ID   NOSIP_MACFA             Reviewed;         301 AA.
AC   Q4R7H4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Nitric oxide synthase-interacting protein;
DE   AltName: Full=E3 ubiquitin-protein ligase NOSIP;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase NOSIP {ECO:0000305};
GN   Name=NOSIP; ORFNames=QtsA-15334;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that is essential for proper
CC       development of the forebrain, the eye, and the face. Catalyzes
CC       monoubiquitination of serine/threonine-protein phosphatase 2A (PP2A)
CC       catalytic subunit PPP2CA/PPP2CB (By similarity). Negatively regulates
CC       nitric oxide production by inducing NOS1 and NOS3 translocation to
CC       actin cytoskeleton and inhibiting their enzymatic activity (By
CC       similarity). {ECO:0000250|UniProtKB:Q9D6T0,
CC       ECO:0000250|UniProtKB:Q9Y314}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- SUBUNIT: Interacts with NOS1 and NOS3 (By similarity). Interacts with
CC       PP2A holoenzyme, containing PPP2CA, PPP2CB, PPP2R1A and PPP2R2A
CC       subunits (By similarity). {ECO:0000250|UniProtKB:Q9D6T0,
CC       ECO:0000250|UniProtKB:Q9Y314}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y314}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9Y314}. Note=Translocates from nucleus to
CC       cytoplasm in the G2 phase of the cell cycle.
CC       {ECO:0000250|UniProtKB:Q9Y314}.
CC   -!- DOMAIN: The U-box-like region is a truncated U-box domain. It is
CC       unknown whether it is functional or not.
CC   -!- SIMILARITY: Belongs to the NOSIP family. {ECO:0000305}.
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DR   EMBL; AB168844; BAE00948.1; -; mRNA.
DR   RefSeq; NP_001271485.1; NM_001284556.1.
DR   AlphaFoldDB; Q4R7H4; -.
DR   STRING; 9541.XP_005589983.1; -.
DR   GeneID; 102130453; -.
DR   VEuPathDB; HostDB:ENSMFAG00000031153; -.
DR   eggNOG; KOG3039; Eukaryota.
DR   OMA; AKEKRPM; -.
DR   OrthoDB; 1567031at2759; -.
DR   Proteomes; UP000233100; Chromosome 19.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR016818; NOSIP.
DR   InterPro; IPR031790; Znf-NOSIP.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13063; PTHR13063; 1.
DR   Pfam; PF15906; zf-NOSIP; 1.
DR   PIRSF; PIRSF023577; ENOS_interacting; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..301
FT                   /note="Nitric oxide synthase-interacting protein"
FT                   /id="PRO_0000280586"
FT   REGION          55..75
FT                   /note="U-box-like"
FT   REGION          131..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           78..101
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y314"
FT   MOD_RES         107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y314"
SQ   SEQUENCE   301 AA;  33143 MW;  A6A95161E5EF266C CRC64;
     MTRHGKNCTA GAVYTYHEKK KDTAASGYGT QNIRLSRDAV KDFDCCCLSL QPCHDPVVTP
     DGYLYEREAI LEYILHQKKE IARQMKAYEK QRGTRREEQK ELQRAASQDH VRGFLEKESA
     IVSRPLNPFT AKALSGTSPD NAQPGPSVGP PSKDKDKVLP SFWIPSLTPE AKATKLEKPS
     RTVTCPMSGK PLRMSDLTPV HFTPLDSSVD RVGLITRSER YVCAVTRDSL SNATPCAVLR
     PSGAVVTLEC VEKLIRKDMV DPVTGDKLTD RDIIVLQRGG TGFAGSGVKL QAEKSRPVMQ
     A