SYJ2B_RAT
ID SYJ2B_RAT Reviewed; 145 AA.
AC Q9WVJ4; A0JN00;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Synaptojanin-2-binding protein;
DE AltName: Full=Mitochondrial outer membrane protein 25;
DE AltName: Full=NPW16;
GN Name=Synj2bp; Synonyms=Omp25;
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 [MRNA], INTERACTION WITH SYNJ2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10357812; DOI=10.1093/emboj/18.11.2991;
RA Nemoto Y., De Camilli P.;
RT "Recruitment of an alternatively spliced form of synaptojanin 2 to
RT mitochondria by the interaction with the PDZ domain of a mitochondrial
RT outer membrane protein.";
RL EMBO J. 18:2991-3006(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Jin W., Wang Y., Yang H., Liao B., Ju G.;
RT "Production and characterization of monoclonal antibodies against NPW16: a
RT novel PDZ protein.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [4]
RP INTERACTION WITH MAPK12.
RX PubMed=15878399; DOI=10.1016/j.bbamcr.2004.11.008;
RA Court N.W., Ingley E., Klinken S.P., Bogoyevitch M.A.;
RT "Outer membrane protein 25-a mitochondrial anchor and inhibitor of stress-
RT activated protein kinase-3.";
RL Biochim. Biophys. Acta 1744:68-75(2005).
CC -!- FUNCTION: Regulates endocytosis of activin type 2 receptor kinases
CC through the Ral/RALBP1-dependent pathway and may be involved in
CC suppression of activin-induced signal transduction.
CC {ECO:0000250|UniProtKB:Q9D6K5}.
CC -!- SUBUNIT: Binds (via the PDZ domain) to isoform 2A of SYNJ2 (via the
CC unique motif in the C-terminus) (PubMed:10357812). Interacts (via C-
CC terminus) with RALBP1. Interacts (via PDZ domain) with ACVR2A (via C-
CC terminus) and ACVR2B (via C-terminus). Forms a ternary complex with
CC ACVR2A and RALBP1 (By similarity). Interacts with MAPK12
CC (PubMed:15878399). Interacts with DLL1; enhances DLL1 protein
CC stability, and promotes notch signaling in endothelial cells (By
CC similarity). {ECO:0000250|UniProtKB:P57105,
CC ECO:0000250|UniProtKB:Q9D6K5, ECO:0000269|PubMed:10357812,
CC ECO:0000269|PubMed:15878399}.
CC -!- INTERACTION:
CC Q9WVJ4; O55207-3: Synj2; NbExp=9; IntAct=EBI-7007454, EBI-7007476;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10357812}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39893.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; AF107295; AAD39893.1; ALT_SEQ; mRNA.
DR EMBL; AF260258; AAF70306.1; -; mRNA.
DR EMBL; BC126067; AAI26068.2; -; mRNA.
DR RefSeq; NP_072121.2; NM_022599.2.
DR AlphaFoldDB; Q9WVJ4; -.
DR SMR; Q9WVJ4; -.
DR BioGRID; 249115; 1.
DR ELM; Q9WVJ4; -.
DR IntAct; Q9WVJ4; 3.
DR MINT; Q9WVJ4; -.
DR STRING; 10116.ENSRNOP00000009119; -.
DR iPTMnet; Q9WVJ4; -.
DR PhosphoSitePlus; Q9WVJ4; -.
DR jPOST; Q9WVJ4; -.
DR PaxDb; Q9WVJ4; -.
DR PRIDE; Q9WVJ4; -.
DR Ensembl; ENSRNOT00000009122; ENSRNOP00000009119; ENSRNOG00000006399.
DR GeneID; 64531; -.
DR KEGG; rno:64531; -.
DR UCSC; RGD:69400; rat.
DR CTD; 55333; -.
DR RGD; 69400; Synj2bp.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00830000128402; -.
DR HOGENOM; CLU_149433_1_0_1; -.
DR InParanoid; Q9WVJ4; -.
DR OMA; WILLRYR; -.
DR OrthoDB; 1502481at2759; -.
DR PRO; PR:Q9WVJ4; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000006399; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; Q9WVJ4; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0070699; F:type II activin receptor binding; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IDA:RGD.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; ISO:RGD.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:RGD.
DR GO; GO:0006605; P:protein targeting; ISO:RGD.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..145
FT /note="Synaptojanin-2-binding protein"
FT /id="PRO_0000072384"
FT TOPO_DOM 1..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..145
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 13..100
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
SQ SEQUENCE 145 AA; 15825 MW; 846CD232A73FE266 CRC64;
MNGRVDYLVS EEEINLTRGP SGLGFNIVGG TDQQYVSNDS GIYVSRIKED GAAARDGRLQ
EGDKILSVNG QDLKNLLHQD AVDLFRNAGY AVSLRVQHRL PVQNGPIVHR GDGEPSGVPV
AVVLLPVFAL TLVAVWAFVR YRKQL