UniProtKB - Q8BI84 (TGO1_MOUSE)
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Protein
Transport and Golgi organization protein 1 homolog
Gene
Mia3
Organism
Mus musculus (Mouse)
Status
Functioni
Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. It may participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. It is also specifically required for the secretion of lipoproteins by participating in their export from the endoplasmic reticulum.By similarity
GO - Molecular functioni
- lipoprotein transporter activity Source: UniProtKB
GO - Biological processi
- cargo loading into COPII-coated vesicle Source: UniProtKB
- chondrocyte development Source: MGI
- collagen fibril organization Source: MGI
- ER to Golgi vesicle-mediated transport Source: UniProtKB
- exocytosis Source: UniProtKB
- lipoprotein transport Source: UniProtKB
- negative regulation of cell adhesion Source: MGI
- negative regulation of cell migration Source: MGI
- positive regulation of bone mineralization Source: MGI
- positive regulation of leukocyte migration Source: MGI
- protein transport Source: UniProtKB
- wound healing Source: MGI
Keywordsi
Biological process | ER-Golgi transport, Exocytosis, Protein transport, Transport |
Protein family/group databases
TCDBi | 9.B.113.1.1. the collagen secretory protein, mia3 (mia3) family. |
Names & Taxonomyi
Protein namesi | Recommended name: Transport and Golgi organization protein 1 homologCuratedShort name: TANGO1Curated Alternative name(s): Melanoma inhibitory activity protein 3Imported |
Gene namesi | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:2443183. Mia3. |
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 25 – 1171 | LumenalSequence analysisAdd BLAST | 1147 | |
Intramembranei | 1172 – 1192 | Sequence analysisAdd BLAST | 21 | |
Topological domaini | 1193 – 1202 | LumenalSequence analysis | 10 | |
Transmembranei | 1203 – 1223 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1224 – 1930 | CytoplasmicSequence analysisAdd BLAST | 707 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 24 | Sequence analysisAdd BLAST | 24 | |
ChainiPRO_0000288999 | 25 – 1930 | Transport and Golgi organization protein 1 homologAdd BLAST | 1906 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 229 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 360 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 631 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 856 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1458 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1693 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1705 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1733 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1754 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1766 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1770 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1805 | Asymmetric dimethylarginineCombined sources | 1 | |
Modified residuei | 1915 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
Glycoprotein, Methylation, PhosphoproteinProteomic databases
EPDi | Q8BI84. |
PaxDbi | Q8BI84. |
PeptideAtlasi | Q8BI84. |
PRIDEi | Q8BI84. |
PTM databases
iPTMneti | Q8BI84. |
PhosphoSitePlusi | Q8BI84. |
Expressioni
Developmental stagei
Ubiquitously expressed during embryogenesis, starting at E8.1 Publication
Gene expression databases
CleanExi | MM_MIA3. |
Interactioni
Subunit structurei
Interacts with CTAGE5. Interacts (via SH3 domain) with COL7A1. Interacts with the COPII coat subunits SEC23A, SEC23B and maybe SEC24C. May interact with APOB and MIA2.By similarity
Protein-protein interaction databases
BioGridi | 237218. 1 interactor. |
IntActi | Q8BI84. 3 interactors. |
MINTi | Q8BI84. |
STRINGi | 10090.ENSMUSP00000064801. |
Structurei
3D structure databases
ProteinModelPortali | Q8BI84. |
SMRi | Q8BI84. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 45 – 107 | SH3PROSITE-ProRule annotationAdd BLAST | 63 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1238 – 1677 | Mediates interaction with CTAGE5By similarityAdd BLAST | 440 | |
Regioni | 1776 – 1930 | Proline-rich domain (PRD); mediates interaction with the COPII coat subunits SEC23A and SEC23BBy similarityAdd BLAST | 155 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 1236 – 1329 | Sequence analysisAdd BLAST | 94 | |
Coiled coili | 1359 – 1422 | Sequence analysisAdd BLAST | 64 | |
Coiled coili | 1514 – 1662 | Sequence analysisAdd BLAST | 149 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 317 – 324 | Poly-Glu | 8 | |
Compositional biasi | 693 – 699 | Poly-Glu | 7 | |
Compositional biasi | 1020 – 1110 | Pro-richAdd BLAST | 91 | |
Compositional biasi | 1667 – 1916 | Pro-richAdd BLAST | 250 |
Domaini
The proline-rich domain (PRD) contains repeated PPP motifs. A single PPP motif is necessary and sufficient to mediate interaction with the COPII coat subunits SEC23A and SEC23B.By similarity
Although 2 transmembrane domains are predicted, it only contains one transmembrane domain. The other predicted transmembrane region is probably a hairpin-type region embedded into the membrane, which does not cross the membrane. It is unclear which of the 2 predicted transmembrane regions is the transmembrane or the hairpin-type region.By similarity
Sequence similaritiesi
Keywords - Domaini
Coiled coil, SH3 domain, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG410IFUG. Eukaryota. ENOG410YVAS. LUCA. |
HOVERGENi | HBG108133. |
InParanoidi | Q8BI84. |
PhylomeDBi | Q8BI84. |
Family and domain databases
InterProi | View protein in InterPro IPR036028. SH3-like_dom_sf. IPR001452. SH3_domain. |
Pfami | View protein in Pfam PF07653. SH3_2. 1 hit. |
SUPFAMi | SSF50044. SSF50044. 1 hit. |
PROSITEi | View protein in PROSITE PS50002. SH3. 1 hit. |
s (3)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q8BI84-1) [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.
10 20 30 40 50
MAAAPGLLFW LFVLGALWWV PGQSDLSHGR RFSDLKVCGD EECSMLMYRG
60 70 80 90 100
KALEDFTGPD CRFVNFKKGD DVYVYYKLAG GSLELWAGSV EHSFGYFPKD
110 120 130 140 150
LIKVLHKYTE EELHIPADET DFVCFEGGRD DFNSYNVEEL LGSLELEDSV
160 170 180 190 200
PEESKKAEEV SQHREKSPEE SRGRELDPVP EPEAFRADSE DGEGAFSEST
210 220 230 240 250
EGLQGQPSAQ ESHPHTSGPA ANAQGVQSSL DTFEEILHDK LKVPGSESRT
260 270 280 290 300
GNSSPASVER EKTDAYKVLK TEMSLDLKTK FGSTADALVS DDEATRLVTS
310 320 330 340 350
LEDGFDEALD AEYYPMEEEE EVEEDADSSD ELPLLTFSDK DEKVPGKPMI
360 370 380 390 400
EKYLTDKDPN LSEEDKVEPP TWGDAFFSIV TGGEGKPGVV DLERSIEEEE
410 420 430 440 450
DVSVSSSHQR KPQPAAGYTD SEDEGDDLFV EEPKTNDVKD SETDPELVIT
460 470 480 490 500
GEEKDIQESR KGLVQPESQS EDAKSETASA YRLQGSKLNP LSAAEKGRDF
510 520 530 540 550
TLKAVFEKKE NGLKESVIHI SKETLHEDKT REIQRDSLES ELVHRALGSS
560 570 580 590 600
VTENNKPKSL GVAPLLGNNK PDASKDSTEV PDGSVSGPKA GQQEGFLEPG
610 620 630 640 650
LKTQHQPRFS PPEETGPSRE LGGKVPISGR NLSWQQEQDV AAVVGKHANE
660 670 680 690 700
KTGFPEEESR EDGTDAEQAR AIRRPQEAES PEVLSVQPGR PDEEEEEEEG
710 720 730 740 750
DNYPPEGLME DENAVSAQQS RENSPSARDG RSDMNSQVFE KVILGTLNLN
760 770 780 790 800
TEKTKQPANM ILETGQESET TSEEAGDVGK ESGHSVVVDS EESHLADMRA
810 820 830 840 850
QRPSQVHGLR DETAAQTPGS GEAVLSKNPN DLQKDNPEEE LVNTLGLEDP
860 870 880 890 900
GVGEISEGEP EDTKEFGVSE SQGTDAEDLR DDPSRQATPE IPDIVLKSIR
910 920 930 940 950
EDLPIINSFF KDDQQSLHRF LKYFDVRELE GLLEDMSIRL RSAHQNSLPY
960 970 980 990 1000
NMEKVLDKVF RASESRILSM AEKMLDTGVA KNRDLGSKES SPLEEAEVLD
1010 1020 1030 1040 1050
DIQDLIYFVR YQYSGVETAP LVTPPPPEEG WARPGEERQP PQQDSLPQEN
1060 1070 1080 1090 1100
TGDLSVQPPE EPELSDQPVT SVQPPEEPEL SDQPVTSVQP PEEPELSDQP
1110 1120 1130 1140 1150
VTSVQPPEEP ELSDQPVTGY TSTSEVSQKP DTKKDIDLGP VMEGGPVGAG
1160 1170 1180 1190 1200
DVQKQLETIA EEPAAVPPLE SAFGSLYAFI LYLSKMLLAT LPDNVQPGPD
1210 1220 1230 1240 1250
FYGLPWQPVI ITAVLGIVSF AIFSWRTILV VKSRVYQVTE KQISEKLENI
1260 1270 1280 1290 1300
KKENAELMQK LSSYEQKIKE SKKYVQETKK QNMILSDEAV KYKDKIKILE
1310 1320 1330 1340 1350
ETNVSLGDKA KSLRLQLESE REQNVKNQDL ILENKKSIEK LKDVISMNAS
1360 1370 1380 1390 1400
ELSEVQVALN EAKLSEENVK SECHRVQEEN ARLKKKKEQL QQQVEEWSKS
1410 1420 1430 1440 1450
HAELTGQIKS FEKSQEDLEI ALTHKDDNIS ALTNCITQLN RLECELESED
1460 1470 1480 1490 1500
PDKGGNESDD LANGETGGDR SEKIRNRIKQ MMDVSRTQTA VSIVEEDLKL
1510 1520 1530 1540 1550
LQLKLRASMS TKCNLEDQIK KLEDDRSSLQ TAKAGLEDEC KTLRQKVEIL
1560 1570 1580 1590 1600
NELYQQKEMA LQKKLSQEEY ERQDREQRLT AADEKVVLAA EEVKTYKRRI
1610 1620 1630 1640 1650
EEMEEELQKT ERSFKNQIAA HEKKAHDNWL KARAAERAMA EEKREAANLR
1660 1670 1680 1690 1700
HKLLEMTQKM AMRQDEPVIV KPMPGRPNTQ NPPRRGLLSQ NGSFGPSPVS
1710 1720 1730 1740 1750
GGECSPPLPA EPPGRPLSAT LSRRDTPRSE FGSLDRHLPR PRWPSEASGK
1760 1770 1780 1790 1800
HSASDPGPAP VVNSSSRSSS PAKAVDEGKV NMAPKGPPPF PGVPLMGGPV
1810 1820 1830 1840 1850
PPPIRYGPPP QLCGGPFGPR PLPPPFVPGM HPPLGVREYA PGVLPGKRDL
1860 1870 1880 1890 1900
PLDPREFLPG HTPFRPPGSL GPREFFIPGT RLPPPTHGPQ EYPPPPPAVR
1910 1920 1930
DSLPSGPREE AKPASPSSVQ DRSQASKPTP
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_025865 | 1 – 1149 | Missing in isoform 3. 1 PublicationAdd BLAST | 1149 | |
Alternative sequenceiVSP_025866 | 1150 – 1186 | GDVQK…YLSKM → MDSLPATVPAVTASPGDPEL LGPLSVLYAALIAKLLE in isoform 3. 1 PublicationAdd BLAST | 37 | |
Alternative sequenceiVSP_025867 | 1232 – 1239 | KSRVYQVT → SKLNYLIT in isoform 2. 1 Publication | 8 | |
Alternative sequenceiVSP_025868 | 1240 – 1930 | Missing in isoform 2. 1 PublicationAdd BLAST | 691 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK044749 mRNA. Translation: BAC32064.1. AK046506 mRNA. Translation: BAC32759.1. AK078951 mRNA. Translation: BAC37474.1. AK084344 mRNA. Translation: BAC39164.1. AK148470 mRNA. Translation: BAE28571.1. Different termination. CAAA01083517 Genomic DNA. No translation available. AK220252 mRNA. Translation: BAD90177.1. BC125472 mRNA. Translation: AAI25473.1. |
RefSeqi | NP_796363.2. NM_177389.3. [Q8BI84-1] |
UniGenei | Mm.41152. |
Genome annotation databases
GeneIDi | 338366. |
KEGGi | mmu:338366. |
UCSCi | uc008icw.1. mouse. [Q8BI84-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | TGO1_MOUSE | |
Accessioni | Q8BI84Primary (citable) accession number: Q8BI84 Secondary accession number(s): A0JLX8 Q8C5B9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 29, 2007 |
Last sequence update: | May 29, 2007 | |
Last modified: | March 28, 2018 | |
This is version 116 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |