LOCUS       NP_081628                451 aa            linear   ROD 10-FEB-2025
DEFINITION  Golgi reassembly-stacking protein 2 [Mus musculus].
ACCESSION   NP_081628
VERSION     NP_081628.3
DBSOURCE    REFSEQ: accession NM_027352.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Klaus,A., Clapes,T., Yvernogeau,L., Basu,S., Weijts,B., Maas,J.,
            Smal,I., Galjart,N. and Robin,C.
  TITLE     CLASP2 safeguards hematopoietic stem cell properties during mouse
            and fish development
  JOURNAL   Cell Rep 39 (11), 110957 (2022)
   PUBMED   35705037
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Grond,R., Veenendaal,T., Duran,J.M., Raote,I., van Es,J.H.,
            Corstjens,S., Delfgou,L., El Haddouti,B., Malhotra,V. and
            Rabouille,C.
  TITLE     The function of GORASPs in Golgi apparatus organization in vivo
  JOURNAL   J Cell Biol 219 (9) (2020)
   PUBMED   32573693
  REMARK    GeneRIF: The function of GORASPs in Golgi apparatus organization in
            vivo.
            Erratum:[J Cell Biol. 2020 Sep 7;219(9):jcb.20200419106242020c.
            doi: 10.1083/jcb.20200419106242020c.. PMID: 32589188]
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Bailly,A.L., Grenier,J.M.P., Cartier-Michaud,A., Bardin,F.,
            Balzano,M., Goubard,A., Lissitzky,J.C., De Grandis,M.,
            Mancini,S.J.C., Serge,A. and Aurrand-Lions,M.
  TITLE     GRASP55 Is Dispensable for Normal Hematopoiesis but Necessary for
            Myc-Dependent Leukemic Growth
  JOURNAL   J Immunol 204 (10), 2685-2696 (2020)
   PUBMED   32229537
  REMARK    GeneRIF: GRASP55 Is Dispensable for Normal Hematopoiesis but
            Necessary for Myc-Dependent Leukemic Growth.
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Kim,J., Kim,H., Noh,S.H., Jang,D.G., Park,S.Y., Min,D., Kim,H.,
            Kweon,H.S., Kim,H., Aum,S., Seo,S., Choi,C.S., Kim,H., Kim,J.W.,
            Moon,S.J., Gee,H.Y. and Lee,M.G.
  TITLE     Grasp55-/- mice display impaired fat absorption and resistance to
            high-fat diet-induced obesity
  JOURNAL   Nat Commun 11 (1), 1418 (2020)
   PUBMED   32184397
  REMARK    GeneRIF: Genetic inactivation of the Golgi-resident protein GRASP55
            in mice reduces whole-body fat mass via impaired intestinal fat
            absorption and evokes resistance to high-fat diet induced body
            weight gain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Chiritoiu,M., Brouwers,N., Turacchio,G., Pirozzi,M. and Malhotra,V.
  TITLE     GRASP55 and UPR Control Interleukin-1beta Aggregation and Secretion
  JOURNAL   Dev Cell 49 (1), 145-155 (2019)
   PUBMED   30880003
  REMARK    GeneRIF: PERK inhibition, on the other hand, controls
            caspase-1-mediated conversion of proIL-1beta to mIL-1beta. These
            findings reveal translation-independent functions of PERK and
            IRE1alpha: PERK controls the production of mIL-1beta, which is then
            followed by GRASP55 and IRE1alpha activity to keep mIL-1beta in a
            secretion-competent form.
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Dupont,N., Jiang,S., Pilli,M., Ornatowski,W., Bhattacharya,D. and
            Deretic,V.
  TITLE     Autophagy-based unconventional secretory pathway for extracellular
            delivery of IL-1beta
  JOURNAL   EMBO J 30 (23), 4701-4711 (2011)
   PUBMED   22068051
  REMARK    GeneRIF: GRASP55 responds to inflammasome stimulation,controls
            autophagy initiation and important for secretion of IL-1b and IL-18
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Jiang,C.H., Tsien,J.Z., Schultz,P.G. and Hu,Y.
  TITLE     The effects of aging on gene expression in the hypothalamus and
            cortex of mice
  JOURNAL   Proc Natl Acad Sci U S A 98 (4), 1930-1934 (2001)
   PUBMED   11172053
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Shorter,J., Watson,R., Giannakou,M.E., Clarke,M., Warren,G. and
            Barr,F.A.
  TITLE     GRASP55, a second mammalian GRASP protein involved in the stacking
            of Golgi cisternae in a cell-free system
  JOURNAL   EMBO J 18 (18), 4949-4960 (1999)
   PUBMED   10487747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU707592.1 and AK169382.1.
            
            On Mar 13, 2009 this sequence version replaced NP_081628.2.
            
            Transcript Variant: This variant (1) is the protein-coding
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK167823.1, AK033413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 41.82 cM"
     Protein         1..451
                     /product="Golgi reassembly-stacking protein 2"
                     /note="golgi reassembly-stacking protein of 55 kDa"
                     /calculated_mol_wt=46907
     Region          <14..100
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          15..215
                     /region_name="GRASP.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01214"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            30
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q9R064; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            47
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q9R064; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Region          69..204
                     /region_name="GRASP55_65"
                     /note="GRASP55/65 PDZ-like domain; pfam04495"
                     /db_xref="CDD:427981"
     Region          194..199
                     /region_name="Important for membrane binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Region          236..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JX3.3)"
     Region          <248..422
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          377..451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q99JX3.3)"
     CDS             1..451
                     /gene="Gorasp2"
                     /gene_synonym="0610011A07Rik; 2410043M02Rik;
                     5730520M13Rik; 9430094F20Rik; GOLPH2; GRASP55; GRS2; p59"
                     /coded_by="NM_027352.4:190..1545"
                     /db_xref="CCDS:CCDS16109.1"
                     /db_xref="GeneID:70231"
                     /db_xref="MGI:MGI:2135962"
ORIGIN      
        1 mgssqsveip gggtegyhvl rvqenspghr aglepffdfi vsingsrlnk dndtlkdllk
       61 anvekpvkml iyssktlelr easvtpsnlw ggqgllgvsi rfcsfdgane nvwhvleves
      121 nspaalaglr phsdyiigad tvmnesedlf slietheakp lklyvyntdt dncreviitp
      181 nsawggegsl gcgigygylh riptrpfeeg kkislpgqmt gtpitplkdg ftevqlssvs
      241 ppslsppgtt gveqslsgls issappavsn vlstgvptvp llppqvnqsl asmppmnpat
      301 tlpslmplsa glpslpnlps lsnfnlpaph impgvglpel gspglpplps lpprnlpgia
      361 plpmlsdflp sfplvpegss aasageplss lpamgppsdp vmttakadas sltvdvtspa
      421 skvpttvedr vsdctpavek pvsdadasep s
//
