDEiQ61810.

Protocols and materials databases

DNASUi16998.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16998.
KEGGimmu:16998.

Organism-specific databases

CTDi4054.
MGIiMGI:1101355. Ltbp3.

Phylogenomic databases

eggNOGiENOG410IR6V. Eukaryota.
ENOG4110G15. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ61810.
KOiK08023.
PhylomeDBiQ61810.

Miscellaneous databases

ChiTaRSiLtbp3. mouse.
PROiQ61810.
SOURCEiSearch...

Family and domain databases

Gene3Di3.90.290.10. 3 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]
PfamiPF07645. EGF_CA. 11 hits.
PF00683. TB. 3 hits.
[Graphical view]
SMARTiSM00181. EGF. 14 hits.
SM00179. EGF_CA. 13 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57581. SSF57581. 3 hits.
PROSITEiPS00010. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] (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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiLTBP3_MOUSE
AccessioniPrimary (citable) accession number: Q61810
Secondary accession number(s): Q8BNQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: July 6, 2016
This is version 142 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.