ID   A0A1U7RZ27_ALLSI        Unreviewed;      1125 AA.
AC   A0A1U7RZ27;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 2.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Formin-like protein 1 isoform X1 {ECO:0000313|RefSeq:XP_006026448.2};
GN   Name=FMNL1 {ECO:0000313|RefSeq:XP_006026448.2};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006026448.2};
RN   [1] {ECO:0000313|RefSeq:XP_006026448.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC       {ECO:0000256|ARBA:ARBA00023449}.
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DR   RefSeq; XP_006026448.2; XM_006026386.3.
DR   AlphaFoldDB; A0A1U7RZ27; -.
DR   STRING; 38654.A0A1U7RZ27; -.
DR   KEGG; asn:102388268; -.
DR   eggNOG; KOG1923; Eukaryota.
DR   InParanoid; A0A1U7RZ27; -.
DR   OrthoDB; 471257at2759; -.
DR   Proteomes; UP000189705; 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; IPR014767; DAD_dom.
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   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; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT   DOMAIN          35..476
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          651..1042
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1079..1113
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1105..1125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..481
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..637
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1108..1125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1125 AA;  125861 MW;  3D0CA7310D2BF880 CRC64;
     MGNAAGSMEQ SPGKEAKAQA PGSGLPAKQP APPKQPMPSE GELEERFSRV LNSMNLPPDK
     MKLLSQYDNE KKWDLVCDQE RVQVKNPPSA YIQKLKSYLE TGGVSRKVTP DWSTALFKRR
     VQESTQVLRE LEISLRTNYI GWVQEFLNEE NKGLDVLLEY LAFAQCSVTY DMESTDNGSP
     GSDKGKPLDR SVEDLTKSNS SSPTQGSSKA RHLTVRLNPT HSRKALRNSR IVSQKDDVHV
     CIMCLRAIMN YQSGFSLVMN HPACVNEITL SLNNKNPRTK ALVLELLAAV CLVRGGHDII
     LAAFDNFKEV CGEKNRFEKL MEYFRNEDSN IDFMVACMQF INIVVHSVEN MNFRVFLQYE
     FTHLGLDEYL ERLRHTESDR LQVQIQAYLD NIFDVGALLE ETETKNAVLE HMEDLQEQVA
     QLTEKLQDSE NESMAKIAEL EKQLNQARRE LEMLRDQLSE SASPVSSPLQ PPPPSQPQPQ
     PPTESYRSAL EQKLEELEDK GLVRILRGPE GDVAIEIVPV VIETPIVPVV TIEASASTST
     DFLSPSTPLP PPSPAAAPAL PPPPPPLPPT KDAGPPTPSS EQQSLPSPPP PAPPLPGVDT
     PPPAPPLPGV EIPPPPPLSA TNGPAPPPPP PPPMGQPLGG SLITAASSVK VKKTIQTKFR
     MPIFNWVALK PNQINGTVFN DLNDEKILEE LDMNDFEEHF KTKAQGPSLD IGTLKTKATQ
     KAPSKVTLIE SNRAKNLAIT LRKGGFSIDS ICKAIQTYDL QTLSLDFLEL LERFLPTEYE
     LLQIRKYEKE QRPLDELSDE DQFMIKFSKL PRLAERMNVM TFLGNFSDTA QRLMPQLHSI
     IAASMSIKSS TKLRNILEIV LAFGNYLNSS KRGAAYGFRL QSLDALLEMK STDRKQTLLH
     YMVRVINDKY PELTGFHTEL HFLDKAGTVS LDSMLQDVRS LQQGMELTRK EFMRQDDSQV
     LKDFLKANTE VMEKLQTDGK TAKEAYESVV EYFGENPKTT PPTMFFPTFM RFIKAYKQAE
     QDIEMWKKQE AAAKEAESNP PSNENQSGQK SPVQKAKRQQ MDMLAELKKR QMVKEPLIYE
     GKDGAIEDII TGLRNNPYRR ADITRCSGKK RSSGQTLQVT SDISL
//