ID A0A226MMV3_CALSU Unreviewed; 1189 AA.
AC A0A226MMV3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=Formin like 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASZ78_003937 {ECO:0000313|EMBL:OXB56646.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB56646.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB56646.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB56646.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB56646.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000256|ARBA:ARBA00005271}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXB56646.1}.
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DR EMBL; MCFN01000626; OXB56646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226MMV3; -.
DR STRING; 9009.A0A226MMV3; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; 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; IPR001265; Formin_Cappuccino_subfam.
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; 2.
DR PRINTS; PR00828; FORMIN.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000198323}.
FT DOMAIN 41..517
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 685..1106
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1143..1177
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..480
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..640
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 131389 MW; 763099F431FD89C0 CRC64;
MGNAAGGMEG AAARENRDPR APGPNAAAAA TPPRPPPPAR LPMPAADELE ERFSRVLSSM
NLPPDKMKLL SQYDNEKKWE LVCDQERFQV KNPPSAYIQK LKSYLDTGGV SRKFKRRVQE
STQVLRELEI SLRTNYIGWV QEFLNEENKG LDVLLEYLAF AQCSVAPGCS HMSAGIEVSP
CPSISVPTWD TRYDMESTEN GSPGSEKGKP LEQSVEDLSK SNSSSPTHGI SKVRHLTVRL
NPSHSRKALR NSRIVNQKDD VHVCIMCLRA IMNYQSGFSL VMNHPACVNE ITLSLNNRNA
RTKALVLELL AAVCLVRGGH DIILAAFDNF KEVCGEKNRF EKLMEYFRNE DSNIDFMVAC
MQFINIVVHS VENMNFRVFL QYEFTHLGLD QYLESLRLTE SDKLQVQIQA YLDNIFDVGA
MLEDSETKTA GLEHMEELEE RVSQLTEKLQ DAENDSMAKI AELEKQLSQA RRELEALREQ
LSPPRPPSPP APQPQECYWL ALERRLAELE EKGLVQILRG PDGDVAIEIV PVVIETTAAP
VVTGEATATS TDTSAPPPSP APAPAAPPPP PPPPPPPLPG AEPVPSVPPA PPLPTGITPP
PAPPLPGAQV PPPPPPLPGG LEGPVPPPPP PPPLCGQPHT GPGAPPAANG SGEWGLGCTD
VSANTLRWGL APPVTLPCSH PAVKVKKPIQ TKFRMPVFNW VALKPSQIDG TVFTELNDEK
VLQELDMSDF EEQFKTKAQG PGLDISALKV KATQKAPSKV TLMESNRAKN LAITLRKGGR
SIQDICTAIE TYDQQALSLD FLELLLRFLP TEYERTLIGK FEREQQSPEE LSEEDQFMVR
FSKIPRLAER MNVMIFLGNF NDTAQLLMPQ LNAIIAASMS LKSSSKLRNI LEIVLAFGNY
MNSSKRGAAY GFRLQSLDAR DVGTSYGEGG LPQAGGSGRW GGADTALSQL LEMKSTDRKQ
TLLHYLVRVI TEKYPELTGF HTELHFLDKA GTVSLDGVLQ DVRSLQQGME LTRKEFMRQD
DSLVLKEFLK TNTELMEKLQ ADSKTAKEAY ESAVEYFGEN PKTSPPTTFF PMFMRFIRAY
KKAEQDIELW KKQEAAAKEA ESGSPCSEEQ LDLKSPFQKA KRQQMDMIAE LKKKQMVKEP
LIYEGKDGAI EDIISDLRNN PYRRADKGRG SAKKRTAGQS LQATADIAL
//
