GOLM2_MOUSE
ID GOLM2_MOUSE Reviewed; 435 AA.
AC Q6P2L7; A2AR57; Q6RZW5; Q6RZW6; Q8C4Z2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein GOLM2 {ECO:0000305};
DE AltName: Full=Cancer susceptibility candidate gene 4 protein homolog;
DE Short=CASC4;
DE AltName: Full=Golgi membrane protein 2 {ECO:0000305};
GN Name=Golm2 {ECO:0000312|MGI:MGI:2443129};
GN Synonyms=Casc4 {ECO:0000312|MGI:MGI:2443129};
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 [MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J;
RA Zhou G., Liu X., Li H.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORMS 1/2/3).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P2L7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2L7-2; Sequence=VSP_026263;
CC Name=3;
CC IsoId=Q6P2L7-3; Sequence=VSP_026263, VSP_026264, VSP_026265;
CC -!- SIMILARITY: Belongs to the GOLM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR26705.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY484583; AAR26704.1; -; mRNA.
DR EMBL; AY484585; AAR26705.1; ALT_FRAME; mRNA.
DR EMBL; AL845286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064446; AAH64446.1; -; mRNA.
DR EMBL; AK080364; BAC37891.1; -; mRNA.
DR CCDS; CCDS16650.1; -. [Q6P2L7-2]
DR CCDS; CCDS50686.1; -. [Q6P2L7-3]
DR CCDS; CCDS57183.1; -. [Q6P2L7-1]
DR RefSeq; NP_001192298.1; NM_001205369.1. [Q6P2L7-1]
DR RefSeq; NP_796028.2; NM_177054.5. [Q6P2L7-2]
DR RefSeq; NP_950239.2; NM_199038.3. [Q6P2L7-3]
DR AlphaFoldDB; Q6P2L7; -.
DR SMR; Q6P2L7; -.
DR BioGRID; 235680; 3.
DR STRING; 10090.ENSMUSP00000087357; -.
DR iPTMnet; Q6P2L7; -.
DR PhosphoSitePlus; Q6P2L7; -.
DR jPOST; Q6P2L7; -.
DR MaxQB; Q6P2L7; -.
DR PaxDb; Q6P2L7; -.
DR PeptideAtlas; Q6P2L7; -.
DR PRIDE; Q6P2L7; -.
DR ProteomicsDB; 281215; -. [Q6P2L7-1]
DR ProteomicsDB; 281216; -. [Q6P2L7-2]
DR ProteomicsDB; 281217; -. [Q6P2L7-3]
DR Antibodypedia; 55771; 89 antibodies from 18 providers.
DR DNASU; 319996; -.
DR Ensembl; ENSMUST00000078752; ENSMUSP00000077811; ENSMUSG00000060227. [Q6P2L7-1]
DR Ensembl; ENSMUST00000089912; ENSMUSP00000087357; ENSMUSG00000060227. [Q6P2L7-2]
DR Ensembl; ENSMUST00000089915; ENSMUSP00000087360; ENSMUSG00000060227. [Q6P2L7-3]
DR GeneID; 319996; -.
DR KEGG; mmu:319996; -.
DR UCSC; uc008lzr.2; mouse. [Q6P2L7-1]
DR UCSC; uc012ccu.1; mouse. [Q6P2L7-2]
DR UCSC; uc012ccv.1; mouse. [Q6P2L7-3]
DR CTD; 113201; -.
DR MGI; MGI:2443129; Golm2.
DR VEuPathDB; HostDB:ENSMUSG00000060227; -.
DR eggNOG; ENOG502QTYH; Eukaryota.
DR GeneTree; ENSGT00530000063675; -.
DR HOGENOM; CLU_052047_1_0_1; -.
DR InParanoid; Q6P2L7; -.
DR OMA; ERGPGLH; -.
DR OrthoDB; 913812at2759; -.
DR PhylomeDB; Q6P2L7; -.
DR TreeFam; TF331127; -.
DR BioGRID-ORCS; 319996; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Casc4; mouse.
DR PRO; PR:Q6P2L7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6P2L7; protein.
DR Bgee; ENSMUSG00000060227; Expressed in humerus cartilage element and 224 other tissues.
DR ExpressionAtlas; Q6P2L7; baseline and differential.
DR Genevisible; Q6P2L7; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR026141; CASC4.
DR InterPro; IPR026139; GOLM1/CASC4.
DR PANTHER; PTHR15896; PTHR15896; 1.
DR PANTHER; PTHR15896:SF7; PTHR15896:SF7; 1.
DR PRINTS; PR02084; GOLM1CASC4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Membrane; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Protein GOLM2"
FT /id="PRO_0000291844"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..435
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 191..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..194
FT /evidence="ECO:0000255"
FT COMPBIAS 191..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..420
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4E1"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4E1"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 267..299
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026263"
FT VAR_SEQ 357
FT /note="S -> N (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026264"
FT VAR_SEQ 358..413
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026265"
SQ SEQUENCE 435 AA; 49409 MW; C62F71B6B2FA7598 CRC64;
MVGFGANRRA GRLPSFVLVV LLVVIVVLAF NYWSISSRHV LLQEEVAELQ GQVQRTEVAR
GRLEKRNSDL LLLVDTHKKQ IDQKEADYGR LSSRLQAKEG LGKRCEDDKV KLQNNISYQM
ADIHHLKEQL AELRQEFLRQ EDQLQDYRKN NTYLVKRLEY ESFQCGQQIK ELRAQHEENI
KKLADQFLQE QKETHKIQSN DGKELGRNDH GAPKNIPNVP ENDANKNEDP SSNHLPHGKE
QLKRVGDAGM PGVEENDLAK VDELPAALKK PPVLASQHES HQTISHLPTG QPLSPNMAPG
SHLNQNENPS TSKQNPSNPL QHIIPGPNLD REPRIQTDTL KQATRDRAND FHKLKQSRFF
DENESPVDPQ HGSKLADYNG DDGNVGEYEA DKQAELAYNE EEDGDGGEED VQDDEERELQ
MDPADYGKQR FSDVL
