FIL1L_HUMAN
ID FIL1L_HUMAN Reviewed; 1135 AA.
AC Q4L180; B2CNV7; B2CNV8; Q13597; Q2YDY5; Q6KFX5; Q6KFX6; Q6KFX7; Q8IUM3;
AC Q8N6Z0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Filamin A-interacting protein 1-like;
DE AltName: Full=130 kDa GPBP-interacting protein;
DE AltName: Full=90 kDa GPBP-interacting protein;
DE AltName: Full=Protein down-regulated in ovarian cancer 1;
DE Short=DOC-1;
GN Name=FILIP1L; Synonyms=COL4A3BPIP, DOC1, GIP90;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Wong K.-K., Mok S.C.;
RT "Cloning and sequencing of full length Doc1 and Doc2 mRNAs.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Revert-Ros F., Raya A., Granero F., Saus J.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT HIS-168.
RA Revert-Ros F.J., Saus J.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-168.
RA Revert F., Revert-Ros F.J., Saus J.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7).
RC TISSUE=Skeletal muscle;
RA Revert-Ros F.J., Lopez-Pascual E., Saus J.;
RT "Molecular cloning of novel isoforms of downregulated in ovarian cancer 1
RT (DOC1) protein.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Pancreas, and Skeletal muscle;
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=8314147; DOI=10.1006/gyno.1994.1040;
RA Mok S.C., Wong K.-K., Chan R.K.W., Lau C.C., Tsao S.-W., Knapp R.C.,
RA Berkowitz R.S.;
RT "Molecular cloning of differentially expressed genes in human epithelial
RT ovarian cancer.";
RL Gynecol. Oncol. 52:247-252(1994).
RN [10]
RP INDUCTION.
RX PubMed=15935955; DOI=10.1016/j.cyto.2005.01.020;
RA Tandle A.T., Mazzanti C., Alexander H.R., Roberts D.D., Libutti S.K.;
RT "Endothelial monocyte activating polypeptide-II induced gene expression
RT changes in endothelial cells.";
RL Cytokine 30:347-358(2005).
RN [11]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18794120; DOI=10.1158/0008-5472.can-08-1087;
RA Kwon M., Hanna E., Lorang D., He M., Quick J.S., Adem A., Stevenson C.,
RA Chung J.-Y., Hewitt S.M., Zudaire E., Esposito D., Cuttitta F.,
RA Libutti S.K.;
RT "Functional characterization of filamin a interacting protein 1-like, a
RT novel candidate for antivascular cancer therapy.";
RL Cancer Res. 68:7332-7341(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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. {ECO:0000269|PubMed:18794120}.
CC -!- INTERACTION:
CC Q4L180-3; P53814-5: SMTN; NbExp=3; IntAct=EBI-12221557, EBI-11100581;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18794120}. Membrane
CC {ECO:0000269|PubMed:18794120}. Nucleus {ECO:0000269|PubMed:18794120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=a, d;
CC IsoId=Q4L180-1; Sequence=Displayed;
CC Name=2; Synonyms=b, c;
CC IsoId=Q4L180-2; Sequence=VSP_029206;
CC Name=3;
CC IsoId=Q4L180-3; Sequence=VSP_029201, VSP_029206;
CC Name=4;
CC IsoId=Q4L180-4; Sequence=VSP_029202, VSP_029203;
CC Name=5;
CC IsoId=Q4L180-5; Sequence=VSP_029201, VSP_029204, VSP_029205,
CC VSP_029206;
CC Name=6;
CC IsoId=Q4L180-6; Sequence=VSP_036502;
CC Name=7;
CC IsoId=Q4L180-7; Sequence=VSP_029201;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells, colon and colon
CC cancers. In the colon, expressed in the vasculature and muscularis
CC mucosa. In colon cancer, strongly expressed in tumor stroma and the
CC vasculature (at protein level). Expressed in ovarian epithelial cells.
CC Down-regulated in ovarian cancer. {ECO:0000269|PubMed:18794120,
CC ECO:0000269|PubMed:8314147}.
CC -!- INDUCTION: Up-regulated in endothelial cells with the angiogenesis
CC inhibitors endostatin and fumagillin. By endothelial monocyte-
CC activating polypeptide II in endothelial cells.
CC {ECO:0000269|PubMed:15935955, ECO:0000269|PubMed:18794120}.
CC -!- SIMILARITY: Belongs to the FILIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98972.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAN16206.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ACB37436.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U53445; AAA98972.1; ALT_FRAME; mRNA.
DR EMBL; AF329092; AAN16206.1; ALT_FRAME; mRNA.
DR EMBL; AF514867; AAQ08177.1; -; mRNA.
DR EMBL; AF514868; AAQ08178.1; -; mRNA.
DR EMBL; AF514869; AAQ08179.1; -; mRNA.
DR EMBL; AY642382; AAV34207.1; -; mRNA.
DR EMBL; EU531865; ACB37436.1; ALT_FRAME; mRNA.
DR EMBL; EU531866; ACB37437.1; -; mRNA.
DR EMBL; AC024938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79833.1; -; Genomic_DNA.
DR EMBL; BC020941; AAH20941.1; -; mRNA.
DR EMBL; BC027860; AAH27860.1; -; mRNA.
DR CCDS; CCDS43117.1; -. [Q4L180-1]
DR CCDS; CCDS43118.1; -. [Q4L180-2]
DR CCDS; CCDS43119.1; -. [Q4L180-3]
DR CCDS; CCDS63700.1; -. [Q4L180-7]
DR CCDS; CCDS74969.1; -. [Q4L180-6]
DR RefSeq; NP_001035924.1; NM_001042459.2. [Q4L180-2]
DR RefSeq; NP_001269722.1; NM_001282793.1. [Q4L180-6]
DR RefSeq; NP_001269723.1; NM_001282794.1. [Q4L180-7]
DR RefSeq; NP_055705.2; NM_014890.3. [Q4L180-3]
DR RefSeq; NP_878913.2; NM_182909.3. [Q4L180-1]
DR RefSeq; XP_006713549.1; XM_006713486.2.
DR AlphaFoldDB; Q4L180; -.
DR SMR; Q4L180; -.
DR BioGRID; 116419; 8.
DR IntAct; Q4L180; 9.
DR MINT; Q4L180; -.
DR STRING; 9606.ENSP00000346560; -.
DR GlyGen; Q4L180; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q4L180; -.
DR PhosphoSitePlus; Q4L180; -.
DR BioMuta; FILIP1L; -.
DR DMDM; 162416295; -.
DR EPD; Q4L180; -.
DR jPOST; Q4L180; -.
DR MassIVE; Q4L180; -.
DR MaxQB; Q4L180; -.
DR PaxDb; Q4L180; -.
DR PeptideAtlas; Q4L180; -.
DR PRIDE; Q4L180; -.
DR ProteomicsDB; 62218; -. [Q4L180-1]
DR ProteomicsDB; 62219; -. [Q4L180-2]
DR ProteomicsDB; 62220; -. [Q4L180-3]
DR ProteomicsDB; 62221; -. [Q4L180-4]
DR ProteomicsDB; 62222; -. [Q4L180-5]
DR ProteomicsDB; 62223; -. [Q4L180-6]
DR ProteomicsDB; 62224; -. [Q4L180-7]
DR Antibodypedia; 46504; 107 antibodies from 19 providers.
DR DNASU; 11259; -.
DR Ensembl; ENST00000331335.9; ENSP00000327880.5; ENSG00000168386.19. [Q4L180-2]
DR Ensembl; ENST00000354552.7; ENSP00000346560.3; ENSG00000168386.19. [Q4L180-1]
DR Ensembl; ENST00000383694.3; ENSP00000373192.2; ENSG00000168386.19. [Q4L180-3]
DR Ensembl; ENST00000398326.2; ENSP00000381371.2; ENSG00000168386.19. [Q4L180-4]
DR Ensembl; ENST00000471562.1; ENSP00000419642.1; ENSG00000168386.19. [Q4L180-7]
DR Ensembl; ENST00000487087.5; ENSP00000417774.1; ENSG00000168386.19. [Q4L180-6]
DR GeneID; 11259; -.
DR KEGG; hsa:11259; -.
DR UCSC; uc003dtm.4; human. [Q4L180-1]
DR CTD; 11259; -.
DR DisGeNET; 11259; -.
DR GeneCards; FILIP1L; -.
DR HGNC; HGNC:24589; FILIP1L.
DR HPA; ENSG00000168386; Low tissue specificity.
DR MIM; 612993; gene.
DR neXtProt; NX_Q4L180; -.
DR OpenTargets; ENSG00000168386; -.
DR PharmGKB; PA162388580; -.
DR VEuPathDB; HostDB:ENSG00000168386; -.
DR eggNOG; KOG1103; Eukaryota.
DR GeneTree; ENSGT00950000182852; -.
DR HOGENOM; CLU_104016_0_0_1; -.
DR InParanoid; Q4L180; -.
DR OMA; GSAQKQF; -.
DR OrthoDB; 111454at2759; -.
DR PhylomeDB; Q4L180; -.
DR TreeFam; TF331399; -.
DR PathwayCommons; Q4L180; -.
DR SignaLink; Q4L180; -.
DR SIGNOR; Q4L180; -.
DR BioGRID-ORCS; 11259; 12 hits in 1083 CRISPR screens.
DR ChiTaRS; FILIP1L; human.
DR GenomeRNAi; 11259; -.
DR Pharos; Q4L180; Tbio.
DR PRO; PR:Q4L180; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q4L180; protein.
DR Bgee; ENSG00000168386; Expressed in saphenous vein and 187 other tissues.
DR ExpressionAtlas; Q4L180; baseline and differential.
DR Genevisible; Q4L180; HS.
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..1135
FT /note="Filamin A-interacting protein 1-like"
FT /id="PRO_0000309470"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..782
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 986
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6L0"
FT MOD_RES 994
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6L0"
FT MOD_RES 1052
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6L0"
FT VAR_SEQ 1..424
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_036502"
FT VAR_SEQ 1..240
FT /note="Missing (in isoform 3, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.5"
FT /id="VSP_029201"
FT VAR_SEQ 203..255
FT /note="LKKLIDQEIKSQEEKEQEKEKRVTTLKEELTKLKSFALMVVDEQQRLTAQLT
FT L -> WSLALLPRLECNGMILAHCNLCLLGSSDSPASAFQVAGITGTRHHAQLVFVFL
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029202"
FT VAR_SEQ 256..1135
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029203"
FT VAR_SEQ 373..386
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029204"
FT VAR_SEQ 1075..1080
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029205"
FT VAR_SEQ 1129..1135
FT /note="EPLLLPH -> SNIYN (in isoform 2, isoform 3 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.3"
FT /id="VSP_029206"
FT VARIANT 168
FT /note="R -> H (in dbSNP:rs793440)"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT /id="VAR_050993"
FT VARIANT 884
FT /note="A -> P (in dbSNP:rs28362487)"
FT /id="VAR_050994"
FT CONFLICT 532
FT /note="V -> A (in Ref. 5; ACB37437)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="E -> G (in Ref. 5; ACB37436)"
FT /evidence="ECO:0000305"
FT CONFLICT 746..747
FT /note="LQ -> CK (in Ref. 1; AAA98972)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="I -> T (in Ref. 5; ACB37436)"
FT /evidence="ECO:0000305"
FT CONFLICT 961
FT /note="T -> A (in Ref. 5; ACB37436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1135 AA; 130382 MW; 8F1E896D20F5B776 CRC64;
MRSRGSDTEG SAQKKFPRHT KGHSFQGPKN MKHRQQDKDS PSESDVILPC PKAEKPHSGN
GHQAEDLSRD DLLFLLSILE GELQARDEVI GILKAEKMDL ALLEAQYGFV TPKKVLEALQ
RDAFQAKSTP WQEDIYEKPM NELDKVVEKH KESYRRILGQ LLVAEKSRRQ TILELEEEKR
KHKEYMEKSD EFICLLEQEC ERLKKLIDQE IKSQEEKEQE KEKRVTTLKE ELTKLKSFAL
MVVDEQQRLT AQLTLQRQKI QELTTNAKET HTKLALAEAR VQEEEQKATR LEKELQTQTT
KFHQDQDTIM AKLTNEDSQN RQLQQKLAAL SRQIDELEET NRSLRKAEEE LQDIKEKISK
GEYGNAGIMA EVEELRKRVL DMEGKDEELI KMEEQCRDLN KRLERETLQS KDFKLEVEKL
SKRIMALEKL EDAFNKSKQE CYSLKCNLEK ERMTTKQLSQ ELESLKVRIK ELEAIESRLE
KTEFTLKEDL TKLKTLTVMF VDERKTMSEK LKKTEDKLQA ASSQLQVEQN KVTTVTEKLI
EETKRALKSK TDVEEKMYSV TKERDDLKNK LKAEEEKGND LLSRVNMLKN RLQSLEAIEK
DFLKNKLNQD SGKSTTALHQ ENNKIKELSQ EVERLKLKLK DMKAIEDDLM KTEDEYETLE
RRYANERDKA QFLSKELEHV KMELAKYKLA EKTETSHEQW LFKRLQEEEA KSGHLSREVD
ALKEKIHEYM ATEDLICHLQ GDHSVLQKKL NQQENRNRDL GREIENLTKE LERYRHFSKS
LRPSLNGRRI SDPQVFSKEV QTEAVDNEPP DYKSLIPLER AVINGQLYEE SENQDEDPND
EGSVLSFKCS QSTPCPVNRK LWIPWMKSKE GHLQNGKMQT KPNANFVQPG DLVLSHTPGQ
PLHIKVTPDH VQNTATLEIT SPTTESPHSY TSTAVIPNCG TPKQRITILQ NASITPVKSK
TSTEDLMNLE QGMSPITMAT FARAQTPESC GSLTPERTMS PIQVLAVTGS ASSPEQGRSP
EPTEISAKHA IFRVSPDRQS SWQFQRSNSN SSSVITTEDN KIHIHLGSPY MQAVASPVRP
ASPSAPLQDN RTQGLINGAL NKTTNKVTSS ITITPTATPL PRQSQITVEP LLLPH
