NOSTN_MOUSE
ID NOSTN_MOUSE Reviewed; 506 AA.
AC Q6WKZ7; Q7TSK5; Q8BWC2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Nostrin;
DE AltName: Full=Disabled homolog 2-interacting protein 2;
DE Short=Dab2-interacting protein 2;
DE AltName: Full=Nitric oxide synthase trafficker;
DE AltName: Full=eNOS-trafficking inducer;
GN Name=Nostrin; Synonyms=Daip2;
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], INDUCTION BY RETINOIC ACID, INTERACTION WITH
RP DAB2, AND SUBCELLULAR LOCATION.
RC TISSUE=Teratocarcinoma;
RX PubMed=15596140; DOI=10.1016/j.bbrc.2004.11.079;
RA Choi Y.-J., Cho S.-Y., Kim H.-W., Kim J.-A., Bae S.-H., Park S.-S.;
RT "Cloning and characterization of mouse disabled 2-interacting protein 2, a
RT mouse orthologue of human NOSTRIN.";
RL Biochem. Biophys. Res. Commun. 326:594-599(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Opitz N.;
RT "Characterization of NOSTRIN - a novel eNOS binding protein.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-177.
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [6]
RP FUNCTION.
RX PubMed=16171775; DOI=10.1016/j.bbrc.2005.08.262;
RA Kim H.-W., Choi Y.-J., Kim J.-A., Bae S.-H., Kim K.-R., Park S.-S.;
RT "Mouse disabled 2-interacting protein 2 functions as a transcriptional
RT repressor through direct binding onto its own promoter.";
RL Biochem. Biophys. Res. Commun. 337:75-81(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, and Spleen;
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: Multivalent adapter protein which may decrease NOS3 activity
CC by inducing its translocation away from the plasma membrane.
CC {ECO:0000250, ECO:0000269|PubMed:16171775}.
CC -!- SUBUNIT: Homotrimer. Interacts with NOS3, DNM2, WASL and CAV1 (By
CC similarity). Interacts with DAB2. {ECO:0000250,
CC ECO:0000269|PubMed:15596140}.
CC -!- INTERACTION:
CC Q6WKZ7; P98078: Dab2; NbExp=2; IntAct=EBI-1391878, EBI-1391846;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IVI9};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8IVI9}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q8IVI9}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q8IVI9}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8IVI9}. Cytoplasm
CC {ECO:0000269|PubMed:15596140}. Nucleus {ECO:0000269|PubMed:15596140}.
CC Note=Enriched in selected actin structures.
CC {ECO:0000250|UniProtKB:Q8IVI9}.
CC -!- INDUCTION: In F9 cells, by retinoic acid (at protein level).
CC {ECO:0000269|PubMed:15596140}.
CC -!- DOMAIN: The SH3 domain mediates interaction with NOS3, DNM2 and WASL.
CC {ECO:0000250}.
CC -!- DOMAIN: The F-BAR domain is necessary for membrane targeting.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Seems to repress its own transcription.
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DR EMBL; AY280963; AAP32311.1; -; mRNA.
DR EMBL; AJ564264; CAD91927.1; -; mRNA.
DR EMBL; AL929221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069942; AAH69942.1; -; mRNA.
DR EMBL; AK052926; BAC35204.1; -; mRNA.
DR CCDS; CCDS16087.1; -.
DR RefSeq; NP_853525.3; NM_181547.3.
DR AlphaFoldDB; Q6WKZ7; -.
DR SMR; Q6WKZ7; -.
DR BioGRID; 236762; 4.
DR IntAct; Q6WKZ7; 3.
DR MINT; Q6WKZ7; -.
DR STRING; 10090.ENSMUSP00000036923; -.
DR iPTMnet; Q6WKZ7; -.
DR PhosphoSitePlus; Q6WKZ7; -.
DR MaxQB; Q6WKZ7; -.
DR PaxDb; Q6WKZ7; -.
DR PeptideAtlas; Q6WKZ7; -.
DR PRIDE; Q6WKZ7; -.
DR ProteomicsDB; 293942; -.
DR Antibodypedia; 47609; 205 antibodies from 27 providers.
DR DNASU; 329416; -.
DR Ensembl; ENSMUST00000041865; ENSMUSP00000036923; ENSMUSG00000034738.
DR GeneID; 329416; -.
DR KEGG; mmu:329416; -.
DR UCSC; uc008jxt.2; mouse.
DR CTD; 115677; -.
DR MGI; MGI:3606242; Nostrin.
DR VEuPathDB; HostDB:ENSMUSG00000034738; -.
DR eggNOG; KOG4429; Eukaryota.
DR GeneTree; ENSGT00510000048120; -.
DR HOGENOM; CLU_027170_1_0_1; -.
DR InParanoid; Q6WKZ7; -.
DR OMA; YSAWCHV; -.
DR OrthoDB; 445432at2759; -.
DR PhylomeDB; Q6WKZ7; -.
DR TreeFam; TF318059; -.
DR Reactome; R-MMU-203641; NOSTRIN mediated eNOS trafficking.
DR BioGRID-ORCS; 329416; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q6WKZ7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6WKZ7; protein.
DR Bgee; ENSMUSG00000034738; Expressed in interventricular septum and 101 other tissues.
DR Genevisible; Q6WKZ7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IBA:GO_Central.
DR CDD; cd11823; SH3_Nostrin; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR028535; Nostrin.
DR InterPro; IPR035656; Nostrin_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF31; PTHR14167:SF31; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endocytosis; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..506
FT /note="Nostrin"
FT /id="PRO_0000289090"
FT DOMAIN 1..260
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 292..372
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 438..497
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 413..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..230
FT /evidence="ECO:0000255"
FT COILED 305..334
FT /evidence="ECO:0000255"
FT COMPBIAS 420..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5I0D6"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CONFLICT 50
FT /note="Q -> R (in Ref. 1; AAP32311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 57673 MW; 78ADED09B493BEC4 CRC64;
MRDPLTDCSY NKVYKSLKEF AQHGDNFCKQ ITSVLQQRAN LEISYAKGLQ KLAVRLSKAL
QSTKKNCLST AWAWASESMK SAADLHQKLG KAIELEAIKP THQVLSMQEK KRKSLDNEVE
KTANLVINNW NQQIKAKKKL MMSTKKHEAL FHLVESSKQS LTQKEKQKLL NKLKKSTEKL
EKEDESYYQK NMAGYSTRLK WESTLENCYK SMLELEKERI QLLCNNLNQY SQHISLFGQT
LTTCHTQIHC AISKVDVEKD IQALMEETAI LSIENKSELL LADYFEEDPK NPMDKERRKS
LLKPKLGRLQ RDIEKASRDK EGLERKLKAL ASSSSFSDAK SQKDMETLMD ENSLKLDLLQ
ANSYKLSSVL ADLEQRPKPC HPCSTCIFKW KEKEHSHTYV KISRPLLTKR LEKAESKAPA
GGQNNPSSSP SGSTVSQASK HLCKALYTFQ ARQDDELNLE KGDIVTVHEK KEEGWWFGSL
KGKRGHFPAA YVEELPPKAG NTATQA
