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GOLI4_MOUSE
ID   GOLI4_MOUSE             Reviewed;         655 AA.
AC   Q8BXA1; Q8BWP9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Golgi integral membrane protein 4;
DE   AltName: Full=Decapacitation factor 10;
DE   AltName: Full=Golgi phosphoprotein 4;
GN   Name=Golim4; Synonyms=Df10, Golph4;
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].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Liver;
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].
RC   STRAIN=C57BL/6J; TISSUE=Fetal 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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=16221991; DOI=10.1095/biolreprod.105.044644;
RA   Nixon B., MacIntyre D.A., Mitchell L.A., Gibbs G.M., O'Bryan M.,
RA   Aitken R.J.;
RT   "The identification of mouse sperm-surface-associated proteins and
RT   characterization of their ability to act as decapacitation factors.";
RL   Biol. Reprod. 74:275-287(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-633, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
RC   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   -!- FUNCTION: Plays a role in endosome to Golgi protein trafficking;
CC       mediates protein transport along the late endosome-bypass pathway from
CC       the early endosome to the Golgi. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC       Endosome membrane {ECO:0000250}; Single-pass type II membrane protein
CC       {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:O00461}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:O00461}. Note=Localizes to cis and medial Golgi
CC       cisternae. Probably cycles between early Golgi and distal compartments
CC       like endosome (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by spermatozoa (at protein level).
CC       {ECO:0000269|PubMed:16221991}.
CC   -!- PTM: Phosphorylated by c-AMP-dependent kinases most probably in its
CC       lumenal part. {ECO:0000250}.
CC   -!- PTM: O-glycosylated; modified by sialic acid residues. {ECO:0000250}.
CC   -!- PTM: N-glycosylated; N-glycans are of the complex type and modified by
CC       sialic acid residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GOLIM4 family. {ECO:0000305}.
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DR   EMBL; AK048434; BAC33335.1; -; mRNA.
DR   EMBL; AK050346; BAC34202.1; -; mRNA.
DR   EMBL; BC086642; AAH86642.1; -; mRNA.
DR   EMBL; BC089354; AAH89354.1; -; mRNA.
DR   CCDS; CCDS17416.1; -.
DR   RefSeq; NP_780402.1; NM_175193.6.
DR   AlphaFoldDB; Q8BXA1; -.
DR   SMR; Q8BXA1; -.
DR   BioGRID; 215783; 2.
DR   STRING; 10090.ENSMUSP00000048997; -.
DR   GlyGen; Q8BXA1; 1 site.
DR   iPTMnet; Q8BXA1; -.
DR   PhosphoSitePlus; Q8BXA1; -.
DR   SwissPalm; Q8BXA1; -.
DR   CPTAC; non-CPTAC-4030; -.
DR   EPD; Q8BXA1; -.
DR   jPOST; Q8BXA1; -.
DR   MaxQB; Q8BXA1; -.
DR   PaxDb; Q8BXA1; -.
DR   PeptideAtlas; Q8BXA1; -.
DR   PRIDE; Q8BXA1; -.
DR   ProteomicsDB; 267646; -.
DR   Antibodypedia; 952; 126 antibodies from 20 providers.
DR   DNASU; 73124; -.
DR   Ensembl; ENSMUST00000038563; ENSMUSP00000048997; ENSMUSG00000034109.
DR   Ensembl; ENSMUST00000167078; ENSMUSP00000132910; ENSMUSG00000034109.
DR   GeneID; 73124; -.
DR   KEGG; mmu:73124; -.
DR   UCSC; uc008pnf.2; mouse.
DR   CTD; 27333; -.
DR   MGI; MGI:1920374; Golim4.
DR   VEuPathDB; HostDB:ENSMUSG00000034109; -.
DR   eggNOG; ENOG502R4Q5; Eukaryota.
DR   GeneTree; ENSGT00390000004096; -.
DR   InParanoid; Q8BXA1; -.
DR   PhylomeDB; Q8BXA1; -.
DR   TreeFam; TF333101; -.
DR   BioGRID-ORCS; 73124; 5 hits in 74 CRISPR screens.
DR   ChiTaRS; Golim4; mouse.
DR   PRO; PR:Q8BXA1; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8BXA1; protein.
DR   Bgee; ENSMUSG00000034109; Expressed in vault of skull and 250 other tissues.
DR   ExpressionAtlas; Q8BXA1; baseline and differential.
DR   Genevisible; Q8BXA1; MM.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR   InterPro; IPR042336; GOLIM4.
DR   PANTHER; PTHR22909; PTHR22909; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Endosome; Glycoprotein; Golgi apparatus; Lipoprotein;
KW   Membrane; Myristate; Phosphoprotein; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O00461"
FT   CHAIN           2..655
FT                   /note="Golgi integral membrane protein 4"
FT                   /id="PRO_0000285098"
FT   TOPO_DOM        2..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..655
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          38..107
FT                   /note="Golgi targeting"
FT                   /evidence="ECO:0000250"
FT   REGION          80..175
FT                   /note="Endosome targeting"
FT                   /evidence="ECO:0000250"
FT   REGION          122..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..220
FT                   /note="Golgi targeting"
FT                   /evidence="ECO:0000250"
FT   REGION          256..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          66..216
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        258..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..536
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..586
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00461"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5BJK8"
FT   MOD_RES         576
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O00461"
FT   MOD_RES         589
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O00461"
FT   MOD_RES         633
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:O00461"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   655 AA;  76785 MW;  273CD26423D05CA7 CRC64;
     MGNGMCSRKQ KRIFQTLLLL TVVFGFLYGA MLYLELQTQL RKAEAVALKY QQHQDSLSAQ
     LQVVYEHRSR LEKSLQKERL EHKKAKEDFL VYKLEAQETL NKGRQDSNSR YSALNVQHQM
     LKSQHEELRK QHSDLEEEHR KQGEDFSRTF NDHKQRYLQL QQEKEQELSK LKETVYNLRE
     ENRQLRKAHQ DIHTQLQDVK TQVAEYKQLK DTLNRIPSFR NPDPVEQQNV TFPHGTHPPQ
     GYNGREKLTG ELQEVQPNHE AGPRRMEEKP LSSMQKDAGF QALEEQNQVE PREPEERQVE
     EEHRKALEEE EMEQVGQAEH LEEEHDPSPE EQDRDWRDQQ GQNAAHLLDG HPQAEVEHST
     KAATNFQSPY EEQLEQQRLA ARRDEEAQRL REHQEALHQQ RLHGQLLRQQ QQQQFLAREM
     AQQKQVAHED GQQQHQEQLR QQAHYNAVEN DIAQGVEDQG IPEEEGGAYD RDNQRQDEAE
     GDPGNRQELR EPGHQEGDPE VEADRAAVED INPADDPNNQ GEDEFEEAEQ VREENLPEES
     EEQKQSEAKQ GNVEMDEHLV MAGNPDQQED NVDEQYQDEG EEEVQEDLTE EKKREMEHNV
     EETYGEHPDD KNNDGEEQGV HNRAHPKGRQ EHYEEEEDEE DGAAVAEKSH RRAEM
 
 
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