ID A0A3B5QJS9_XIPMA Unreviewed; 1490 AA.
AC A0A3B5QJS9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Formin-2-like {ECO:0000313|Ensembl:ENSXMAP00000030772.1};
GN Name=FMN2 {ECO:0000313|Ensembl:ENSXMAP00000030772.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000030772.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000030772.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000030772.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000256|ARBA:ARBA00005271}.
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DR Ensembl; ENSXMAT00000042085.1; ENSXMAP00000030772.1; ENSXMAG00000025975.1.
DR GeneTree; ENSGT00940000161899; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR001265; Formin_Cappuccino_subfam.
DR PANTHER; PTHR13037; FORMIN; 1.
DR PANTHER; PTHR13037:SF16; FORMIN-2; 1.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR00828; FORMIN.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT DOMAIN 1051..1466
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 743..770
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1490 AA; 162296 MW; 4FF0F0E1D943C961 CRC64;
MGNQEAKQKR AAPSSGNGSY PSLNEGWREG GGDLTKRGGK KLGKQGGKGT NSSGGGGTHG
TGPGKKRNKS DSKSSVFSLR KRKINLKGKG DTCSSIPGLN EDDWASQHDD LDSTKTPDLS
ADELGHSDSE AAFPEKRKKS EQENRNKDRR EDEKSHVQLK ASTETTSPTE EAGQKGGSSG
SDTDIYSFHS AADHEDLLAD IQLAIRLQHQ QQHDGENAIS EVHAGGAGDL NWRAAEEWTK
KSNRVEKETH QEVLGMTPEL EVGSDALSFL ETESHVSVNH TDSLPMLSSR ETYLSSHTEM
KGQGEVQKGL GPPKLSMKTR EGQAFLCIAT GTKDQHVDIS MATGSLTVSP ITMATCDNCS
PIVSIDSEGK CLGMVEEAEF SPPPVSNSKS TEHAEGFSSG AVFDEGDGQL GSGTSAESLE
DCVLTGSKSN QCAASCNGFS PSDQLCSRDS ICFITLTPQG SPKLAKQLLK STHSSNFYSH
VVKSYPTIFP SYIKTTTRQL STPGQSPALS PSHSPLSPRR AHLHNRRMVA GEHETHRQRS
LSLTGTLSRS ADWTEELEKR LRGREVDGGE YLMGYRGGGS QPICATRRSS CGQVSLCAFQ
DVFTGRTLLE KLFLQQQQKE PEEAERLCSK ILAMGLLLPF TDCFREQLGG STAQISSTAS
AKFDHDQLYT WAAVNQPPHS LDLLEGKLAG QLKTQWSPLR LGENRTGHKS MGADHCEAVP
TTRQQDSEER SGGEYVLPSK KLKEKHVDVI QQLEQTIEDL RTKIAELERQ PPLLEEKGIT
TITSTTDGEC GGDESLLRSL CDAHLQTEAG ASLGCQEVKS VQTSPMDDSF RFNRFCRGLD
GGFLQPSSNH DCSCQLDPCT SPLLHQGETV ILHSCLNLVP PPPPPPPLPG FPYPPPPPPL
PPPPLFPGLP GPPLPPPSPP PPGFPGPPPP PPPLPGFPGP PPPPPPPPLP GFPGPPPPPP
PPPLPGFPGP PPPPPPLSLP GFPGPPPPPP PPPPLPGCSG PPHPPPGCGP PPPPPGATGV
PPSLPAVMGS LPPPMPLGLY SLPLTQDKPT RKAAVEPPRP MKPLYWTRIQ LHTKRDIPSS
LVWELVEEPD VDFDEFVALF SKTAVKEKKQ PLSDTITKSK AKQVAKLLNN KRSQAVGILM
SSLHLDMKDI QHAVLNLDNN VVDTETLQAL YENRAQQEEL DKIEKHIKSS KDKENAKPLD
KPEQFLYQLS LIPDFSSRVF CILFQSSFCE CMSSITRKIN TLQRVCKTLQ DNVSVKKILG
LVLAFGNFMN GGNRTRGQAD GFTLEILPKL KDVKSNDGAK SLLSYIVAYY LRHFDEDAGK
ETSVFPLPEP HDLFQVSQMK FEDFQKDFIR LRKDLRACTS EVEKVCKVSD EDNLQPFKEK
MDAFLAQAKS ELEILDAQLS STHKLFIELT VFYSVKPKAG EKEASPNTLF SIWHEFSSDF
KDQWKKENKT ILKERLKAAE ECFRQAKEKT SYSVKPKHAS GIKAKLGMKI
//
