TGO1_BOVIN
ID TGO1_BOVIN Reviewed; 1905 AA.
AC Q0VC16;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Transport and Golgi organization protein 1 homolog {ECO:0000305};
DE Short=TANGO1 {ECO:0000305};
DE Flags: Precursor;
GN Name=MIA3 {ECO:0000250|UniProtKB:Q5JRA6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1427-1905.
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the transport of cargos that are too large to
CC fit into COPII-coated vesicles and require specific mechanisms to be
CC incorporated into membrane-bound carriers and exported from the
CC endoplasmic reticulum. This protein is required for collagen VII
CC (COL7A1) secretion by loading COL7A1 into transport carriers. It may
CC participate in cargo loading of COL7A1 at endoplasmic reticulum exit
CC sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound
CC COL7A1 into a growing carrier. Does not play a role in global protein
CC secretion and is apparently specific to COL7A1 cargo loading. However,
CC it may participate in secretion of other proteins in cells that do not
CC secrete COL7A1. It is also specifically required for the secretion of
CC lipoproteins by participating in their export from the endoplasmic
CC reticulum. Required for correct assembly of COPII coat components at
CC endoplasmic reticulum exit sites (ERES) and for the localization of
CC SEC16A and membrane-bound ER-resident complexes consisting of MIA2 and
CC PREB/SEC12 to ERES. {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- SUBUNIT: Interacts with MIA2. Interacts (via SH3 domain) with COL7A1.
CC Interacts with the COPII coat subunits SEC23A, SEC23B and maybe SEC24C.
CC May interact with APOB and MIA2. Interacts with SEC16A.
CC {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5JRA6}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5JRA6}. Note=Localizes at endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). SEC16A is required for its proper localization to ERES. After
CC loading of COL7A1 into transport carriers, it is not incorporated into
CC COPII carriers and remains in the endoplasmic reticulum membrane.
CC {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- DOMAIN: The proline-rich domain (PRD) contains repeated PPP motifs. A
CC single PPP motif is necessary and sufficient to mediate interaction
CC with the COPII coat subunits SEC23A and SEC23B.
CC {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- DOMAIN: Although 2 transmembrane domains are predicted, it only
CC contains one transmembrane domain. The other predicted transmembrane
CC region is probably a hairpin-type region embedded into the membrane,
CC which does not cross the membrane. It is unclear which of the 2
CC predicted transmembrane regions is the transmembrane or the hairpin-
CC type region. {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- SIMILARITY: Belongs to the MIA/OTOR family. Tango1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFC03070852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03070853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03010368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120395; AAI20396.1; -; mRNA.
DR RefSeq; NP_001160043.1; NM_001166571.1.
DR AlphaFoldDB; Q0VC16; -.
DR SMR; Q0VC16; -.
DR STRING; 9913.ENSBTAP00000025055; -.
DR PaxDb; Q0VC16; -.
DR PeptideAtlas; Q0VC16; -.
DR PRIDE; Q0VC16; -.
DR GeneID; 509133; -.
DR KEGG; bta:509133; -.
DR CTD; 375056; -.
DR eggNOG; ENOG502QS87; Eukaryota.
DR InParanoid; Q0VC16; -.
DR OrthoDB; 208382at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; ISS:UniProtKB.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0035459; P:vesicle cargo loading; IBA:GO_Central.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Exocytosis;
KW Glycoprotein; Membrane; Methylation; Phosphoprotein; Protein transport;
KW Reference proteome; SH3 domain; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1905
FT /note="Transport and Golgi organization protein 1 homolog"
FT /id="PRO_0000370509"
FT TOPO_DOM 23..1141
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 1142..1162
FT /evidence="ECO:0000255"
FT TOPO_DOM 1163..1173
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1174..1194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1195..1905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..107
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 154..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1647
FT /note="Mediates interaction with MIA2"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT REGION 1416..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1905
FT /note="Proline-rich domain (PRD); mediates interaction with
FT the COPII coat subunits SEC23A and SEC23B"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT REGION 1785..1845
FT /note="SEC16A-interacting region (SIR); required for its
FT localization to endoplasmic reticulum exit sites and for
FT its interaction with SEC16A"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT COILED 467..527
FT /evidence="ECO:0000255"
FT COILED 1211..1393
FT /evidence="ECO:0000255"
FT COILED 1484..1636
FT /evidence="ECO:0000255"
FT COMPBIAS 154..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1728..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1887..1905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 1428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 1724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 1781
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1905 AA; 211668 MW; 8711A1D5C29F12CE CRC64;
MAAAQGLLFW LLLLGPPCRV PGQPEQDPGR RFSQFKLCAD EECCMLMYRG EALEDFTGPD
CRFVNFKKGD TVYVYYKLAG GSPEVWAGSV GHTFGYFPKD LIQVVHEYTQ EELQVPTDET
DFVCFDGGRD DFDNYNVEDL LGFLELYDSA TEDSEKVKEK TAQRVEEPPE ASNESDAEPE
PGEPNSEESE SVLSENTAEL RERSEAQKSH PQVNSQTGHA QGERTSFESF GEMLQDKLKV
PDSENNKTSN SSQVSHEQEK IDAYKLLKTE MTLDLKTKFG STADALVSDD ETTRLVTSLE
DDFVEDLDPE YYTVGKEEEE NKEDFDELPL LTFTDGEDTK SPGHSGIEKH PTEKEQNSNK
EHKVEETQPP GIKKGDKEIP KHREDTVFSD VMEGEENTDT DLESSDSKEE DDPLVMDSRL
GKPRPEDHTD PEKAADHLVN VEVPKADSDD DPEVGAGLHM KDKGRKVEEP RRDWVQHEVG
LEDETQEDQA VQGSSQSGHL RSSPAAEKST ETLKSAFANQ ENDLKGAAVH ISKEMLHEEK
PSGRSLEGAS KSDSVPQAKA AGNQGEEGKT EREPVGVAAP SGDHQPNASK DSVDEVDGSI
SGPKPHVLSG EHPSAELIKD RLLKLQNQTR FSSPDDMGLP GDLEKKRPIL ERKLSWQQGG
VAAAVNKQVS EKRELPEEEV TRVTKDASDE GQEVRKTGQT DSIEGRGFRP KEPNPEDEDY
SPEELLEDEN AVSAKQSKER SPEIQDKRLD VDLQNPEKPV SGAIKTDPET EKNKEETRHV
SENERKNETA GKAVDSLGRD AGGPVVEKEG SSPVHQKVQR PSEGSDVPGK KQNQTPELGE
ASQKKDPDYL KEDNHEGHPK TSGLMEKPGV EPSKEDDEHA EKFVDPGSRG SASEDPDDDP
FPWAPHAPVQ PEESVHLEDL PIISSFFKDQ QSLQRFQKYF DIHKLEAMFQ DMSSKLKSAQ
RESLPYNVEK VLDKVFRAWE SHILTEAENM LDARVTENRD LETKDSSVFE EAAVLDDVQD
LIYFVRYKHS TVEETAPPAA AQPVEGGWDG PAEDTQPPLE ENFPQEHMEV PLMQIPKEPG
HLAQPVTRDM GTSGVAQKPQ TEEDGDPGII TPQGTPVDAD DAQKQLAANT EEPASVTPLE
NAIAFIYSLV FHLTKTLLAT LPDDVQPGPD FYGLPWKPVL ITASLGIVSF AVFFWRTVLA
VKSRVYQVTE QQISEKLKNI MKENAELVQK LSSYEQKIKE SKKHVQETKK QNMILSDEAI
KFKDKIKSLE ETNEILGDTA KSLRAMLESE REQNAKNQDL ISENKKSIEK LKDVISVNAS
EFSEVQIALN EAKLSEEKVK SECHRVQEEN ARLKKKKEQL QQEIKDWSKS HAELSEQIRS
FEKSQKDLEV ALTHKDDNIN ALTNCITQLN RLDCESESED QNKGGSESDE LANGEVGGDR
SEKVKNQIKQ MMDVSRTQTA ISVVEEDLKL LQCKLRASMS TKCNLEDQIK KLEEDRSSLQ
SAKTVLEDEC KTLRQKVEIL NELYQQKEMA LQKKLSQEEY ERQEREQRLS AADEKAVLAA
EEVKTYKRRI EEMEDELQKT ERSFKNQIAT HEKKAHDNWL KARAAERAIA EEKREAANLR
HKLLELTQKM AMMQEEPVIV KPMPGRPNTQ NPPRRGPLSQ NGSFGPSPVS GGECSPPLTA
DPPARPLSAT LNRREMPRSE FGSVDGPLPR PRWASEASGK PSASDPESGA APTVNSSSRS
SSPSKVMDEG KVSMAAKGPP PFPGTPLMSS PVGGPLLPPI RYGPPPQLCG PFGPRPLPPP
FGPGMRPPLG LREYAPGVPP GKRDLPLDPR EFLPPGHAPF RPLGSLGPRE YFFPGTRLPP
PNHGPQDYPP SSAARDLPPS GSRDEPPPAS QGASQDCSPA LKQSP
