NOSTN_RAT
ID NOSTN_RAT Reviewed; 502 AA.
AC Q5I0D6; Q923J7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Nostrin;
DE AltName: Full=BM247;
DE AltName: Full=Nitric oxide synthase trafficker;
DE AltName: Full=eNOS-trafficking inducer;
GN Name=Nostrin;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-143, AND TISSUE SPECIFICITY.
RC STRAIN=SHRSP;
RX PubMed=11489260; DOI=10.1016/s0006-8993(01)02670-1;
RA Kirsch T., Wellner M., Luft F.C., Haller H., Lippoldt A.;
RT "Altered gene expression in cerebral capillaries of stroke-prone
RT spontaneously hypertensive rats.";
RL Brain Res. 910:106-115(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Multivalent adapter protein which may decrease NOS3 activity
CC by inducing its translocation away from the plasma membrane.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Interacts with DAB2. Interacts with NOS3, DNM2,
CC WASL and CAV1 (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q6WKZ7}. Nucleus {ECO:0000250|UniProtKB:Q6WKZ7}.
CC Note=Enriched in selected actin structures.
CC {ECO:0000250|UniProtKB:Q8IVI9}.
CC -!- TISSUE SPECIFICITY: Over-expressed in brain microcapillaries from
CC spontaneously hypertensive rats. {ECO:0000269|PubMed:11489260}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC088446; AAH88446.1; -; mRNA.
DR EMBL; AY032855; AAK64518.1; -; mRNA.
DR RefSeq; NP_001019431.1; NM_001024260.1.
DR AlphaFoldDB; Q5I0D6; -.
DR SMR; Q5I0D6; -.
DR STRING; 10116.ENSRNOP00000062066; -.
DR iPTMnet; Q5I0D6; -.
DR PhosphoSitePlus; Q5I0D6; -.
DR PaxDb; Q5I0D6; -.
DR PRIDE; Q5I0D6; -.
DR Ensembl; ENSRNOT00000067161; ENSRNOP00000062066; ENSRNOG00000006611.
DR GeneID; 311111; -.
DR KEGG; rno:311111; -.
DR UCSC; RGD:727920; rat.
DR CTD; 115677; -.
DR RGD; 727920; Nostrin.
DR eggNOG; KOG4429; Eukaryota.
DR GeneTree; ENSGT00510000048120; -.
DR HOGENOM; CLU_027170_1_0_1; -.
DR InParanoid; Q5I0D6; -.
DR OMA; YSAWCHV; -.
DR OrthoDB; 445432at2759; -.
DR PhylomeDB; Q5I0D6; -.
DR Reactome; R-RNO-203641; NOSTRIN mediated eNOS trafficking.
DR PRO; PR:Q5I0D6; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006611; Expressed in lung and 18 other tissues.
DR Genevisible; Q5I0D6; RN.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
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; SM00055; FCH; 1.
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..502
FT /note="Nostrin"
FT /id="PRO_0000289091"
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..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..230
FT /evidence="ECO:0000255"
FT COILED 305..335
FT /evidence="ECO:0000255"
FT COMPBIAS 420..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ7"
SQ SEQUENCE 502 AA; 57352 MW; DE8944D1939CCC4C CRC64;
MRDPLTDCSY NKVYKSLKEF AQNGDNFCKQ ITSVLQQRAN LEISYAKGLQ KLAVKLSKAL
QSTKKNCLST AWAWASESMK SAADLHQKLG KAIELEAIKP THQVLSMQEK KRKSLDNEVE
KSANLVINNW NQQIKAKKKL MMSTKKHEAL FHLIESSKQS MTQKEKQKLL NKLKKSTEKL
EKEDESYYQK NMAGYSTRLK WESTLEKCYK SMLELEKERI QLLCNNLNQY SQHISLFGQT
LTTCHTQIHC AISKVDVEKD IQALMEETAV LSLENKSELL LADYFEEDPK NPMDKERRKS
LIKPKLWRLQ KDIEKASRDK EGLEQKLKAL ASSASFSDAK SQKDAETLMD ENSLKLDLLQ
ANSYKLSTVL ADLEQRPKPC HPCSNCIFKW KEKEHSHSYV KISRPLLTKR LEKAESKAPA
GEQNNPSSSR PGSSVSQGNN QLCKALYTFQ ARQDDELNLE KGDIVTIHEK KEEGWWFGSL
NGKKGHFPAA YVEELPPKAG QA
