ADIP_MOUSE
ID ADIP_MOUSE Reviewed; 615 AA.
AC Q8VC66; Q8BG59; Q8C7X0; Q8K2F7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Afadin- and alpha-actinin-binding protein;
DE Short=ADIP;
DE AltName: Full=Afadin DIL domain-interacting protein;
GN Name=Ssx2ip;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH AFIDIN AND ALPHA-ACTININ, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12446711; DOI=10.1074/jbc.m209832200;
RA Asada M., Irie K., Morimoto K., Yamada A., Ikeda W., Takeuchi M., Takai Y.;
RT "ADIP, a novel afadin- and alpha-actinin-binding protein localized at cell-
RT cell adherens junctions.";
RL J. Biol. Chem. 278:4103-4111(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313 AND SER-319, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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).
RN [5]
RP FUNCTION, AND INTERACTION WITH VAV2.
RX PubMed=22027834; DOI=10.1074/jbc.m111.308858;
RA Fukumoto Y., Kurita S., Takai Y., Ogita H.;
RT "Role of scaffold protein afadin dilute domain-interacting protein (ADIP)
RT in platelet-derived growth factor-induced cell movement by activating Rac
RT protein through Vav2 protein.";
RL J. Biol. Chem. 286:43537-43548(2011).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PCM1.
RX PubMed=24356449; DOI=10.1091/mbc.e13-09-0526;
RA Klinger M., Wang W., Kuhns S., Baerenz F., Draeger-Meurer S., Pereira G.,
RA Gruss O.J.;
RT "The novel centriolar satellite protein SSX2IP targets Cep290 to the
RT ciliary transition zone.";
RL Mol. Biol. Cell 25:495-507(2014).
CC -!- FUNCTION: Belongs to an adhesion system, which plays a role in the
CC organization of homotypic, interneuronal and heterotypic cell-cell
CC adherens junctions (AJs). May connect the nectin-afadin and E-cadherin-
CC catenin system through alpha-actinin and may be involved in
CC organization of the actin cytoskeleton at AJs through afadin and alpha-
CC actinin (PubMed:12446711). Acts as a centrosome maturation factor,
CC probably by maintaining the integrity of the pericentriolar material
CC and proper microtubule nucleation at mitotic spindle poles. The
CC function seems to implicate at least in part WRAP73; the SSX2IP:WRAP73
CC complex is proposed to act as regulator of spindle anchoring at the
CC mitotic centrosome (By similarity). Involved in cell movement:
CC localizes at the leading edge of moving cells in response to PDGF and
CC is required for the formation of the leading edge and the promotion of
CC cell movement, possibly via activation of Rac signaling
CC (PubMed:22027834). Involved in ciliogenesis (By similarity). It is
CC required for targeted recruitment of the BBSome, CEP290, RAB8, and
CC SSTR3 to the cilia (By similarity). {ECO:0000250|UniProtKB:Q9Y2D8,
CC ECO:0000269|PubMed:12446711, ECO:0000269|PubMed:22027834}.
CC -!- SUBUNIT: Interacts with SSX2 and SSX3 (By similarity). Does not
CC interact with SSX1 and SSX4 (By similarity). Interacts with afadin and
CC alpha-actinin (PubMed:12446711). Interacts with VAV2 (PubMed:22027834).
CC Interacts with PCM1 (PubMed:24356449). Interacts with WRAP73 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y2D8,
CC ECO:0000269|PubMed:12446711, ECO:0000269|PubMed:22027834,
CC ECO:0000269|PubMed:24356449}.
CC -!- INTERACTION:
CC Q8VC66; P12814: ACTN1; Xeno; NbExp=3; IntAct=EBI-6654049, EBI-351710;
CC Q8VC66; O35889: Afdn; Xeno; NbExp=4; IntAct=EBI-6654049, EBI-6654073;
CC Q8VC66; Q9P2S5: WRAP73; Xeno; NbExp=4; IntAct=EBI-6654049, EBI-1054904;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:12446711}. Nucleus {ECO:0000250|UniProtKB:Q9Y2D8}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite {ECO:0000269|PubMed:24356449}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:24356449}. Note=Not
CC found at cell-matrix AJs.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12446711}.
CC -!- SIMILARITY: Belongs to the ADIP family. {ECO:0000305}.
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DR EMBL; AF532969; AAO15015.1; -; mRNA.
DR EMBL; AK049080; BAC33536.1; -; mRNA.
DR EMBL; AK031356; BAC27363.1; -; mRNA.
DR EMBL; AK043865; BAC31684.1; -; mRNA.
DR EMBL; BC021749; AAH21749.1; -; mRNA.
DR EMBL; BC031527; AAH31527.1; -; mRNA.
DR CCDS; CCDS38665.1; -.
DR RefSeq; NP_001240697.1; NM_001253768.1.
DR RefSeq; NP_001240698.1; NM_001253769.1.
DR RefSeq; NP_001240699.1; NM_001253770.1.
DR RefSeq; NP_620083.1; NM_138744.3.
DR RefSeq; XP_006502467.1; XM_006502404.3.
DR RefSeq; XP_006502468.1; XM_006502405.3.
DR RefSeq; XP_006502469.1; XM_006502406.3.
DR AlphaFoldDB; Q8VC66; -.
DR SMR; Q8VC66; -.
DR IntAct; Q8VC66; 7.
DR STRING; 10090.ENSMUSP00000101759; -.
DR iPTMnet; Q8VC66; -.
DR PhosphoSitePlus; Q8VC66; -.
DR MaxQB; Q8VC66; -.
DR PaxDb; Q8VC66; -.
DR PRIDE; Q8VC66; -.
DR ProteomicsDB; 285726; -.
DR Antibodypedia; 19778; 235 antibodies from 30 providers.
DR DNASU; 99167; -.
DR Ensembl; ENSMUST00000106153; ENSMUSP00000101759; ENSMUSG00000036825.
DR GeneID; 99167; -.
DR KEGG; mmu:99167; -.
DR UCSC; uc008rrb.1; mouse.
DR CTD; 117178; -.
DR MGI; MGI:2139150; Ssx2ip.
DR VEuPathDB; HostDB:ENSMUSG00000036825; -.
DR eggNOG; ENOG502QQJF; Eukaryota.
DR GeneTree; ENSGT00390000007688; -.
DR HOGENOM; CLU_031049_0_0_1; -.
DR InParanoid; Q8VC66; -.
DR OMA; QHCKEMI; -.
DR OrthoDB; 753479at2759; -.
DR TreeFam; TF332889; -.
DR BioGRID-ORCS; 99167; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ssx2ip; mouse.
DR PRO; PR:Q8VC66; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VC66; protein.
DR Bgee; ENSMUSG00000036825; Expressed in ileal epithelium and 259 other tissues.
DR ExpressionAtlas; Q8VC66; baseline and differential.
DR Genevisible; Q8VC66; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; ISS:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; IMP:MGI.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IMP:MGI.
DR InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR Pfam; PF11559; ADIP; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..615
FT /note="Afadin- and alpha-actinin-binding protein"
FT /id="PRO_0000064456"
FT REGION 293..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..227
FT /evidence="ECO:0000255"
FT COILED 266..293
FT /evidence="ECO:0000255"
FT COILED 375..461
FT /evidence="ECO:0000255"
FT COMPBIAS 293..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D8"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D8"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D8"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D8"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D8"
FT CONFLICT 47
FT /note="K -> R (in Ref. 3; AAH31527)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="Missing (in Ref. 2; BAC33536/BAC27363)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="S -> SKPG (in Ref. 2; BAC33536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 70956 MW; CC41D7078591919F CRC64;
MGDWMTVTDP VLCTENKNLS QYTSETKMSP SSLYSQQVLC SSVPLSKNVH GVFGVFCTGE
NIEQSISYLD QELTTFGFPS LYEESKSKEA KRELNIVAVL NCMNELLVLQ RKNLLAQESV
ETQNLKLGSD MDHLQSCYAK LKEQLETSRR EMIGLQERDR QLQCKNRSLH QLLKNEKDEV
QKLQNIIASR ATQYNHDVKR KEREYNKLKE RLHQLVMNKK DKNIAMDVLN YVGRADGKRG
SWRTDKTEAR NEDEMYKILL NDYEYRQKQI LMENAELKKV LQQMKKEMIS LLSPQKKKPR
ERAEDGTGTV AISDIEDDSG ELSRDSVWGL SCDTVREQLT NSIRKQWRIL KSHVEKLDNQ
ASKVHSEGLN EEDVISRQDH EQETEKLELE IERCKEMIKA QQQLLQQQLA TTCDDDTTSL
LRDCYLLEEK ERLKEEWTLF KEQKKNFERE RRSFTEAAIR LGLERKAFEE ERASWVKQQF
LNMTNFDHQN SENVKLFSAF SGSSDPDNLI VHSRPRQKKL HSVANGVPAC TSKLTKSLPA
SPSTSDFRQT HSCVSEHSSI SVLNITPEES KPSEVAREST DQKWSVQSRP SSREGCYSGC
SSAFRSAHGD RDDLP
