ID   NOSTN_BOVIN             Reviewed;         505 AA.
AC   Q2KJB5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Nostrin;
DE   AltName: Full=Nitric oxide synthase trafficker;
DE   AltName: Full=eNOS trafficking inducer;
GN   Name=NOSTRIN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17071725; DOI=10.1152/ajpheart.00990.2006;
RA   Mukhopadhyay S., Xu F., Sehgal P.B.;
RT   "Aberrant cytoplasmic sequestration of eNOS in endothelial cells after
RT   monocrotaline, hypoxia, and senescence: live-cell caveolar and cytoplasmic
RT   NO imaging.";
RL   Am. J. Physiol. 292:H1373-H1389(2007).
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:0000269|PubMed:17071725}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q8IVI9}. Note=Enriched in selected actin
CC       structures. {ECO:0000250|UniProtKB:Q8IVI9}.
CC   -!- TISSUE SPECIFICITY: Present in pulmonary arterial endothelial cells (at
CC       protein level). {ECO:0000269|PubMed:17071725}.
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; BC105426; AAI05427.1; -; mRNA.
DR   RefSeq; NP_001039722.1; NM_001046257.2.
DR   AlphaFoldDB; Q2KJB5; -.
DR   SMR; Q2KJB5; -.
DR   STRING; 9913.ENSBTAP00000013682; -.
DR   PaxDb; Q2KJB5; -.
DR   PRIDE; Q2KJB5; -.
DR   GeneID; 521834; -.
DR   KEGG; bta:521834; -.
DR   CTD; 115677; -.
DR   eggNOG; KOG4429; Eukaryota.
DR   InParanoid; Q2KJB5; -.
DR   OrthoDB; 445432at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IBA:GO_Central.
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; IPR036274; HR1_rpt_sf.
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; SSF46585; SSF46585; 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; Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..505
FT                   /note="Nostrin"
FT                   /id="PRO_0000289088"
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          437..496
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   COILED          101..128
FT                   /evidence="ECO:0000255"
FT   COILED          160..222
FT                   /evidence="ECO:0000255"
FT   COILED          295..332
FT                   /evidence="ECO:0000255"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5I0D6"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6WKZ7"
SQ   SEQUENCE   505 AA;  57307 MW;  3EE984572780623B CRC64;
     MRDPLTDCSY NKVYKNLKEF SQNGEDFCKQ ITSILQQRAN LEINYAKGLQ KLATKLSKTL
     QSAKKNCLVS AWAWVSEGMK SAGDLHQKLG KAIELEAIKP AHQVLSAHEK KRKSLENEVE
     KTANLVISNW NQQIKAKKKL MVSTKKHEAL FHLVESSKQI TTEKEKQKLL NKLKKSTEKL
     SKEDENYYQK NVASCSTRLK WENTLENCFQ SILELEKERI QLLCNNLNQY SQHISVFGQT
     LTTCHTQIHC AISKIDIEKD IQALMEETTV SSTENKSEFL LTDYFEEDPK NAMSKERQTS
     SIKSKLLRLQ KDIEKASRDQ EGLERMLRAY SSHSSFSDSE SKKSTAALMD ENSLKLDLLQ
     ANSYKLSSVL AELEQRPQPN HPCSNSIFKW KEKQTHSSVK ISRPVLMKRL ENVVNRASSD
     GQRIPSPSST ASGVTQLGNG LCKALYPFQA RQDDELDLEK GDIVTIHKKK DEGWWFGSLK
     GKKGHFPAAY VEELPLNAGD TASQA