ID   ADIP_ORYLA              Reviewed;         583 AA.
AC   H2MTR9;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Afadin- and alpha-actinin-binding protein;
DE            Short=ADIP;
DE   AltName: Full=Afadin DIL domain-interacting protein;
DE   AltName: Full=SSX2-interacting protein;
GN   Name=ssx2ip;
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR;
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
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).
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. {ECO:0000250,
CC       ECO:0000269|PubMed:23816619}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC       centriolar satellite {ECO:0000269|PubMed:23816619}.
CC   -!- SIMILARITY: Belongs to the ADIP family. {ECO:0000305}.
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DR   AlphaFoldDB; H2MTR9; -.
DR   SMR; H2MTR9; -.
DR   STRING; 8090.ENSORLP00000022176; -.
DR   eggNOG; ENOG502QQJF; Eukaryota.
DR   HOGENOM; CLU_031049_0_0_1; -.
DR   InParanoid; H2MTR9; -.
DR   OMA; DNIPQCI; -.
DR   TreeFam; TF332889; -.
DR   Proteomes; UP000001038; Unplaced.
DR   Proteomes; UP000265180; Chromosome 9.
DR   Proteomes; UP000265200; Chromosome 9.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0034451; C:centriolar satellite; IBA:GO_Central.
DR   GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IBA:GO_Central.
DR   InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR   Pfam; PF11559; ADIP; 1.
PE   3: Inferred from homology;
KW   Cell adhesion; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Reference proteome.
FT   CHAIN           1..583
FT                   /note="Afadin- and alpha-actinin-binding protein"
FT                   /id="PRO_0000425546"
FT   REGION          285..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          108..220
FT                   /evidence="ECO:0000255"
FT   COILED          255..333
FT                   /evidence="ECO:0000255"
FT   COILED          420..453
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        300..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  66487 MW;  32DD13FD4E67EAA1 CRC64;
     MGDWGLTETS MDNYEISILS HVAMSPSRHN NLMSAYSLPS SKSSYSVISA FCTEDNIPQC
     ISYINQELGS LGLAAHIQAD PPGRASLNAA PALNAMYELL QIHRRSMNNV EELEKEQLKK
     TSTLEHMQTS NSRLKDQLEL SIREKSGLHE TERQLQLKLK TLQSCLKTEK DEVQKLQSII
     ASRASQYSHD AKRKEREAAK LKERLSQLLV DRKDKKLAIE MLNSVGRSDG KRSHWKTAKA
     TASREAEMYK SLLSDYEASQ RALMLENAEL QKVLQQMKKE MMHILSPCPP LNRGGSAEES
     QELGDSDREE RSAETSRETL DQSCEHAREQ LTNSIRQQWR KLRNHVQKLD NQASLVQNQP
     PSNAEVIPLE THEHEVERMR LEVQQCKEFI HAQQQLLQQQ LNTSFDDETA ALLNGCYTLE
     EKERLKEEWR LFDEQKRNFE KERKNFTEAA IRLGREKRAF EEDRAAWLKH QFLSMTPFAD
     RMRSSSSDGQ SALSVKSEPE IRTSSSKAPP VKSSAYTTFS TPKSSKSAAV PSTIDVCRTL
     RLIPDYRESS ATEDEESWLK SKSKVCSSDL SIFSLDEDKN PLT