JAGN1_MOUSE
ID JAGN1_MOUSE Reviewed; 183 AA.
AC Q5XKN4; Q9CQ67; Q9CX52;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein jagunal homolog 1 {ECO:0000305};
GN Name=Jagn1 {ECO:0000312|MGI:MGI:1915017};
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;
RC TISSUE=Bone marrow, Embryo, Spinal cord, Thymus, and Wolffian duct;
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=FVB/N; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, 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).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25129145; DOI=10.1038/ng.3070;
RA Wirnsberger G., Zwolanek F., Stadlmann J., Tortola L., Liu S.W., Perlot T.,
RA Jaervinen P., Duernberger G., Kozieradzki I., Sarao R., De Martino A.,
RA Boztug K., Mechtler K., Kuchler K., Klein C., Elling U., Penninger J.M.;
RT "Jagunal homolog 1 is a critical regulator of neutrophil function in fungal
RT host defense.";
RL Nat. Genet. 46:1028-1033(2014).
CC -!- FUNCTION: Endoplasmic reticulum transmembrane protein involved in
CC vesicle-mediated transport, which is required for neutrophil function.
CC Required for vesicle-mediated transport; it is however unclear whether
CC it is involved in early secretory pathway or intracellular protein
CC transport. Acts as a regulator of neutrophil function, probably via its
CC role in vesicle-mediated transport: required for defense against fungal
CC pathogens and for granulocyte colony-stimulating factor (GM-CSF)
CC signaling pathway; possibly by regulating glycosylation and/or
CC targeting of proteins contributing to the viability and migration of
CC neutrophils. {ECO:0000269|PubMed:25129145, ECO:0000305}.
CC -!- SUBUNIT: Interacts with COPA, COPB2 and COPG2.
CC {ECO:0000250|UniProtKB:Q8N5M9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N5M9}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Lethality around embryonic day 8.5. Mice carrying
CC a hematopoietic lineage-specific deletion of Jagn1 show defects in
CC neutrophil-dependent immune response to the fungal pathogen Candida
CC albicans. Neutrophils display defects in the glycosylation of proteins
CC involved in cell adhesion and cytotoxicity as well as impaired
CC migration in response to Candida albicans infection and impaired
CC formation of cytotoxic granules. {ECO:0000269|PubMed:25129145}.
CC -!- SIMILARITY: Belongs to the jagunal family. {ECO:0000305}.
CC -!- CAUTION: Experiments in human confirm the importance of JAGN1 in
CC neutrophil function with some differences. Defects in JAGN1 cause
CC neutropenia in human, while it is not the case in mice lacking Jagn1.
CC Mutant mice show defects in neutrophil migration and increased
CC susceptibility to fungal infections due to defective killing capacity
CC of neutrophil granulocytes. {ECO:0000269|PubMed:25129145, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB32013.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK003673; BAB22929.1; -; mRNA.
DR EMBL; AK017953; BAB31017.1; -; mRNA.
DR EMBL; AK020149; BAB32013.1; ALT_FRAME; mRNA.
DR EMBL; AK141417; BAE24678.1; -; mRNA.
DR EMBL; AK151252; BAE30241.1; -; mRNA.
DR EMBL; BC011296; AAH11296.1; -; mRNA.
DR EMBL; BC025910; AAH25910.1; -; mRNA.
DR EMBL; BC037019; AAH37019.1; -; mRNA.
DR CCDS; CCDS20419.1; -.
DR RefSeq; NP_001230668.1; NM_001243739.1.
DR RefSeq; NP_080641.1; NM_026365.3.
DR AlphaFoldDB; Q5XKN4; -.
DR SMR; Q5XKN4; -.
DR BioGRID; 212427; 2.
DR STRING; 10090.ENSMUSP00000098631; -.
DR iPTMnet; Q5XKN4; -.
DR PhosphoSitePlus; Q5XKN4; -.
DR EPD; Q5XKN4; -.
DR jPOST; Q5XKN4; -.
DR MaxQB; Q5XKN4; -.
DR PaxDb; Q5XKN4; -.
DR PeptideAtlas; Q5XKN4; -.
DR PRIDE; Q5XKN4; -.
DR ProteomicsDB; 269114; -.
DR TopDownProteomics; Q5XKN4; -.
DR Antibodypedia; 59146; 67 antibodies from 16 providers.
DR DNASU; 67767; -.
DR Ensembl; ENSMUST00000101070; ENSMUSP00000098631; ENSMUSG00000051256.
DR GeneID; 67767; -.
DR KEGG; mmu:67767; -.
DR UCSC; uc009dgf.2; mouse.
DR CTD; 84522; -.
DR MGI; MGI:1915017; Jagn1.
DR VEuPathDB; HostDB:ENSMUSG00000051256; -.
DR eggNOG; KOG4054; Eukaryota.
DR GeneTree; ENSGT00390000005596; -.
DR HOGENOM; CLU_121621_0_0_1; -.
DR InParanoid; Q5XKN4; -.
DR OMA; VWRGYPY; -.
DR OrthoDB; 1452436at2759; -.
DR PhylomeDB; Q5XKN4; -.
DR TreeFam; TF313137; -.
DR BioGRID-ORCS; 67767; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Jagn1; mouse.
DR PRO; PR:Q5XKN4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q5XKN4; protein.
DR Bgee; ENSMUSG00000051256; Expressed in right kidney and 260 other tissues.
DR ExpressionAtlas; Q5XKN4; baseline and differential.
DR Genevisible; Q5XKN4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1904577; P:cellular response to tunicamycin; IEA:Ensembl.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0038158; P:granulocyte colony-stimulating factor signaling pathway; IMP:UniProtKB.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0002446; P:neutrophil mediated immunity; IMP:UniProtKB.
DR GO; GO:1990266; P:neutrophil migration; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR InterPro; IPR009787; Jagunal.
DR PANTHER; PTHR20955; PTHR20955; 1.
DR Pfam; PF07086; Jagunal; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Immunity; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..183
FT /note="Protein jagunal homolog 1"
FT /id="PRO_0000313609"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..71
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..137
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5M9"
FT CONFLICT 6
FT /note="G -> S (in Ref. 1; BAB32013)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="S -> Y (in Ref. 1; BAB32013)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="A -> D (in Ref. 1; BAB32013)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="M -> L (in Ref. 2; AAH11296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 21102 MW; BEEE51BF5E28EC23 CRC64;
MASRAGPRAA GTDGSDFQHR ERVAMHYQMS VTLKYEIKKL IYVHLVIWLL LVAKMSVGHL
RLLSHDQVAM PYQWEYPYLL SIVPSVLGLL SFPRNNISYL VLSMISMGLF SIAPLIYGSM
EMFPAAQQLY RHGKAYRFLF GFSAVSVMYL VLVLAVQVHA WQLYYSKKLL DSWFTSTQEK
KRK
