FLIP1_MOUSE
ID FLIP1_MOUSE Reviewed; 1211 AA.
AC Q9CS72;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Filamin-A-interacting protein 1;
DE Short=FILIP;
GN Name=Filip1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-516.
RC STRAIN=C57BL/6J;
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 INTERACTION WITH FLNA.
RX PubMed=15794127; DOI=10.1111/j.1447-073x.2005.00101.x;
RA Sato M., Nagano T.;
RT "Involvement of filamin A and filamin A-interacting protein (FILIP) in
RT controlling the start and cell shape of radially migrating cortical
RT neurons.";
RL Anat. Sci. Int. 80:19-29(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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).
CC -!- FUNCTION: By acting through a filamin-A/F-actin axis, it controls the
CC start of neocortical cell migration from the ventricular zone. May be
CC able to induce the degradation of filamin-A.
CC {ECO:0000250|UniProtKB:Q8K4T4}.
CC -!- SUBUNIT: Interacts with FLNA. Interacts with RHOD (in GTP-bound form).
CC {ECO:0000269|PubMed:15794127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q7Z7B0, ECO:0000250|UniProtKB:Q8K4T4}.
CC -!- SIMILARITY: Belongs to the FILIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30888.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC140247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK017709; BAB30888.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q9CS72; -.
DR SMR; Q9CS72; -.
DR IntAct; Q9CS72; 1.
DR STRING; 10090.ENSMUSP00000091329; -.
DR iPTMnet; Q9CS72; -.
DR PhosphoSitePlus; Q9CS72; -.
DR MaxQB; Q9CS72; -.
DR PaxDb; Q9CS72; -.
DR PeptideAtlas; Q9CS72; -.
DR PRIDE; Q9CS72; -.
DR ProteomicsDB; 271701; -.
DR MGI; MGI:1917848; Filip1.
DR eggNOG; ENOG502QRWK; Eukaryota.
DR InParanoid; Q9CS72; -.
DR PhylomeDB; Q9CS72; -.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR ChiTaRS; Filip1; mouse.
DR PRO; PR:Q9CS72; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9CS72; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0099010; P:modification of postsynaptic structure; IDA:SynGO.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF09727; CortBP2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..1211
FT /note="Filamin-A-interacting protein 1"
FT /id="PRO_0000234541"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..581
FT /evidence="ECO:0000255"
FT COILED 624..778
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4T4"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1211 AA; 137599 MW; 47C07842F052FA1C CRC64;
MRSRNQGGES SSNGHVSCPK PSIISSDGGK GPSEDAKKNK ANRKGEDDVM ASGTVKRHLK
PSGESEKKTK KPLELSKEDL IQLLSIMEGE LQAREDVIHM LKTEKTKPEV LEAHYGSAEP
EKVLRVLHRD AILAQEKSIG EDVYEKPISE LDRLEEKQKE TYRRMLEQLL LAEKCHRRTV
YELENEKHKH TDYMNKSDDF TNLLEQERER LKKLLEQEKA YQARKEKENA KRLNKLRDEL
VKLKSFALML VDERQMHIEQ LGLQSQKVQD LTQKLREEEE KLKAITYKSK EDRQKLLKLE
VDFEHKASRF SQEHEEMNAK LANQESHNRQ LRLKLVGLSQ RIEELEETNK SLQKAEEELQ
ELRDKIAKGE CGNSSLMAEV ESLRKRVLEM EGKDEEITKT EAQCRELKKK LQEEEHHSKE
LRLEVEKLQK RMSELEKLEE AFSRSKSECT QLHLNLEKEK NLTKDLLNEL EVVKSRVKEL
ECSESRLEKV ELSLKDDLTK LKSFTVMLVD ERKNMMEKIK QEERKVDGLN KNFKVEQGKV
MDVTEKLIEE SKKLLKLKSE MEEKVYSLTK ERDELMGKLR SEEERSCELS CSVDLLKKRL
DGIEEVEREI NRGRLCKGSE FTCPEDNKIR ELTLEIERLK KRLQQLEVVE GDLMKTEDEY
DQLEQKFRTE QDKANFLSQQ LEEIKHQMAK NKAIEKGEAV SQEAELRHRF RMEEAKSRDL
QAEVQALKEK IHELMNKEDQ LSQLQVDYSV LQQRFMEEET KNKNMGREVL NLTKELELSK
RYSRALRPSG NGRRMVDVPV ASTGVQTEAV CGDAAEEETP AVFIRKSFQE ENHIMSNLRQ
VGLKKPMERS SVLDRYPPAA NELTMRKSWI PWMRKRENGP SAPQEKGPRP NQGTGHPGEL
VLAPKQGQPL HIRVTPDHEN STATLEITSP TSEEFFSSTT VIPTLGNQKP RITIIPSPNV
MSQKPKSADP TLGPERAMSP VTITTISREK SPEGGRGAFA DRPASPIQIM TVSTSAAPPE
IAVSPDSQEV PMGRTILKVT PEKQTVPTPM RKYNANANII TTEDNKIHIH LGSQFKRSPG
PAAAEGVSPV ITVRPVNVTA EKEVSTGTVL RSPRNHLSSR PGANKVTSTI TITPVTTSST
RGTSGQDGSS QRPTPTRIPM SKGMKAGKPV VAAPGAGNLT KFQPRAETQS MKIELKKSAA
SSTASLGGGK G
