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P82198 (BGH3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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

Names and origin

Protein namesRecommended name:
Transforming growth factor-beta-induced protein ig-h3

Short name=Beta ig-h3
Gene names
Name:Tgfbi
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Binds to type I, II, and IV collagens. This adhesion protein may play an important role in cell-collagen interactions. In cartilage, may be involved in endochondral bone formation By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity. Note: May be associated both with microfibrils and with the cell surface By similarity.

Induction

By TGF-beta.

Post-translational modification

Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium By similarity.

Sequence similarities

Contains 1 EMI domain.

Contains 4 FAS1 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 By similarity
Chain24 – 683660Transforming growth factor-beta-induced protein ig-h3
PRO_0000041980

Regions

Domain45 – 9955EMI
Domain103 – 236134FAS1 1
Domain240 – 371132FAS1 2
Domain375 – 498124FAS1 3
Domain502 – 632131FAS1 4
Motif642 – 6443Cell attachment site Potential

Amino acid modifications

Modified residue10814-carboxyglutamate Potential
Modified residue12614-carboxyglutamate Potential
Modified residue13114-carboxyglutamate Potential
Modified residue13314-carboxyglutamate Potential
Modified residue14614-carboxyglutamate Potential
Modified residue15414-carboxyglutamate Potential
Modified residue16614-carboxyglutamate Potential
Modified residue18414-carboxyglutamate Potential
Modified residue24814-carboxyglutamate Potential
Modified residue25014-carboxyglutamate Potential
Modified residue25414-carboxyglutamate Potential
Modified residue27014-carboxyglutamate Potential
Modified residue28314-carboxyglutamate Potential
Modified residue28614-carboxyglutamate Potential
Modified residue29114-carboxyglutamate Potential
Modified residue30114-carboxyglutamate Potential
Modified residue31914-carboxyglutamate Potential
Modified residue32814-carboxyglutamate Potential
Modified residue33614-carboxyglutamate Potential
Modified residue52914-carboxyglutamate Potential
Modified residue53414-carboxyglutamate Potential
Modified residue54514-carboxyglutamate Potential
Modified residue55414-carboxyglutamate Potential
Modified residue56414-carboxyglutamate Potential
Modified residue57614-carboxyglutamate Potential
Modified residue59814-carboxyglutamate Potential
Modified residue61114-carboxyglutamate Potential
Modified residue61514-carboxyglutamate Potential
Disulfide bond49 ↔ 85 By similarity
Disulfide bond65 ↔ 74 By similarity
Disulfide bond84 ↔ 97 By similarity

Sequences

Sequence LengthMass (Da)Tools
P82198 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2B6E9DBB9C50F52B

FASTA68374,597
        10         20         30         40         50         60 
MALLMRLLTL ALALSVGPAG TLAGPAKSPY QLVLQHSRLR GRQHGPNVCA VQKVIGTNKK 

        70         80         90        100        110        120 
YFTNCKQWYQ RKICGKSTVI SYECCPGYEK VPGEKGCPAA LPLSNLYETM GVVGSTTTQL 

       130        140        150        160        170        180 
YTDRTEKLRP EMEGPGSFTI FAPSNEAWSS LPAEVLDSLV SNVNIELLNA LRYHMVDRRV 

       190        200        210        220        230        240 
LTDELKHGMT LTSMYQNSNI QIHHYPNGIV TVNCARLLKA DHHATNGVVH LIDKVISTIT 

       250        260        270        280        290        300 
NNIQQIIEIE DTFETLRAAV AASGLNTVLE GDGQFTLLAP TNEAFEKIPA ETLNRILGDP 

       310        320        330        340        350        360 
EALRDLLNNH ILKSAMCAEA IVAGMSMETL GGTTLEVGCS GDKLTINGKA VISNKDILAT 

       370        380        390        400        410        420 
NGVIHFIDEL LIPDSAKTLL ELAGESDVST AIDILKQAGL DTHLSGKEQL TFLAPLNSVF 

       430        440        450        460        470        480 
KDGVPRIDAQ MKTLLLNHMV KEQLASKYLY SGQTLDTLGG KKLRVFVYRN SLCIENSCIA 

       490        500        510        520        530        540 
AHDKRGRFGT LFTMDRMLTP PMGTVMDVLK GDNRFSMLVA AIQSAGLMEI LNREGVYTVF 

       550        560        570        580        590        600 
APTNEAFQAM PPEELNKLLA NAKELTNILK YHIGDEILVS GGIGALVRLK SLQGDKLEVS 

       610        620        630        640        650        660 
SKNNVVSVNK EPVAETDIMA TNGVVYAINT VLQPPANRPQ ERGDELADSA LEIFKQASAY 

       670        680 
SRAAQRSVRL APVYQRLLER MKH 

« Hide

References

« Hide 'large scale' references
[1]"Beta ig-h3: a transforming growth factor-beta-responsive gene encoding a secreted protein that inhibits cell attachment in vitro and suppresses the growth of CHO cells in nude mice."
Skonier J., Bennett K., Rothwell V., Kosowski S., Plowman G., Wallace P., Edelhoff S., Disteche C.M., Neubauer M., Marquardt H., Rodgers J., Purchio A.F.
DNA Cell Biol. 13:571-584(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: G8.
[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].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Eye and Heart.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19932 mRNA. Translation: AAC37658.1.
AK084431 mRNA. Translation: BAC39181.1.
AK142323 mRNA. Translation: BAE25032.1.
AK151680 mRNA. Translation: BAE30605.1.
AK152365 mRNA. Translation: BAE31155.1.
AK155572 mRNA. Translation: BAE33330.1.
AK155828 mRNA. Translation: BAE33452.1.
AK170495 mRNA. Translation: BAE41834.1.
RefSeqNP_033395.1. NM_009369.4.
UniGeneMm.14455.

3D structure databases

ProteinModelPortalP82198.
SMRP82198. Positions 125-236, 252-373, 377-634.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP82198. 1 interaction.
MINTMINT-4106293.

PTM databases

PhosphoSiteP82198.

Proteomic databases

PaxDbP82198.
PRIDEP82198.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045173; ENSMUSP00000037719; ENSMUSG00000035493.
GeneID21810.
KEGGmmu:21810.
UCSCuc011zae.1. mouse.

Organism-specific databases

CTD7045.
MGIMGI:99959. Tgfbi.

Phylogenomic databases

eggNOGCOG2335.
GeneTreeENSGT00530000063860.
HOGENOMHOG000220865.
HOVERGENHBG000715.
InParanoidP82198.
OMAQFTLLAP.
OrthoDBEOG7N8ZV1.
PhylomeDBP82198.
TreeFamTF316269.

Gene expression databases

ArrayExpressP82198.
BgeeP82198.
CleanExMM_TGFBI.
GenevestigatorP82198.

Family and domain databases

Gene3D2.30.180.10. 4 hits.
InterProIPR011489. EMI_domain.
IPR000782. FAS1_domain.
IPR016666. TGFb-ind_bIGH3/osteoblast_fac2.
[Graphical view]
PfamPF02469. Fasciclin. 4 hits.
[Graphical view]
PIRSFPIRSF016553. BIGH3_OSF2. 1 hit.
SMARTSM00554. FAS1. 4 hits.
[Graphical view]
SUPFAMSSF82153. SSF82153. 4 hits.
PROSITEPS51041. EMI. 1 hit.
PS50213. FAS1. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio301198.
PROP82198.
SOURCESearch...

Entry information

Entry nameBGH3_MOUSE
AccessionPrimary (citable) accession number: P82198
Secondary accession number(s): Q3U9R1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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