ID   FH13_ARATH              Reviewed;        1266 AA.
AC   Q9LVN1; F4KDJ5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 3.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Formin-like protein 13;
DE            Short=AtFH13;
GN   Name=FH13; OrderedLocusNames=At5g58160; ORFNames=MCK7.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX   PubMed=12417149; DOI=10.1016/s1360-1385(02)02341-5;
RA   Deeks M.J., Hussey P.J., Davies B.;
RT   "Formins: intermediates in signal-transduction cascades that affect
RT   cytoskeletal reorganization.";
RL   Trends Plant Sci. 7:492-498(2002).
RN   [4]
RP   GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX   PubMed=15256004; DOI=10.1186/1471-2164-5-44;
RA   Cvrckova F., Novotny M., Pickova D., Zarsky V.;
RT   "Formin homology 2 domains occur in multiple contexts in angiosperms.";
RL   BMC Genomics 5:44-44(2004).
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA96907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB019228; BAA96907.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED97006.2; -; Genomic_DNA.
DR   RefSeq; NP_001318825.1; NM_001345291.1.
DR   AlphaFoldDB; Q9LVN1; -.
DR   SMR; Q9LVN1; -.
DR   STRING; 3702.AT5G58160.1; -.
DR   iPTMnet; Q9LVN1; -.
DR   PaxDb; Q9LVN1; -.
DR   PRIDE; Q9LVN1; -.
DR   ProteomicsDB; 230029; -.
DR   EnsemblPlants; AT5G58160.1; AT5G58160.1; AT5G58160.
DR   GeneID; 835928; -.
DR   Gramene; AT5G58160.1; AT5G58160.1; AT5G58160.
DR   KEGG; ath:AT5G58160; -.
DR   Araport; AT5G58160; -.
DR   eggNOG; ENOG502QQEE; Eukaryota.
DR   InParanoid; Q9LVN1; -.
DR   OMA; AKPQDIH; -.
DR   OrthoDB; 1204639at2759; -.
DR   PRO; PR:Q9LVN1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LVN1; baseline and differential.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.2220; -; 1.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   Pfam; PF02181; FH2; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..1266
FT                   /note="Formin-like protein 13"
FT                   /id="PRO_0000308538"
FT   DOMAIN          9..193
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT   DOMAIN          199..337
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT   DOMAIN          829..1226
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   REGION          497..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1210..1266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..558
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..743
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..816
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        126
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
SQ   SEQUENCE   1266 AA;  139728 MW;  1AC89C4D547B0B92 CRC64;
     MALFRKLFYR KPPDGLLEIC DRVFVFDCCF STDSWEEENY KVYMAGVVNQ LQEHFPEASS
     LVFNFREVGT RSVMADVLSE HGLTIMDYPR HYEGCSLLPV EVMHHFLRSS ESWLSLGPNN
     LLLMHCESGA WPVLAFMLAA LLIYRKQYSG ESKTLDMIYK QAPRELLRLF SPLNPIPSQL
     RYLQYVSRRN LVSEWPPLDR ALTMDCVILR FIPDVSGQGG FRPMFRIYGQ DPFFVDDKKP
     KLLYTTPKKG KHLRVYKQAE CELVKIDINC HVQGDIVIEC LSLNDDMERE VMMFRVVFNT
     AFIRSNILML NRDEVDTLWH IKEFPKGFRV ELLFSDMDAA SSVDLMNFSS LEEKDGLPIE
     VFSKVHEFFN QVDWVDQTDA TRNMFQQLAI ANAVQEGLDG NSSPRLQGLS PKSIHDIMKH
     AAIENSAKFK LSSMSEVETI DTPEKPPTDS VKKFIAEDVH SVLQINNQEQ NASEDATKLL
     HQESPSLKLV HHSATVKPLV DDSKSPENAE ENFPKSPSAH DGKAISFSPP TPSPPHPVRP
     QLAQAGAPPP PPPLPAAASK PSEQLQHSVV QATEPLSQGN SWMSLAGSTF QTVPNEKNLI
     TLPPTPPLAS TSHASPEPSS KTTNSLLLSP QASPATPTNP SKTVSVDFFG AATSPHLGAS
     DNVASNLGQP ARSPPPISNS DKKPALPRPP PPPPPPPMQH STVTKVPPPP PPAPPAPPTP
     IVHTSSPPPP PPPPPPPAPP TPQSNGISAM KSSPPAPPAP PRLPTHSASP PPPTAPPPPP
     LGQTRAPSAP PPPPPKLGTK LSPSGPNVPP TPALPTGPLS SGKGRMLRVN LKNSPAKKLK
     PYHWLKLTRA VNGSLWAETQ MSSEASKAPD IDMTELESLF SASAPEQAGK SRLDSSRGPK
     PEKVQLIEHR RAYNCEIMLS KVKVPLQDLT NSVLNLEESA LDADQVENLI KFCPTREEME
     LLKGYTGDKD KLGKCELFFL EMMKVPRVET KLRVFSFKMQ FTSQISELRN SLGVVNSAAE
     QVKNSEKFKR IMQTILSLGN ALNQGTARGA AVGFKLDSLP KLSETRARNN RMTLMHYLCK
     ILAEKIPEVL DFTKELSSLE PATKIQLKFL AEEMQAINKG LEKVVQELSL SENDGPISHN
     FNKILKEFLH YAEAEVRSLA SLYSGVGRNV DGLILYFGED PAKCPFEQVV STLLNFVRLF
     NRAHEENGKQ LEAEAKKNAA EKEKPKTGGL DTEIKKPLNE EVKEEKTKTS GLGKEMSDRL
     KERTAP