FMNL1_HUMAN
ID FMNL1_HUMAN Reviewed; 1100 AA.
AC O95466; D2DGW2; Q6DKG5; Q6IBP3; Q86UH1; Q8N671; Q8TDH1; Q96H10;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Formin-like protein 1;
DE AltName: Full=CLL-associated antigen KW-13;
DE AltName: Full=Leukocyte formin;
GN Name=FMNL1; Synonyms=C17orf1, C17orf1B, FMNL, FRL1;
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 1).
RC TISSUE=Bone marrow;
RA Favaro P.M.B., Medina S.S., Basseres D.S., Costa F.F., Saad S.T.O.;
RT "Human leukocyte formin: a new protein preferentially expressed in
RT lymphocytes.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 110-1100 (ISOFORM 1).
RA Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M.,
RA Barrett P., Gribben J.G.;
RT "Identification of novel tumor antigens in CLL by SEREX: assessment of
RT their potential as targets for immunotherapeutic approaches.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 419-1100 (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Lymph;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 629-1100 (ISOFORM 2).
RX PubMed=9799091; DOI=10.1007/s004390050827;
RA Aronsson F.C., Magnusson P., Andersson B., Karsten S.L., Shibasaki Y.,
RA Lendon C.L., Goate A.M., Brookes A.J.;
RT "The NIK protein kinase and C17orf1 genes: chromosomal mapping, gene
RT structures and mutational screening in frontotemporal dementia and
RT parkinsonism linked to chromosome 17.";
RL Hum. Genet. 103:340-345(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 642-1100 (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 668-1100 (ISOFORM 3), MYRISTOYLATION AT
RP GLY-2, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=19815554; DOI=10.1074/jbc.m109.060699;
RA Han Y., Eppinger E., Schuster I.G., Weigand L.U., Liang X., Kremmer E.,
RA Peschel C., Krackhardt A.M.;
RT "Formin-like 1 (FMNL1) is regulated by N-terminal myristoylation and
RT induces polarized membrane blebbing.";
RL J. Biol. Chem. 284:33409-33417(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-624, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-184 AND SER-624, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-624, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INTERACTION WITH SRGAP2.
RX PubMed=21148482; DOI=10.1074/jbc.m110.190397;
RA Mason F.M., Heimsath E.G., Higgs H.N., Soderling S.H.;
RT "Bi-modal regulation of a formin by srGAP2.";
RL J. Biol. Chem. 286:6577-6586(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-624; SER-693 AND
RP SER-1031, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624 AND SER-1031, AND
RP IDENTIFICATION BY 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).
RN [18]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May play a role in the control of cell motility and survival
CC of macrophages (By similarity). Plays a role in the regulation of cell
CC morphology and cytoskeletal organization. Required in the cortical
CC actin filament dynamics and cell shape. {ECO:0000250,
CC ECO:0000269|PubMed:21834987}.
CC -!- SUBUNIT: Interacts with RAC1, PFN1 and PFN2 (By similarity). Interacts
CC (activated by RAC1) with SRGAP2 (via SH3 domain); regulates the actin
CC filament severing activity of FMNL1. {ECO:0000250,
CC ECO:0000269|PubMed:21148482}.
CC -!- INTERACTION:
CC O95466; O75044: SRGAP2; NbExp=3; IntAct=EBI-720020, EBI-1051034;
CC O95466; D0ZIB5: steC; Xeno; NbExp=6; IntAct=EBI-720020, EBI-27033646;
CC O95466-2; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-10191924, EBI-740641;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:19815554}; Lipid-anchor
CC {ECO:0000269|PubMed:19815554}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250}. Note=Recruited to actin-rich phagosomes during
CC phagocytosis. Translocates to the plasma membrane upon activation by
CC RAC1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cell cortex. Cell
CC projection, bleb. Note=Colocalized with F-actin in bleb protrusions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=FMNL1alpha;
CC IsoId=O95466-1; Sequence=Displayed;
CC Name=2; Synonyms=FMNL1beta;
CC IsoId=O95466-2; Sequence=VSP_013977;
CC Name=3; Synonyms=FMNL1gamma;
CC IsoId=O95466-3; Sequence=VSP_043845;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the N-terminus. This autoinhibition is released upon
CC competitive binding of an activated GTPase. The release of DAD allows
CC the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- PTM: Myristoylation mediates membrane localization and blebbing.
CC {ECO:0000269|PubMed:19815554}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. Constitutively
CC activated form, probably due to alterations in the DAD domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21906.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA07870.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY278319; AAP32476.1; -; mRNA.
DR EMBL; AC008105; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF432213; AAL99920.1; -; mRNA.
DR EMBL; BC001710; AAH01710.2; -; mRNA.
DR EMBL; BC009000; AAH09000.2; -; mRNA.
DR EMBL; BC021906; AAH21906.1; ALT_INIT; mRNA.
DR EMBL; BC073988; AAH73988.1; -; mRNA.
DR EMBL; AJ008112; CAA07870.1; ALT_INIT; mRNA.
DR EMBL; CR456759; CAG33040.1; -; mRNA.
DR EMBL; FJ534522; ACR19333.1; -; mRNA.
DR CCDS; CCDS11497.1; -. [O95466-1]
DR RefSeq; NP_005883.2; NM_005892.3. [O95466-1]
DR RefSeq; XP_006722126.1; XM_006722063.3. [O95466-3]
DR RefSeq; XP_006722133.1; XM_006722070.3. [O95466-2]
DR PDB; 4YDH; X-ray; 3.80 A; A/C=1-458.
DR PDBsum; 4YDH; -.
DR AlphaFoldDB; O95466; -.
DR SMR; O95466; -.
DR BioGRID; 107208; 95.
DR IntAct; O95466; 21.
DR MINT; O95466; -.
DR STRING; 9606.ENSP00000329219; -.
DR GlyGen; O95466; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95466; -.
DR MetOSite; O95466; -.
DR PhosphoSitePlus; O95466; -.
DR SwissPalm; O95466; -.
DR BioMuta; FMNL1; -.
DR EPD; O95466; -.
DR jPOST; O95466; -.
DR MassIVE; O95466; -.
DR MaxQB; O95466; -.
DR PaxDb; O95466; -.
DR PeptideAtlas; O95466; -.
DR PRIDE; O95466; -.
DR ProteomicsDB; 50898; -. [O95466-1]
DR ProteomicsDB; 50899; -. [O95466-2]
DR ProteomicsDB; 50900; -. [O95466-3]
DR Antibodypedia; 17595; 186 antibodies from 32 providers.
DR DNASU; 752; -.
DR Ensembl; ENST00000331495.8; ENSP00000329219.2; ENSG00000184922.15. [O95466-1]
DR GeneID; 752; -.
DR KEGG; hsa:752; -.
DR MANE-Select; ENST00000331495.8; ENSP00000329219.2; NM_005892.4; NP_005883.3.
DR UCSC; uc002iin.4; human. [O95466-1]
DR CTD; 752; -.
DR DisGeNET; 752; -.
DR GeneCards; FMNL1; -.
DR HGNC; HGNC:1212; FMNL1.
DR HPA; ENSG00000184922; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 604656; gene.
DR neXtProt; NX_O95466; -.
DR OpenTargets; ENSG00000184922; -.
DR PharmGKB; PA28186; -.
DR VEuPathDB; HostDB:ENSG00000184922; -.
DR eggNOG; KOG1922; Eukaryota.
DR eggNOG; KOG1923; Eukaryota.
DR GeneTree; ENSGT00940000156292; -.
DR HOGENOM; CLU_003597_0_0_1; -.
DR InParanoid; O95466; -.
DR OMA; FMRQDDC; -.
DR OrthoDB; 288325at2759; -.
DR PhylomeDB; O95466; -.
DR TreeFam; TF325155; -.
DR PathwayCommons; O95466; -.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; O95466; -.
DR BioGRID-ORCS; 752; 18 hits in 1083 CRISPR screens.
DR ChiTaRS; FMNL1; human.
DR GeneWiki; FMNL1; -.
DR GenomeRNAi; 752; -.
DR Pharos; O95466; Tbio.
DR PRO; PR:O95466; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O95466; protein.
DR Bgee; ENSG00000184922; Expressed in granulocyte and 161 other tissues.
DR ExpressionAtlas; O95466; baseline and differential.
DR Genevisible; O95466; HS.
DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0032794; F:GTPase activating protein binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR027657; FMNL1.
DR InterPro; IPR043592; FMNL_animal.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45857; PTHR45857; 1.
DR PANTHER; PTHR45857:SF2; PTHR45857:SF2; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 2.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoplasmic vesicle; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..1100
FT /note="Formin-like protein 1"
FT /id="PRO_0000194890"
FT DOMAIN 27..468
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 632..1023
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1059..1090
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:19815554,
FT ECO:0000269|PubMed:25255805"
FT VAR_SEQ 1070
FT /note="T -> TGKGLARPWSYPQSVLLCFLLTQCAILWGTGCHTASCYLFCFSFLFP
FT FSTPLHLPHPHS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19815554"
FT /id="VSP_043845"
FT VAR_SEQ 1071..1100
FT /note="VIKTVPFTARTGKRTSRLLCEASLGEEMPL -> DLRNQPYIRADTGRRSAR
FT RRPPGPPLQVTSDLSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9799091, ECO:0000303|Ref.6"
FT /id="VSP_013977"
FT CONFLICT 455
FT /note="P -> A (in Ref. 1; AAP32476, 3; AAL99920 and 4;
FT AAH73988)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="Missing (in Ref. 4; AAH21906)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="G -> R (in Ref. 5; CAA07870)"
FT /evidence="ECO:0000305"
FT CONFLICT O95466-2:1101..1102
FT /note="DL -> EV (in Ref. 4; AAH21906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1100 AA; 121854 MW; 91F9CE2B3B526FFC CRC64;
MGNAAGSAEQ PAGPAAPPPK QPAPPKQPMP AAGELEERFN RALNCMNLPP DKVQLLSQYD
NEKKWELICD QERFQVKNPP AAYIQKLKSY VDTGGVSRKV AADWMSNLGF KRRVQESTQV
LRELETSLRT NHIGWVQEFL NEENRGLDVL LEYLAFAQCS VTYDMESTDN GASNSEKNKP
LEQSVEDLSK GPPSSVPKSR HLTIKLTPAH SRKALRNSRI VSQKDDVHVC IMCLRAIMNY
QSGFSLVMNH PACVNEIALS LNNKNPRTKA LVLELLAAVC LVRGGHDIIL AAFDNFKEVC
GEQHRFEKLM EYFRNEDSNI DFMVACMQFI NIVVHSVENM NFRVFLQYEF THLGLDLYLE
RLRLTESDKL QVQIQAYLDN IFDVGALLED TETKNAVLEH MEELQEQVAL LTERLRDAEN
ESMAKIAELE KQLSQARKEL ETLRERFSES TAMGPSRRPP EPEKAPPAAP TRPSALELKV
EELEEKGLIR ILRGPGDAVS IEILPVAVAT PSGGDAPTPG VPTGSPSPDL APAAEPAPGA
APPPPPPLPG LPSPQEAPPS APPQAPPLPG SPEPPPAPPL PGDLPPPPPP PPPPPGTDGP
VPPPPPPPPP PPGGPPDALG RRDSELGPGV KAKKPIQTKF RMPLLNWVAL KPSQITGTVF
TELNDEKVLQ ELDMSDFEEQ FKTKSQGPSL DLSALKSKAA QKAPSKATLI EANRAKNLAI
TLRKGNLGAE RICQAIEAYD LQALGLDFLE LLMRFLPTEY ERSLITRFER EQRPMEELSE
EDRFMLCFSR IPRLPERMTT LTFLGNFPDT AQLLMPQLNA IIAASMSIKS SDKLRQILEI
VLAFGNYMNS SKRGAAYGFR LQSLDALLEM KSTDRKQTLL HYLVKVIAEK YPQLTGFHSD
LHFLDKAGSV SLDSVLADVR SLQRGLELTQ REFVRQDDCM VLKEFLRANS PTMDKLLADS
KTAQEAFESV VEYFGENPKT TSPGLFFSLF SRFIKAYKKA EQEVEQWKKE AAAQEAGADT
PGKGEPPAPK SPPKARRPQM DLISELKRRQ QKEPLIYESD RDGAIEDIIT VIKTVPFTAR
TGKRTSRLLC EASLGEEMPL
