ID   ADIPB_XENLA             Reviewed;         545 AA.
AC   Q6NRX3;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Afadin- and alpha-actinin-binding protein B;
DE            Short=ADIP-B;
DE   AltName: Full=Afadin DIL domain-interacting protein B;
DE   AltName: Full=SSX2-interacting protein B;
GN   Name=ssx2ip-b; 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=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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. Acts as a
CC       centrosome maturation factor, probably by maintaining the integrity of
CC       the pericentriolar material and proper microtubule nucleation at
CC       mitotic spindle poles. The function seems to implicate at least in part
CC       WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of
CC       spindle anchoring at the mitotic centrosome (By similarity).
CC       {ECO:0000250|UniProtKB:Q6NRK1, ECO:0000250|UniProtKB:Q8VC66,
CC       ECO:0000250|UniProtKB:Q9Y2D8}.
CC   -!- SUBUNIT: Interacts with WRAP73. {ECO:0000250|UniProtKB:Q6NRK1}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC       centriolar satellite {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ADIP family. {ECO:0000305}.
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DR   EMBL; BC070587; AAH70587.1; -; mRNA.
DR   RefSeq; NP_001084872.1; NM_001091403.1.
DR   AlphaFoldDB; Q6NRX3; -.
DR   SMR; Q6NRX3; -.
DR   DNASU; 431921; -.
DR   GeneID; 431921; -.
DR   KEGG; xla:431921; -.
DR   CTD; 431921; -.
DR   Xenbase; XB-GENE-17342025; ssx2ip.L.
DR   OrthoDB; 753479at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 431921; Expressed in egg cell and 18 other tissues.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0034451; C:centriolar satellite; ISS: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; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR   Pfam; PF11559; ADIP; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Reference proteome.
FT   CHAIN           1..545
FT                   /note="Afadin- and alpha-actinin-binding protein B"
FT                   /id="PRO_0000425548"
FT   REGION          497..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          106..287
FT                   /evidence="ECO:0000255"
FT   COILED          358..442
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        514..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  63836 MW;  79A2CE644DBA2CA3 CRC64;
     MGDWRTISLP ESDKILQYSS EIRMSPTSLL SSPSHSAANT LSGIVYNFCT EDNIEQCITY
     IDQELRTIGF PTVQAVSKNG DGRKLHLVSI VNCIHELLQR NSQNMRSKEE VETQLLKING
     DLEHLQSIYQ RQKDQMEATR RENCALQERD RQMQCKNRNL LQLLKNEKEE VQKLQNIIAS
     RSTQFNHSVK RKEREYNKLK ERLYQLVMDK RDKKISIDVL NYVGRADGKR TSWRTGKTDA
     KNEEEMYKVL LNDYEQRQKQ LMVENAELKK VLQQMKKEMI SILSQRKTKE KLDDSIGPVA
     SDIEEDLADS SKENLSELSC EAVREQLVSS IRQQWRILKS HMEKLDNQAT PDENGMIARG
     DHEQELGKLI NEIQQCKETI KIQQQLLKQQ FSVPRDDTST LLQDCYLLED KERLQEEWKL
     FNEQKKNFEK ERRNFTEAAI RLGHEKKAFE EDRAAWLKHQ FLNMTVFTDH KNSEEKRAHG
     VHFSPEQDHC RLHSRTHDRH LASSGDHYQR PRKTLPITPS SKHSLTQRES VAWRDSSISP
     NGTDF