SYJ2B_MOUSE
ID SYJ2B_MOUSE Reviewed; 145 AA.
AC Q9D6K5; Q2TTN6; Q6YNE6; Q78HT9; Q8K4F3; Q9D8G4;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Synaptojanin-2-binding protein {ECO:0000250|UniProtKB:P57105};
DE AltName: Full=Activin receptor-interacting protein 2 {ECO:0000303|PubMed:11882656};
DE AltName: Full=Activin receptor-interacting protein 4 {ECO:0000312|EMBL:AAT70239.1};
DE AltName: Full=Mitochondrial outer membrane protein 25 {ECO:0000250|UniProtKB:P57105};
GN Name=Synj2bp {ECO:0000312|MGI:MGI:1344347};
GN Synonyms=Arip2 {ECO:0000303|PubMed:11882656},
GN Omp25 {ECO:0000250|UniProtKB:P57105};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM43958.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, SUBUNIT, INTERACTION WITH
RP ACVR2A; ACVR2B AND RALBP1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:11882656};
RX PubMed=11882656; DOI=10.1074/jbc.m112472200;
RA Matsuzaki T., Hanai S., Kishi H., Liu Z., Bao Y., Kikuchi A., Tsuchida K.,
RA Sugino H.;
RT "Regulation of endocytosis of activin type II receptors by a novel PDZ
RT protein through Ral/Ral-binding protein 1-dependent pathway.";
RL J. Biol. Chem. 277:19008-19018(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL60065.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, AND
RP INTERACTION WITH ACVR2A.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAL60065.1};
RX PubMed=16648306; DOI=10.1677/joe.1.06420;
RA Liu Z.H., Tsuchida K., Matsuzaki T., Bao Y.L., Kurisaki A., Sugino H.;
RT "Characterization of isoforms of activin receptor-interacting protein 2
RT that augment activin signaling.";
RL J. Endocrinol. 189:409-421(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAO12271.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Tai G.X., Liu Z.H., Xu G.Y., Yang Y., Zhang P.Y.;
RT "Identification and characterization of a novel protein that interacts with
RT activin type II receptors.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAB28873.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB28873.1};
RC TISSUE=Colon {ECO:0000312|EMBL:BAC28333.1},
RC Egg {ECO:0000312|EMBL:BAE37317.1},
RC Hippocampus {ECO:0000312|EMBL:BAB28873.1}, and
RC Small intestine {ECO:0000312|EMBL:BAB25432.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH27433.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH27433.2};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH27433.2};
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 [6] {ECO:0000305}
RP INDUCTION.
RX PubMed=17907296; DOI=10.3748/wjg.v13.i41.5501;
RA Zhang H.J., Tai G.X., Zhou J., Ma D., Liu Z.H.;
RT "Regulation of activin receptor-interacting protein 2 expression in mouse
RT hepatoma Hepa1-6 cells and its relationship with collagen type IV.";
RL World J. Gastroenterol. 13:5501-5505(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Isoform 1 regulates endocytosis of activin type 2 receptor
CC kinases through the Ral/RALBP1-dependent pathway and may be involved in
CC suppression of activin-induced signal transduction. Isoform 2 and
CC isoform 3 show a stimulatory affect on activin-induced signal
CC transduction and enhance activin type 2 expression at the cell surface.
CC {ECO:0000269|PubMed:11882656, ECO:0000269|PubMed:16648306}.
CC -!- SUBUNIT: Binds (via the PDZ domain) to isoform 2A of SYNJ2 (via the
CC unique motif in the C-terminus) (By similarity). 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 (PubMed:11882656, PubMed:16648306). Interacts with
CC MAPK12 (By similarity). 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:Q9WVJ4, ECO:0000269|PubMed:11882656,
CC ECO:0000269|PubMed:16648306}.
CC -!- INTERACTION:
CC Q9D6K5; A2ARV4: Lrp2; NbExp=2; IntAct=EBI-300910, EBI-300875;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9WVJ4}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q9WVJ4}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9WVJ4}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11882656}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q9D6K5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16648306, ECO:0000269|Ref.3};
CC IsoId=Q9D6K5-2; Sequence=VSP_053102, VSP_053104;
CC Name=3 {ECO:0000269|PubMed:16648306};
CC IsoId=Q9D6K5-3; Sequence=VSP_053101, VSP_053102, VSP_053104;
CC Name=4 {ECO:0000269|PubMed:11882656};
CC IsoId=Q9D6K5-4; Sequence=VSP_053103;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed,
CC notably in brain, heart, lung, liver, kidney, skeletal muscle, ovary
CC and testis. Isoform 3 is detected only in heart, spleen and testis.
CC {ECO:0000269|PubMed:11882656, ECO:0000269|PubMed:16648306}.
CC -!- INDUCTION: Up-regulated between 12 and 24 hours after treatment with
CC activin A and lipopolysaccharide (LPS). Down-regulated by calcium
CC ionophore A23187. {ECO:0000269|PubMed:17907296}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27433.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF414433; AAM43958.1; -; mRNA.
DR EMBL; AY071903; AAL60065.1; -; mRNA.
DR EMBL; AY157057; AAO12271.1; -; mRNA.
DR EMBL; AY138960; AAN17786.1; -; mRNA.
DR EMBL; AY566156; AAT70239.1; -; mRNA.
DR EMBL; AK008054; BAB25432.1; -; mRNA.
DR EMBL; AK013474; BAB28873.1; -; mRNA.
DR EMBL; AK033514; BAC28333.1; -; mRNA.
DR EMBL; AK163362; BAE37317.1; -; mRNA.
DR EMBL; BC027433; AAH27433.2; ALT_INIT; mRNA.
DR CCDS; CCDS26021.1; -. [Q9D6K5-1]
DR CCDS; CCDS83979.1; -. [Q9D6K5-2]
DR RefSeq; NP_001296743.1; NM_001309814.1. [Q9D6K5-2]
DR RefSeq; NP_001296777.1; NM_001309848.1. [Q9D6K5-4]
DR RefSeq; NP_079568.1; NM_025292.7. [Q9D6K5-1]
DR AlphaFoldDB; Q9D6K5; -.
DR SMR; Q9D6K5; -.
DR BioGRID; 204883; 1.
DR IntAct; Q9D6K5; 4.
DR STRING; 10090.ENSMUSP00000129224; -.
DR iPTMnet; Q9D6K5; -.
DR PhosphoSitePlus; Q9D6K5; -.
DR EPD; Q9D6K5; -.
DR jPOST; Q9D6K5; -.
DR MaxQB; Q9D6K5; -.
DR PaxDb; Q9D6K5; -.
DR PeptideAtlas; Q9D6K5; -.
DR PRIDE; Q9D6K5; -.
DR ProteomicsDB; 254835; -. [Q9D6K5-1]
DR ProteomicsDB; 254836; -. [Q9D6K5-2]
DR ProteomicsDB; 254837; -. [Q9D6K5-3]
DR DNASU; 24071; -.
DR Ensembl; ENSMUST00000114201; ENSMUSP00000109839; ENSMUSG00000090935. [Q9D6K5-3]
DR Ensembl; ENSMUST00000163402; ENSMUSP00000129224; ENSMUSG00000090935. [Q9D6K5-1]
DR Ensembl; ENSMUST00000164386; ENSMUSP00000132941; ENSMUSG00000021139. [Q9D6K5-4]
DR Ensembl; ENSMUST00000169158; ENSMUSP00000130691; ENSMUSG00000090935. [Q9D6K5-2]
DR GeneID; 105940408; -.
DR GeneID; 24071; -.
DR KEGG; mmu:105940408; -.
DR KEGG; mmu:24071; -.
DR UCSC; uc007oca.1; mouse. [Q9D6K5-4]
DR UCSC; uc007och.2; mouse. [Q9D6K5-1]
DR UCSC; uc007ocj.2; mouse. [Q9D6K5-2]
DR CTD; 55333; -.
DR MGI; MGI:1344347; Synj2bp.
DR VEuPathDB; HostDB:ENSMUSG00000021139; -.
DR VEuPathDB; HostDB:ENSMUSG00000090935; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00830000128402; -.
DR HOGENOM; CLU_149433_1_0_1; -.
DR InParanoid; Q9D6K5; -.
DR OMA; CKIKENG; -.
DR OrthoDB; 1333715at2759; -.
DR PhylomeDB; Q9D6K5; -.
DR TreeFam; TF318964; -.
DR BioGRID-ORCS; 105940408; 0 hits in 2 CRISPR screens.
DR BioGRID-ORCS; 24071; 5 hits in 71 CRISPR screens.
DR PRO; PR:Q9D6K5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9D6K5; protein.
DR Bgee; ENSMUSG00000021139; Expressed in spermatid and 63 other tissues.
DR ExpressionAtlas; Q9D6K5; baseline and differential.
DR Genevisible; Q9D6K5; MM.
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; IDA:UniProtKB.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0070699; F:type II activin receptor binding; IPI:UniProtKB.
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:0007028; P:cytoplasm organization; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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; IEA:Ensembl.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IDA:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
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 Alternative splicing; Cytoplasm; Endocytosis; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..145
FT /note="Synaptojanin-2-binding protein"
FT /id="PRO_0000375982"
FT TOPO_DOM 1..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical; Anchor for type IV membrane protein"
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"
FT VAR_SEQ 1..20
FT /note="MNGRVDYLVTEEEINLTRGP -> MIF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16648306"
FT /id="VSP_053101"
FT VAR_SEQ 100..118
FT /note="LPVQNGPIVHRGEGEPSGV -> VGITCTWIWDSRLLHCSCE (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16648306, ECO:0000303|Ref.3"
FT /id="VSP_053102"
FT VAR_SEQ 101..145
FT /note="PVQNGPIVHRGEGEPSGVPVAMVLLPVFALTMVAVWAFVRYRKQL -> LVV
FT GGSFGLREFSQIRYDAVTIKIDPELEKKLKVNKITLESEYERLLCLLCRQ (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:11882656,
FT ECO:0000303|PubMed:16648306"
FT /id="VSP_053103"
FT VAR_SEQ 119..145
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16648306, ECO:0000303|Ref.3"
FT /id="VSP_053104"
FT CONFLICT 34
FT /note="Q -> E (in Ref. 4; BAB25432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 15815 MW; BB40BB0114084F67 CRC64;
MNGRVDYLVT EEEINLTRGP SGLGFNIVGG TDQQYVSNDS GIYVSRIKED GAAAQDGRLQ
EGDKILSVNG QDLKNLLHQD AVDLFRNAGC AVSLRVQHRL PVQNGPIVHR GEGEPSGVPV
AMVLLPVFAL TMVAVWAFVR YRKQL
