FIL1L_MOUSE
ID FIL1L_MOUSE Reviewed; 1131 AA.
AC Q6P6L0; B2ZAA3; B3GM33; Q05CK4; Q3UIY5; Q4G0B9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Filamin A-interacting protein 1-like;
DE AltName: Full=Protein down-regulated in ovarian cancer 1 homolog;
DE Short=DOC-1;
GN Name=Filip1l; Synonyms=Doc1;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C3H/HeJ;
RA Revert-Ros F., Saadeddin A., Saus J.;
RT "Molecular cloning of a novel variant of mouse downregulated in ovarian
RT cancer 1 (DOC1) homolog.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic heart;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 223-1131 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, Embryo, and Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789; THR-984; THR-992 AND
RP SER-1050, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
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: Acts as a regulator of the antiangiogenic activity on
CC endothelial cells. When overexpressed in endothelial cells, leads to
CC inhibition of cell proliferation and migration and an increase in
CC apoptosis. Inhibits melanoma growth When expressed in tumor-associated
CC vasculature (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P6L0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P6L0-2; Sequence=VSP_029208, VSP_029209;
CC Name=3;
CC IsoId=Q6P6L0-3; Sequence=VSP_029207;
CC -!- SIMILARITY: Belongs to the FILIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24523.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH24523.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH62166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ACC91883.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EU623548; ACC91883.1; ALT_INIT; mRNA.
DR EMBL; EU704258; ACD92726.1; -; mRNA.
DR EMBL; AK146705; BAE27371.1; -; mRNA.
DR EMBL; BC024523; AAH24523.1; ALT_SEQ; mRNA.
DR EMBL; BC062166; AAH62166.1; ALT_INIT; mRNA.
DR EMBL; BC098507; AAH98507.1; -; mRNA.
DR CCDS; CCDS37366.2; -. [Q6P6L0-1]
DR CCDS; CCDS49877.1; -. [Q6P6L0-3]
DR AlphaFoldDB; Q6P6L0; -.
DR SMR; Q6P6L0; -.
DR IntAct; Q6P6L0; 1.
DR STRING; 10090.ENSMUSP00000124179; -.
DR iPTMnet; Q6P6L0; -.
DR PhosphoSitePlus; Q6P6L0; -.
DR jPOST; Q6P6L0; -.
DR MaxQB; Q6P6L0; -.
DR PaxDb; Q6P6L0; -.
DR PRIDE; Q6P6L0; -.
DR ProteomicsDB; 266846; -. [Q6P6L0-1]
DR ProteomicsDB; 266848; -. [Q6P6L0-3]
DR Antibodypedia; 46504; 107 antibodies from 19 providers.
DR Ensembl; ENSMUST00000099667; ENSMUSP00000133252; ENSMUSG00000043336. [Q6P6L0-2]
DR MGI; MGI:1925999; Filip1l.
DR VEuPathDB; HostDB:ENSMUSG00000043336; -.
DR eggNOG; KOG1103; Eukaryota.
DR GeneTree; ENSGT00950000182852; -.
DR HOGENOM; CLU_104016_0_0_1; -.
DR InParanoid; Q6P6L0; -.
DR ChiTaRS; Filip1l; mouse.
DR PRO; PR:Q6P6L0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6P6L0; protein.
DR Bgee; ENSMUSG00000043336; Expressed in ascending aorta and 173 other tissues.
DR ExpressionAtlas; Q6P6L0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF09727; CortBP2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1131
FT /note="Filamin A-interacting protein 1-like"
FT /id="PRO_0000309471"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..583
FT /evidence="ECO:0000255"
FT COILED 610..780
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 984
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 992
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..238
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029207"
FT VAR_SEQ 201
FT /note="L -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029208"
FT VAR_SEQ 202..1131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029209"
FT CONFLICT 632
FT /note="N -> K (in Ref. 1; ACD92726 and 2; ACC91883)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="L -> V (in Ref. 1; ACD92726 and 2; ACC91883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1131 AA; 129772 MW; 765E51CBFEEF91CE CRC64;
MRSRSSNAEG SAPKQIPRHS KFQDSIQDMK HRTHKKDPSC ESEGVLPRPV SEKSHTGKGH
HTEDLSRDDL LFLLSILEGE LQARDEVIGI LRAEKIDLAL LEAQYGFVTP KKVLEALQRD
AFQAKSAPWQ EDIYEKPMNE LDKVVEKHKE SHRRILEQLL MVERSHRQTI MEMEEEKRKH
KEYMKKSDEF INLLEQECER LKKLIDQETA SQEKKEQEKE KRIKTLKEEL TKLKSFALMV
VDEQQRLTAQ LALQRQKIQA LTTSAKETQG KLALAEARAQ EEEQKATRLE KELQTQTTEF
HQNQDKIMAK LTNEDSQNRQ LRQKLAALSR QIDELEETNR SLRKAEEELQ DIKDKINKGE
YGNSGIMDEV DELRKRVLDM EGKDEELIKM EEQCRDLNKR LEKETVQSKD FKLEVDKLSV
RITALEKLED ALDKSKQECY SLKCNLEKEK MTTKQLSEEL ESLNARIKEL EAIESRLEKT
EITLKDDLTK LKTLTVMLVD ERKTMSEKLK QTEDKLQSTT SQLQAEQNKV TTVTEKLIEE
TKRALKSKTD AEEKMYSVTK ERDDLRNKLK AEEEKGHDLL SKVTILKNRL QSLEAIEKDF
VKNKLNQDSS KSTAALHQEN NKIKELSQEV ENLKLKLKDM KAIEDDLMKT EDEYETLERR
YANERDKAQF LSQELEHAKM ELAKYKLAEK TESSHEQWLF RRLQEEEAKS GHLSREVDAL
KEKIHEYMAT EDLICHLQGD HSLLQKKLNQ QENRNRDLGR EIENLTKELE RYRHFSKSLR
PSLNGRRISD PQVFSKEVQT EAADSEPPDY KSLIPLERAV INGQFYEENE DQDDDPNEEE
SVLSFRCSQS SSLPMNRKLW IPWMKSKEGH PQNGKIQTKS NGNFVQPGDL VLSHTPGQPL
HIKVTPDHIQ NTATLEITSP TTESPHSYTS TAVIPNCGTP KQRITILQNA SITPIKSKSS
TESLMNLEQS MSPVTMATFA RAQTPESCGS VTPERTMSPI QVLAMTGSPS SPEQGCSPEP
IEISAKHAIF RVSPDRQSSW QFQRSNSNSS SVITTEDNKI HIHLGSPYMQ AVAGPMRPAS
PSAPLQDNRT QGLTNGALNK TTNKVTSSIT ITPTATPLPR QSQITVSNIY N
