GO45_MOUSE
ID GO45_MOUSE Reviewed; 403 AA.
AC Q8R2X8; Q3TJC4; Q8C0U6; Q9DAV7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Golgin-45;
DE AltName: Full=Basic leucine zipper nuclear factor 1;
GN Name=Blzf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Placenta, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH GORASP2 AND RAB2.
RX PubMed=11739401; DOI=10.1083/jcb.200108079;
RA Short B., Preisinger C., Koerner R., Kopajtich R., Byron O., Barr F.A.;
RT "A GRASP55-rab2 effector complex linking Golgi structure to membrane
RT traffic.";
RL J. Cell Biol. 155:877-883(2001).
RN [4] {ECO:0007744|PDB:5H3J}
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 379-403 IN COMPLEX WITH GORASP2,
RP REGION, AND MUTAGENESIS OF CYS-393; CYS-396 AND LEU-403.
RX PubMed=28049725; DOI=10.1074/jbc.m116.765990;
RA Zhao J., Li B., Huang X., Morelli X., Shi N.;
RT "Structural Basis for the Interaction between Golgi Reassembly-stacking
RT Protein GRASP55 and Golgin45.";
RL J. Biol. Chem. 292:2956-2965(2017).
CC -!- FUNCTION: Required for normal Golgi structure and for protein transport
CC from the endoplasmic reticulum (ER) through the Golgi apparatus to the
CC cell surface. {ECO:0000250|UniProtKB:Q9H2G9}.
CC -!- SUBUNIT: Interacts with GORASP2 (PubMed:11739401, PubMed:28049725).
CC Interacts with the GTP-bound form of RAB2, but not with other Golgi Rab
CC proteins (PubMed:11739401). Identified in a complex with RAB2 and
CC GORASP2 (PubMed:11739401). {ECO:0000269|PubMed:11739401,
CC ECO:0000269|PubMed:28049725}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9H2G9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R2X8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2X8-2; Sequence=VSP_011188;
CC -!- DOMAIN: The tankyrase-binding motif (also named TBD) is required for
CC interaction with tankyrase TNKS and TNKS2.
CC {ECO:0000250|UniProtKB:Q9H2G9}.
CC -!- PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated
CC protein is recognized by RNF146, followed by ubiquitination.
CC {ECO:0000250|UniProtKB:Q9H2G9}.
CC -!- PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its
CC degradation. {ECO:0000250|UniProtKB:Q9H2G9}.
CC -!- CAUTION: Was initially thought to be a potential transcription factor,
CC localized in the nucleus. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK005489; BAB24074.1; -; mRNA.
DR EMBL; AK029787; BAC26617.1; -; mRNA.
DR EMBL; AK167493; BAE39571.1; -; mRNA.
DR EMBL; BC027025; AAH27025.1; -; mRNA.
DR CCDS; CCDS15435.1; -. [Q8R2X8-2]
DR CCDS; CCDS48423.1; -. [Q8R2X8-1]
DR RefSeq; NP_001153680.1; NM_001160208.1. [Q8R2X8-1]
DR RefSeq; NP_001153681.1; NM_001160209.1. [Q8R2X8-1]
DR RefSeq; NP_079781.2; NM_025505.4. [Q8R2X8-2]
DR PDB; 5H3J; X-ray; 1.33 A; B=379-403.
DR PDBsum; 5H3J; -.
DR AlphaFoldDB; Q8R2X8; -.
DR SMR; Q8R2X8; -.
DR BioGRID; 211404; 7.
DR IntAct; Q8R2X8; 8.
DR STRING; 10090.ENSMUSP00000027866; -.
DR iPTMnet; Q8R2X8; -.
DR PhosphoSitePlus; Q8R2X8; -.
DR jPOST; Q8R2X8; -.
DR MaxQB; Q8R2X8; -.
DR PaxDb; Q8R2X8; -.
DR PRIDE; Q8R2X8; -.
DR ProteomicsDB; 271243; -. [Q8R2X8-1]
DR ProteomicsDB; 271244; -. [Q8R2X8-2]
DR Antibodypedia; 20542; 311 antibodies from 29 providers.
DR DNASU; 66352; -.
DR Ensembl; ENSMUST00000027866; ENSMUSP00000027866; ENSMUSG00000026577. [Q8R2X8-2]
DR Ensembl; ENSMUST00000086032; ENSMUSP00000083196; ENSMUSG00000026577. [Q8R2X8-1]
DR Ensembl; ENSMUST00000120447; ENSMUSP00000113479; ENSMUSG00000026577. [Q8R2X8-1]
DR GeneID; 66352; -.
DR KEGG; mmu:66352; -.
DR UCSC; uc007dig.1; mouse. [Q8R2X8-2]
DR UCSC; uc007dih.1; mouse. [Q8R2X8-1]
DR CTD; 8548; -.
DR MGI; MGI:1201607; Blzf1.
DR VEuPathDB; HostDB:ENSMUSG00000026577; -.
DR eggNOG; KOG4074; Eukaryota.
DR GeneTree; ENSGT00390000009400; -.
DR HOGENOM; CLU_057527_0_0_1; -.
DR InParanoid; Q8R2X8; -.
DR OMA; HVVPTKN; -.
DR OrthoDB; 1218216at2759; -.
DR PhylomeDB; Q8R2X8; -.
DR TreeFam; TF317238; -.
DR Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR BioGRID-ORCS; 66352; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Blzf1; mouse.
DR PRO; PR:Q8R2X8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8R2X8; protein.
DR Bgee; ENSMUSG00000026577; Expressed in lumbar dorsal root ganglion and 260 other tissues.
DR Genevisible; Q8R2X8; MM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:MGI.
DR InterPro; IPR027095; Golgin-45.
DR InterPro; IPR013183; Hsk3-like.
DR PANTHER; PTHR13066; PTHR13066; 1.
DR Pfam; PF08227; DASH_Hsk3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing; Coiled coil;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..403
FT /note="Golgin-45"
FT /id="PRO_0000087540"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..403
FT /note="Essential for interaction with GORASP2"
FT /evidence="ECO:0000269|PubMed:28049725"
FT COILED 123..216
FT /evidence="ECO:0000255"
FT MOTIF 22..26
FT /note="Tankyrase-binding motif"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G9"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G9"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G9"
FT VAR_SEQ 14
FT /note="G -> GKQEMMKG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011188"
FT MUTAGEN 393
FT /note="C->A: Reduced interaction with GORASP2; when
FT associated with A-396."
FT /evidence="ECO:0000269|PubMed:28049725"
FT MUTAGEN 396
FT /note="C->A: Reduced interaction with GORASP2; when
FT associated with A-393."
FT /evidence="ECO:0000269|PubMed:28049725"
FT MUTAGEN 403
FT /note="L->R: Reduced interaction with GORASP2."
FT /evidence="ECO:0000269|PubMed:28049725"
FT CONFLICT 320
FT /note="S -> R (in Ref. 2; AAH27025)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="I -> N (in Ref. 2; AAH27025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 45541 MW; F87A9752AEEC3559 CRC64;
MEKMTTLKSS ENKGILTSTP IRGAGDGMET EEPPKSVEVT HGVQPINQHV LPSPRKKVSS
DSPGVLQLGK ILNERTVEVE AVRIFVPKAA ITHDIPTKNT KVKSLGHHRE ELHNQAEVVT
DPRKELSEVK KVLEKLKNSE RRLLQDKEGL SNQLRVQTEI NRELKKLLVA SVGDDPQYHF
ERLAREKNQL ILENEALGRN TAQLSEQLER MSIQCDVWRS KFLASRVMAD ELTNFRVVLQ
RQNRDAQSAI QDLLSEREQF RQEMTSTQKF LEELLVSLQW GREQTYSPNT QPHSTADLAL
TNHGLAQAIH AHLLGNVGIS HQKKIPTTVE FCSTPAEKMA EKVLRILDPV ACTESSPDNQ
FAESSPTTLL TTKKNIGRFH PYTRYENITF NCCNHCQGEL IAL
