ADIPA_XENLA
ID ADIPA_XENLA Reviewed; 554 AA.
AC Q6NRK1;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Afadin- and alpha-actinin-binding protein A;
DE Short=ADIP-A;
DE AltName: Full=Afadin DIL domain-interacting protein A;
DE AltName: Full=SSX2-interacting protein A;
DE Short=XSSX2IP;
GN Name=ssx2ip-a; Synonyms=ssx2ip;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, MICROTUBULE-BINDING, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=23816619; DOI=10.1083/jcb.201302122;
RA Barenz F., Inoue D., Yokoyama H., Tegha-Dunghu J., Freiss S., Draeger S.,
RA Mayilo D., Cado I., Merker S., Klinger M., Hoeckendorf B., Pilz S.,
RA Hupfeld K., Steinbeisser H., Lorenz H., Ruppert T., Wittbrodt J.,
RA Gruss O.J.;
RT "The centriolar satellite protein SSX2IP promotes centrosome maturation.";
RL J. Cell Biol. 202:81-95(2013).
RN [3]
RP INTERACTION WITH WRAP73.
RX PubMed=26545777; DOI=10.1016/j.bbrc.2015.10.169;
RA Hori A., Morand A., Ikebe C., Frith D., Snijders A.P., Toda T.;
RT "The conserved Wdr8-hMsd1/SSX2IP complex localises to the centrosome and
RT ensures proper spindle length and orientation.";
RL Biochem. Biophys. Res. Commun. 468:39-45(2015).
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). Involved in cell movement (By similarity).
CC Acts as a centrosome maturation factor, probably by maintaining the
CC integrity of the pericentriolar material and proper microtubule
CC nucleation at mitotic spindle poles. The function seems to implicate at
CC least in part WRAP73; the SSX2IP:WRAP73 complex is proposed to act as
CC regulator of spindle anchoring at the mitotic centrosome.
CC {ECO:0000250|UniProtKB:Q8VC66, ECO:0000250|UniProtKB:Q9Y2D8,
CC ECO:0000269|PubMed:23816619}.
CC -!- SUBUNIT: Interacts with WRAP73. {ECO:0000305|PubMed:26545777}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite {ECO:0000269|PubMed:23816619}.
CC -!- DEVELOPMENTAL STAGE: Expressed at M-phase onset and accumulates at
CC microtubule minus ends. {ECO:0000269|PubMed:23816619}.
CC -!- SIMILARITY: Belongs to the ADIP family. {ECO:0000305}.
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DR EMBL; BC070749; AAH70749.1; -; mRNA.
DR RefSeq; NP_001084793.1; NM_001091324.1.
DR AlphaFoldDB; Q6NRK1; -.
DR SMR; Q6NRK1; -.
DR DNASU; 431833; -.
DR GeneID; 431833; -.
DR KEGG; xla:431833; -.
DR CTD; 431833; -.
DR Xenbase; XB-GENE-6077817; ssx2ip.S.
DR OrthoDB; 753479at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 431833; Expressed in egg cell and 16 other tissues.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR Pfam; PF11559; ADIP; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Reference proteome.
FT CHAIN 1..554
FT /note="Afadin- and alpha-actinin-binding protein A"
FT /id="PRO_0000425547"
FT REGION 508..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..287
FT /evidence="ECO:0000255"
FT COILED 359..449
FT /evidence="ECO:0000255"
SQ SEQUENCE 554 AA; 64680 MW; 439EA3AEE3C2C98D CRC64;
MGDRRTISLP ESDKILQYCS EIRMSPTSLL PSPSHSVANN LSGSVYTFCT EDNLEQCITY
IDQELRTIGF PTVQAVSKNG EGRKLHLVSI INCIYELLQR NSQTMRSNEE VETQLLKING
DLEYLQSIHQ RQKDQLEATK RENCALQERD RQMQCKNRNL LQLLKNEKEE VQKLQNIIAS
RSTQYNHSVK RKEREYNKLK ERLYQLVMDK RDKKISIDVL NYVGRADGKR SSWRTGKTDA
KNEEEMYKVL LNDYEQRQKQ LMVENVELKK VLQQMKKEMI SIVSQRKTKE KLEDSTGTVT
SDIEEEIADS SKENLSELSC EAVREQLISS IRQQWRILKS HMEKLDNQAC LVNVPTPDEN
GLIARAEHEQ ELDKLISEIQ QCKETIRSQQ QLLKQQLSVP RDDDTSKLLQ DCYLLEDKER
LQEEWKLFNA QKKNFEKERR NFTEAAIRLG HEKKVFEEDR AAWLKHQFLN MTVFSDHKNL
EERKVPGVHF SSEQDNCRLH SRPHDKVLAS SGDYSRRPSK ALPITSSSKH SLTQIESISW
RDSSISPNDT DFLN