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   27-MAR-2024, entry version 121.
DE   RecName: Full=Nostrin {ECO:0000305};
DE   AltName: Full=BM247;
DE   AltName: Full=Nitric oxide synthase trafficker;
DE   AltName: Full=eNOS-trafficking inducer;
GN   Name=Nostrin {ECO:0000312|RGD:727920};
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   INTERACTION WITH DNM2.
RX   PubMed=16234328; DOI=10.1242/jcs.02620;
RA   Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W.,
RA   Schilling K.;
RT   "NOSTRIN functions as a homotrimeric adaptor protein facilitating
RT   internalization of eNOS.";
RL   J. Cell Sci. 118:5059-5069(2005).
RN   [4]
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, WASL and
CC       CAV1 (By similarity). Interacts (via SH3 domain) with DNM2; this
CC       interaction allows the recruitment of NOS3 to dynamin-positive
CC       structures (PubMed:16234328). {ECO:0000250,
CC       ECO:0000269|PubMed:16234328}.
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}.
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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; 10116-ENSRNOP00000062066; -.
DR   Ensembl; ENSRNOT00000067161.4; ENSRNOP00000062066.2; ENSRNOG00000006611.8.
DR   Ensembl; ENSRNOT00055039879; ENSRNOP00055032357; ENSRNOG00055023185.
DR   Ensembl; ENSRNOT00060005035; ENSRNOP00060003687; ENSRNOG00060003055.
DR   Ensembl; ENSRNOT00065027250; ENSRNOP00065021405; ENSRNOG00065016350.
DR   GeneID; 311111; -.
DR   KEGG; rno:311111; -.
DR   UCSC; RGD:727920; rat.
DR   AGR; RGD:727920; -.
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   OrthoDB; 5400939at2759; -.
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 cell types or tissues.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd11823; SH3_Nostrin; 1.
DR   Gene3D; 6.10.140.470; -; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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; IPR035656; Nostrin_SH3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23065:SF62; NOSTRIN, ISOFORM H; 1.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS51860; REM_1; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q5I0D6; RN.
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
//