MACIR_MOUSE
ID MACIR_MOUSE Reviewed; 207 AA.
AC Q8VEB3; Q3UXG2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Macrophage immunometabolism regulator;
GN Name=MACIR; Synonyms=D1Ertd622e;
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=Bone marrow, Egg, Liver, and Urinary bladder;
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, and 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 TISSUE SPECIFICITY.
RX PubMed=22085962; DOI=10.1101/gad.173443.111;
RA Wright K.J., Baye L.M., Olivier-Mason A., Mukhopadhyay S., Sang L.,
RA Kwong M., Wang W., Pretorius P.R., Sheffield V.C., Sengupta P.,
RA Slusarski D.C., Jackson P.K.;
RT "An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary
RT cilium.";
RL Genes Dev. 25:2347-2360(2011).
CC -!- FUNCTION: Regulates the macrophage function, by enhancing the
CC resolution of inflammation and wound repair functions mediated by M2
CC macrophages. The regulation of macrophage function is, due at least in
CC part, to its ability to inhibit glycolysis. May also play a role in
CC trafficking of proteins via its interaction with UNC119 and UNC119B
CC cargo adapters: may help the release of UNC119 and UNC119B cargo or the
CC recycling of UNC119 and UNC119B. May play a role in ciliary membrane
CC localization via its interaction with UNC119B and protein transport
CC into photoreceptor cells. {ECO:0000250|UniProtKB:Q96GV9}.
CC -!- SUBUNIT: Interacts with UNC119 and UNC119B; interaction preferentially
CC takes place when UNC119 and UNC119B are unliganded with myristoylated
CC proteins. {ECO:0000250|UniProtKB:Q96GV9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96GV9}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q96GV9}. Note=Localizes to
CC the transition zone and proximal cilium in addition to being found
CC throughout the cytoplasm. {ECO:0000250|UniProtKB:Q96GV9}.
CC -!- TISSUE SPECIFICITY: Highly expressed in photoreceptors.
CC {ECO:0000269|PubMed:22085962}.
CC -!- SIMILARITY: Belongs to the UNC119-binding protein family.
CC {ECO:0000305}.
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DR EMBL; AK135656; BAE22601.1; -; mRNA.
DR EMBL; AK137265; BAE23288.1; -; mRNA.
DR EMBL; AK152370; BAE31160.1; -; mRNA.
DR EMBL; AK162223; BAE36800.1; -; mRNA.
DR EMBL; AK168549; BAE40424.1; -; mRNA.
DR EMBL; BC019375; AAH19375.1; -; mRNA.
DR EMBL; BC023951; AAH23951.1; -; mRNA.
DR CCDS; CCDS15202.1; -.
DR RefSeq; NP_598586.1; NM_133825.3.
DR RefSeq; XP_006529811.1; XM_006529748.3.
DR RefSeq; XP_006529812.1; XM_006529749.3.
DR RefSeq; XP_006529813.1; XM_006529750.3.
DR RefSeq; XP_006529814.1; XM_006529751.1.
DR RefSeq; XP_006529815.1; XM_006529752.1.
DR AlphaFoldDB; Q8VEB3; -.
DR STRING; 10090.ENSMUSP00000051034; -.
DR iPTMnet; Q8VEB3; -.
DR PhosphoSitePlus; Q8VEB3; -.
DR EPD; Q8VEB3; -.
DR jPOST; Q8VEB3; -.
DR MaxQB; Q8VEB3; -.
DR PaxDb; Q8VEB3; -.
DR PeptideAtlas; Q8VEB3; -.
DR PRIDE; Q8VEB3; -.
DR ProteomicsDB; 281524; -.
DR Antibodypedia; 52940; 7 antibodies from 7 providers.
DR DNASU; 52392; -.
DR Ensembl; ENSMUST00000053033; ENSMUSP00000051034; ENSMUSG00000044768.
DR Ensembl; ENSMUST00000149927; ENSMUSP00000121997; ENSMUSG00000044768.
DR Ensembl; ENSMUST00000153115; ENSMUSP00000138031; ENSMUSG00000044768.
DR GeneID; 52392; -.
DR KEGG; mmu:52392; -.
DR UCSC; uc007cfg.2; mouse.
DR CTD; 90355; -.
DR MGI; MGI:1277184; D1Ertd622e.
DR VEuPathDB; HostDB:ENSMUSG00000044768; -.
DR eggNOG; ENOG502QRGS; Eukaryota.
DR GeneTree; ENSGT00390000005782; -.
DR HOGENOM; CLU_082309_0_0_1; -.
DR InParanoid; Q8VEB3; -.
DR OMA; LHMNSNY; -.
DR OrthoDB; 1190422at2759; -.
DR PhylomeDB; Q8VEB3; -.
DR TreeFam; TF331553; -.
DR BioGRID-ORCS; 52392; 3 hits in 72 CRISPR screens.
DR ChiTaRS; D1Ertd622e; mouse.
DR PRO; PR:Q8VEB3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VEB3; protein.
DR Bgee; ENSMUSG00000044768; Expressed in granulocyte and 262 other tissues.
DR ExpressionAtlas; Q8VEB3; baseline and differential.
DR Genevisible; Q8VEB3; MM.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0010631; P:epithelial cell migration; IMP:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:MGI.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:MGI.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR029219; UNC119-bd.
DR PANTHER; PTHR31224; PTHR31224; 1.
DR Pfam; PF15435; UNC119_bdg; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Inflammatory response; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..207
FT /note="Macrophage immunometabolism regulator"
FT /id="PRO_0000316777"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96GV9"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GV9"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GV9"
FT CONFLICT 83..84
FT /note="SK -> MQ (in Ref. 1; BAE22601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 23130 MW; 6134FC92EB9A8045 CRC64;
MEVDINGDSR STLTTLPLPV AEGSSPGKAE AEKPRCSSTP CSPMRRTVSG YQILHMDSNY
LVGFTTGEEL LKLAQKCTGG EDSKGEAMPA LRAKQLDTGL ARSSRLYKTR SRYYQPYEIP
AVNGRRRRRM PSSGDKCTKP LPYEPYKALH GPLPLCLLKG KRAHSKSLDY LNLDKMNIKE
PADTEVLQYQ LQHLTLRGDR VFARNNT
