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   24-JAN-2024, entry version 145.
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}.
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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; 8.
DR   IntAct; Q8R2X8; 8.
DR   STRING; 10090.ENSMUSP00000027866; -.
DR   iPTMnet; Q8R2X8; -.
DR   PhosphoSitePlus; Q8R2X8; -.
DR   jPOST; Q8R2X8; -.
DR   MaxQB; Q8R2X8; -.
DR   PaxDb; 10090-ENSMUSP00000027866; -.
DR   ProteomicsDB; 271243; -. [Q8R2X8-1]
DR   ProteomicsDB; 271244; -. [Q8R2X8-2]
DR   Pumba; Q8R2X8; -.
DR   Antibodypedia; 20542; 339 antibodies from 29 providers.
DR   DNASU; 66352; -.
DR   Ensembl; ENSMUST00000027866.11; ENSMUSP00000027866.5; ENSMUSG00000026577.14. [Q8R2X8-2]
DR   Ensembl; ENSMUST00000086032.4; ENSMUSP00000083196.4; ENSMUSG00000026577.14. [Q8R2X8-1]
DR   Ensembl; ENSMUST00000120447.8; ENSMUSP00000113479.2; ENSMUSG00000026577.14. [Q8R2X8-1]
DR   GeneID; 66352; -.
DR   KEGG; mmu:66352; -.
DR   UCSC; uc007dig.1; mouse. [Q8R2X8-2]
DR   UCSC; uc007dih.1; mouse. [Q8R2X8-1]
DR   AGR; MGI:1201607; -.
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; ELCNTPA; -.
DR   OrthoDB; 2879260at2759; -.
DR   PhylomeDB; Q8R2X8; -.
DR   TreeFam; TF317238; -.
DR   Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR   BioGRID-ORCS; 66352; 4 hits in 78 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 264 other cell types or tissues.
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; BASIC LEUCINE ZIPPER NUCLEAR FACTOR 1 BLZF1 PROTEIN; 1.
DR   PANTHER; PTHR13066:SF2; GOLGIN-45; 1.
DR   Pfam; PF08227; DASH_Hsk3; 1.
DR   Genevisible; Q8R2X8; MM.
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
//