FLIP1_RAT
ID FLIP1_RAT Reviewed; 1212 AA.
AC Q8K4T4; Q8JZS5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Filamin-A-interacting protein 1;
DE Short=FILIP;
GN Name=Filip1;
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP INTERACTION WITH FLNA, SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=Wistar;
RX PubMed=12055638; DOI=10.1038/ncb808;
RA Nagano T., Yoneda T., Hatanaka Y., Kubota C., Murakami F., Sato M.;
RT "Filamin A-interacting protein (FILIP) regulates cortical cell migration
RT out of the ventricular zone.";
RL Nat. Cell Biol. 4:495-501(2002).
RN [2]
RP TISSUE SPECIFICITY, INTERACTION WITH FLNA, SUBCELLULAR LOCATION, AND
RP FUNCTION.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP 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: 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:0000269|PubMed:12055638, ECO:0000269|PubMed:15794127}.
CC -!- SUBUNIT: Interacts with FLNA. Interacts with RHOD (in GTP-bound form).
CC {ECO:0000269|PubMed:12055638, ECO:0000269|PubMed:15794127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12055638, ECO:0000269|PubMed:15794127}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12055638}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:12055638}. Note=Localized along actin stress
CC fibers, except at their ends, suggesting colocalization with F-actin
CC (fiber-like). {ECO:0000269|PubMed:12055638}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12055638}. Note=Punctate distribution in the
CC cytoplasm distinct from that of F-actin. {ECO:0000269|PubMed:12055638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L-FILIP;
CC IsoId=Q8K4T4-1; Sequence=Displayed;
CC Name=2; Synonyms=S-FILIP;
CC IsoId=Q8K4T4-2; Sequence=VSP_018346;
CC -!- TISSUE SPECIFICITY: Expressed in muscle tissue, including heart. Found
CC in cortical ventricular zone. {ECO:0000269|PubMed:12055638,
CC ECO:0000269|PubMed:15794127}.
CC -!- SIMILARITY: Belongs to the FILIP1 family. {ECO:0000305}.
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DR EMBL; AB055759; BAC00851.1; -; mRNA.
DR EMBL; D87257; BAC00852.1; -; mRNA.
DR RefSeq; NP_663715.1; NM_145682.1. [Q8K4T4-1]
DR AlphaFoldDB; Q8K4T4; -.
DR SMR; Q8K4T4; -.
DR STRING; 10116.ENSRNOP00000015365; -.
DR CarbonylDB; Q8K4T4; -.
DR iPTMnet; Q8K4T4; -.
DR PhosphoSitePlus; Q8K4T4; -.
DR PaxDb; Q8K4T4; -.
DR PRIDE; Q8K4T4; -.
DR GeneID; 246776; -.
DR KEGG; rno:246776; -.
DR UCSC; RGD:628597; rat. [Q8K4T4-1]
DR CTD; 27145; -.
DR RGD; 628597; Filip1.
DR eggNOG; ENOG502QRWK; Eukaryota.
DR InParanoid; Q8K4T4; -.
DR OrthoDB; 90683at2759; -.
DR PhylomeDB; Q8K4T4; -.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR PRO; PR:Q8K4T4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0099010; P:modification of postsynaptic structure; ISO:RGD.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF09727; CortBP2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1212
FT /note="Filamin-A-interacting protein 1"
FT /id="PRO_0000234542"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..575
FT /evidence="ECO:0000255"
FT COILED 623..777
FT /evidence="ECO:0000255"
FT COMPBIAS 1..28
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 948..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CS72"
FT VAR_SEQ 1..247
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12055638"
FT /id="VSP_018346"
SQ SEQUENCE 1212 AA; 137753 MW; A1D5B9C5AF7D4F80 CRC64;
MRSRNQGGES SSNGHVSCPK SSIISSDGGK GPSEDAKKNK ANRKEEDVMA SGTIKRHLKP
SGESEKKTKK SVELSKEDLI QLLSIMEGEL QAREDVIHML RTEKTKPEVL EAHYGSAEPE
KVLRVLHRDA ILAQEKSIGE DVYEKPISEL DRLEEKQKET YRRMLEQLLL AEKCHRRTVY
ELENEKHKHT DYMNKSDDFT NLLEQERERL KKLLEQEKAY QARKEKENAK RLNKLRDELV
KLKSFALMLV DERQMHIEQL GLQSQKVQDL TQKLREEEEK LKAVTYKSKE DRQKLLKLEV
DFEHKASRFS QEHEEMNAKL ANQESHNRQL RLKLVGLSQR IEELEETNKS LQKAEEELQE
LREKIAKGEC GNSSLMAEVE SLRKRVLEME GKDEEITKTE AQCRELKKKL QEEEHHSKEL
RLEVEKLQKR MSELEKLEEA FSRSKSECTQ LHLNLEKEKN LTKDLLNELE VVKSRVKELE
CSESRLEKAE LSLKDDLTKL KSFTVMLVDE RKNMMEKIKQ EERKVDGLNK NFKVEQGKVM
DVTEKLIEES KKLLKLKSEM EEKEYSLTKE RDELMGKLRS EEERSCELSC SVDLLKKRLD
GIEEVEREIN RGRSCKGSEF TCPEDNKIRE LTLEIERLKK RLQQLEVVEG DLMKTEDEYD
QLEQKFRTEQ DKANFLSQQL EEIKHQMAKH KAIEKGEAVS QEAELRHRFR LEEAKSRDLQ
AEVQALKEKI HELMNKEDQL SQLQVDYSVL QQRFMEEETK NKNMGREVLN LTKELELSKR
YSRALRPSGN GRRMVDVPVA STGVQTEAVC GDAAEEETPA VFIRKSFQEE NHIMSNLRQV
GLKKPMERSS VLDRYPPAAN ELTMRKSWIP WMRKRENGPS TPQEKGPRPN QGAGHPGELV
LAPKQGQPLH IRVTPDHENS TATLEITSPT SEEFFSSTTV IPTLGNQKPR ITIIPSPNVM
SQKPKSADPT LGPERAMSPV TITTISREKS PEGGRSAFAD RPASPIQIMT VSTSAAPTEI
AVSPESQEVP MGRTILKVTP EKQTVPAPVR KYNSNANIIT TEDNKIHIHL GSQFKRSPGP
AAEGVSPVIT VRPVNVTAEK EVSTGTVLRS PRNHLSSRPG ASKVTSTITI TPVTTSSTRG
TQSVSGQDGS SQRPTPTRIP MSKGMKAGKP VVAASGAGNL TKFQPRAETQ SMKIELKKSA
ASSTASLGGG KG
