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Database: UniProt
Entry: A0A3Q3B5P0_KRYMA
LinkDB: A0A3Q3B5P0_KRYMA
Original site: A0A3Q3B5P0_KRYMA 
ID   A0A3Q3B5P0_KRYMA        Unreviewed;      1125 AA.
AC   A0A3Q3B5P0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Formin like 1 {ECO:0000313|Ensembl:ENSKMAP00000024455.1};
GN   Name=FMNL1 {ECO:0000313|Ensembl:ENSKMAP00000024455.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000024455.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000024455.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC       {ECO:0000256|ARBA:ARBA00023449}.
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DR   AlphaFoldDB; A0A3Q3B5P0; -.
DR   STRING; 37003.ENSKMAP00000024455; -.
DR   Ensembl; ENSKMAT00000024761.1; ENSKMAP00000024455.1; ENSKMAG00000018106.1.
DR   GeneTree; ENSGT00940000156292; -.
DR   OMA; AQKGPMM; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IEA:InterPro.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR043592; FMNL_animal.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR45857:SF2; FORMIN-LIKE PROTEIN 1; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 2.
DR   Pfam; PF02181; FH2; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT   DOMAIN          46..518
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          686..1076
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..679
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1125 AA;  124939 MW;  387164244F0C8062 CRC64;
     MGNAAAGGLE QEPAEGREAR NSVGAASTMS EPTLTLQKKQ PAPPKLPMPP EEELEERFNA
     VLSSMNLPPD KLKLLSQYDS DKKWELVCDQ ERFQVKSPPS TYLSKIKSFY QDQGGVSRRS
     KKKIQDATQV LKALEISLRT NHIGWAQEFL NEQNNGLDVL VEYLSHAQSD TSFDFESVEN
     GGTLSDRQKP VERSMEDLTK SSSGGGGGGG HSHGMTRAAR ALTVRISATL SNKMHKKSHL
     SQQRDDIHVC IMCLRAIMNY QSGFNLVMTH PRCVNEITLS LNSRNPRTKA LVLELLAAVC
     LVRGGHDIIL SAFDNFKEVS KERNRFEKLM EYFINDDNNI DFMVACMQFI NIVVHSVENM
     NFRVHLQYEF TFLGLDKYLE NLKQTESEKL QVQIQAYLDN VLDVGALLED AENRGGVLNH
     VEDLQNANLE VGREIIRGQC EVKQAFVVCG TNLKERSLCV VLQLNARLQE IDGQTTERIS
     ELETQLMQAT KETELLKESL RESCSQVSAL QQRERERELN REREKDRERL GTSISQSPSE
     LEQKIQELQD KGLIQVGRNP SGGLDIQVVP VKVVEYIQSP PSTTQTSSPA STLPSSPPPP
     PATGGAPPPP PPPPPPPPPG QSTIAHPPPP PGAGPPPPPP PPPPPGAGPP PPPPPPGAGP
     PPPPPPPGGG PPPPPGAPGT QSGFKNKKPI QTKYRMPLLN WQALKPNQVT GTVFNDLDDE
     QILEELNMDM FEEQFKTRAQ GNPTDISKIK KKTQKAPSKT SLIDANKAKN LAITLRKGGM
     NPSAICTAIE TYDQQSLSID FLELLEHFIP SDFEMKLLVN YEKDGRPLEE LTDEDRFILR
     FGKIPRLSQR INTLTFMGNF PETVKRLQPQ LDSIIAASMS IKSSAKLKKI LEIVLAFGNY
     MNSSKRGAAY GFRLQSLDLL LETKSTDRTQ TLLQFMTSII LEKYPDLANF HTELRFIDKA
     ALVSLDGILQ DIRSLERGME MTKKEFLVQD DSPVLKEFIK TNSEQLESLI KDSKTAQEAY
     VSVVEYFGEN PKTTQPSMFF PMFGRFIKGY KTSQQEIEQK KKMEVEVSEV KETPSPNKAG
     GQKGPMMPKM PQMDLIAELK KKQLKPSVRE GKDGALEDII TGTAT
//
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