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   22-APR-2020, entry version 111.
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};
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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   SMR; Q4L180; -.
DR   BioGrid; 116419; 1.
DR   IntAct; Q4L180; 7.
DR   MINT; Q4L180; -.
DR   STRING; 9606.ENSP00000346560; -.
DR   iPTMnet; Q4L180; -.
DR   PhosphoSitePlus; Q4L180; -.
DR   BioMuta; FILIP1L; -.
DR   DMDM; 162416295; -.
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; 99 antibodies.
DR   Ensembl; ENST00000331335; ENSP00000327880; ENSG00000168386. [Q4L180-2]
DR   Ensembl; ENST00000354552; ENSP00000346560; ENSG00000168386. [Q4L180-1]
DR   Ensembl; ENST00000383694; ENSP00000373192; ENSG00000168386. [Q4L180-3]
DR   Ensembl; ENST00000398326; ENSP00000381371; ENSG00000168386. [Q4L180-4]
DR   Ensembl; ENST00000471562; ENSP00000419642; ENSG00000168386. [Q4L180-7]
DR   Ensembl; ENST00000487087; ENSP00000417774; ENSG00000168386. [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   eggNOG; ENOG410IKR8; Eukaryota.
DR   eggNOG; ENOG410ZUGY; LUCA.
DR   GeneTree; ENSGT00950000182852; -.
DR   HOGENOM; CLU_104016_0_0_1; -.
DR   InParanoid; Q4L180; -.
DR   OMA; PQDNRTQ; -.
DR   OrthoDB; 111454at2759; -.
DR   PhylomeDB; Q4L180; -.
DR   TreeFam; TF331399; -.
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 thoracic aorta and 217 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; Polymorphism; Reference proteome.
FT   CHAIN           1..1135
FT                   /note="Filamin A-interacting protein 1-like"
FT                   /id="PRO_0000309470"
FT   COILED          164..782
FT                   /evidence="ECO:0000255"
FT   MOD_RES         791
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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
//