ADIP_RAT
ID ADIP_RAT Reviewed; 613 AA.
AC Q8CGZ2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Afadin- and alpha-actinin-binding protein;
DE Short=ADIP;
DE AltName: Full=Afadin DIL domain-interacting protein;
GN Name=Ssx2ip;
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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH AFIDIN AND ALPHA-ACTININ.
RC STRAIN=Sprague-Dawley;
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 TISSUE=Testis;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as a centrosome maturation factor, probably by
CC maintaining the integrity of the pericentriolar material and proper
CC microtubule nucleation at mitotic spindle poles. The function seems to
CC implicate at least in part WRAP73; the SSX2IP:WRAP73 complex is
CC proposed to act as regulator of spindle anchoring at the mitotic
CC centrosome (By similarity). Involved in cell movement: localizes at the
CC leading edge of moving cells in response to PDGF and is required for
CC the formation of the leading edge and the promotion of cell movement,
CC possibly via activation of Rac signaling (By similarity). Belongs to an
CC adhesion system, which plays a role in the organization of homotypic,
CC interneuronal and heterotypic cell-cell adherens junctions (AJs). May
CC connect the nectin-afadin and E-cadherin-catenin system through alpha-
CC actinin and may be involved in organization of the actin cytoskeleton
CC at AJs through afadin and alpha-actinin (PubMed:12446711). Involved in
CC ciliogenesis (By similarity). It is required for targeted recruitment
CC of the BBSome, CEP290, RAB8, and SSTR3 to the cilia (By similarity).
CC {ECO:0000250|UniProtKB:Q8VC66, ECO:0000250|UniProtKB:Q9Y2D8,
CC ECO:0000269|PubMed:12446711}.
CC -!- SUBUNIT: Interacts with SSX2 and SSX3 (By similarity). Does not
CC interact with SSX1 and SSX4. Interacts with VAV2 (By similarity).
CC Interacts with afadin and alpha-actinin (PubMed:12446711). Interacts
CC with WRAP73 (By similarity). {ECO:0000250|UniProtKB:Q8VC66,
CC ECO:0000269|PubMed:12446711}.
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:0000250|UniProtKB:Q9Y2D8}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9Y2D8}.
CC Note=Not found at cell-matrix AJs.
CC -!- SIMILARITY: Belongs to the ADIP family. {ECO:0000305}.
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DR EMBL; AF532970; AAO15016.1; -; mRNA.
DR EMBL; BC078687; AAH78687.1; -; mRNA.
DR RefSeq; NP_783187.1; NM_175597.3.
DR RefSeq; XP_006233516.1; XM_006233454.3.
DR RefSeq; XP_006233517.1; XM_006233455.3.
DR AlphaFoldDB; Q8CGZ2; -.
DR SMR; Q8CGZ2; -.
DR IntAct; Q8CGZ2; 1.
DR STRING; 10116.ENSRNOP00000043877; -.
DR ChEMBL; CHEMBL2176790; -.
DR iPTMnet; Q8CGZ2; -.
DR PhosphoSitePlus; Q8CGZ2; -.
DR PaxDb; Q8CGZ2; -.
DR PRIDE; Q8CGZ2; -.
DR Ensembl; ENSRNOT00000041186; ENSRNOP00000043877; ENSRNOG00000015425.
DR GeneID; 308023; -.
DR KEGG; rno:308023; -.
DR CTD; 117178; -.
DR RGD; 708490; Ssx2ip.
DR eggNOG; ENOG502QQJF; Eukaryota.
DR GeneTree; ENSGT00390000007688; -.
DR InParanoid; Q8CGZ2; -.
DR OMA; QHCKEMI; -.
DR OrthoDB; 753479at2759; -.
DR PhylomeDB; Q8CGZ2; -.
DR TreeFam; TF332889; -.
DR PRO; PR:Q8CGZ2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000015425; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q8CGZ2; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IDA:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS: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; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:RGD.
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; ISO:RGD.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:RGD.
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..613
FT /note="Afadin- and alpha-actinin-binding protein"
FT /id="PRO_0000064457"
FT REGION 361..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..595
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 MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D8"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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"
SQ SEQUENCE 613 AA; 70679 MW; 55A6174A810AB8DE CRC64;
MGDWMTVTDP VLCTENKNLS QYTSETKMSP SSLYSQQVLC SATPLSKNVH GVFSAFCTGE
NIEQSISYLD QELTTFGFPS LYEESKSKEA KRELSIVALL NCMNELLVLQ RKNLLAQESV
ETQNLKLGSD MDHLQSCYAK LKEQLEASRR EMISLQERDR QLQCKNRNLH QLLKNEKEEV
QKLQNIIASR ATQYNHDVKR KEREYNKLKE RLHQLVMNKK DKNIAMDVLN YVGRVDGKRG
SWRTDKTEAR NEDEMYKILL NDYEYRQKQI LLENAELKKV LQQMKKEMIS LLSPQKKKPR
ERAEDSTGTV VISDVEDDAG ELSRDGVWSL SCDTVREQLT NSIRKQWRIL KSHVEKLDNQ
ASKVHSEGFH EEDVISRQDH EQETEKLELE IERCKEMIKA QQQLLQQQLA TACDDDTTSL
LRDCYLLEEK ERLKEEWSLF KEQKKNFERE RRSFTEAAIR LGLERKAFEE ERASWVKQQF
LNMTTFDHQN SENVKLFSAF SGSSDPDNLI VHPRPRQKKP HSVANGVPAC TSKLAKSLPT
SPSDFCPSRS CVSEHSPVSA LTVTPEETKP NEVGRESTDQ KWSVVSRPSS REGCYGGCSS
AYTSSHVERD DLP
