FMN_CHICK
ID FMN_CHICK Reviewed; 1213 AA.
AC Q05858;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Formin;
DE AltName: Full=Limb deformity protein;
GN Name=LD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Embryo;
RX PubMed=1730407; DOI=10.1101/gad.6.1.14;
RA Trumpp A., Blundell P.A., de la Pompa J.L., Zeller R.;
RT "The chicken limb deformity gene encodes nuclear proteins expressed in
RT specific cell types during morphogenesis.";
RL Genes Dev. 6:14-28(1992).
CC -!- FUNCTION: Is important for morphogenesis of limb and kidney and may be
CC involved in determining dorsoventral neural tube polarity and motor
CC neuron induction. It may also have a function in differentiated cells
CC or be involved in maintaining specific differentiated states.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q05858-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Present in the adult brain, kidney, brain, heart
CC and intestine and throughout the embryo.
CC -!- DEVELOPMENTAL STAGE: In the developing limb bud, the protein is
CC expressed in the apical ectodermal ridge and the mesenchymal
CC compartment, predominantly in the posterior region. During kidney
CC morphogenesis, expression is initially restricted to the epithelial
CC compartment of the pronephros and mesonephros.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000305}.
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DR EMBL; X62681; CAA44555.1; -; mRNA.
DR PIR; S24286; A41724.
DR RefSeq; NP_989754.1; NM_204423.1. [Q05858-1]
DR AlphaFoldDB; Q05858; -.
DR SMR; Q05858; -.
DR DIP; DIP-168N; -.
DR STRING; 9031.ENSGALP00000015810; -.
DR PaxDb; Q05858; -.
DR PRIDE; Q05858; -.
DR GeneID; 386747; -.
DR KEGG; gga:386747; -.
DR CTD; 342184; -.
DR VEuPathDB; HostDB:geneid_386747; -.
DR eggNOG; KOG1922; Eukaryota.
DR InParanoid; Q05858; -.
DR PhylomeDB; Q05858; -.
DR PRO; PR:Q05858; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR001265; Formin_Cappuccino_subfam.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR00828; FORMIN.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Developmental protein; Nucleus;
KW Reference proteome.
FT CHAIN 1..1213
FT /note="Formin"
FT /id="PRO_0000194885"
FT DOMAIN 652..751
FT /note="FH1"
FT DOMAIN 766..1182
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..450
FT /evidence="ECO:0000255"
FT COILED 503..572
FT /evidence="ECO:0000255"
FT COILED 1050..1125
FT /evidence="ECO:0000255"
FT COMPBIAS 73..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..703
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..753
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 135241 MW; ADE3EF0B3FB9D862 CRC64;
MEGGNAGCSR QLPERAGPAE SEPDVFTTFA VRTLLGLTTK LESVTPKEEE AVLKAFQPLH
IDVNTQANNR YERNDNDGVD DSENQHCESC TSDQADPMSG SRAEPELEPE PAGQNEILLP
HLRSVQTSLS ESDNDAILVQ GTLVHTTSDT ESDGESKDPD ADETGTSKCG LNNAALSAVA
LDGNNQSKEE SDSEGYGHSD DTVGRDDTEL HPPISQWLPR KLDSILEHDS SGKDRTLMDE
QFSCLLATGE CSPELSGEDQ RPSADNVSFH KAALTERSFQ LPAFFSGLRV RKKGLNTEDG
ETITEIKPRE NDLALLKLRQ PVKKSNITSG LTTKKKSSEP KASPTFLEQL SHLLNIDVSK
NDERTQDSGA GFGETEDSDE GPENKASGQT EPLFPSEEIK SSPAESALDV FKALFTRPPK
KETTADPSEL EAIKRKMRNE KESLKAVFER SKSKPGDGPS DKSPDLSPSE QDDKTPGRLQ
TVWPPPKANH EEVKVGLKYT EAEYQAAILH LKREHKEEIE TLKSQFELRV FHIRGEHAVS
TAQLEETIAH LKNELDNKLN RRNEEARDIG VSTEDDNLPK TYRNVCIQTD RETFIKPSEE
ENRAVKNNQI VPKKLNISSL THSISTQGEN KDSYDVPSSE SVLSCQPKQM LPPSPPPPPP
PPPPPPPPPP PFSDSSLPGL VPPPPPLPTG PTSVTPHFAF GPPLPPQLSE GCRDFQAPAP
PAPPPLPGLG PPVPPPLPGS GLPPPPPPPG PGLFFNSTLS SSQGPRKPAI EPSRPMKPLY
WTRIQLQGSR KTAIPTLWES LEEPDILDTT EFEYLFSKDT TQEKRKPLSE TYEKKTKAKK
IIKLLDGKRS QTVGILISSL HLEMKDIQQA ILCVDDSVVD LETLEALYEN RAQKDELEKI
EQYYQTSKEE ELKLLDKPEQ FLYELSQIPN FTERAQCIIF QSVFSEGITS VHRKVDIITR
VSKALLNMTS VKEILGLILA FGNYMNGGNR TRGQADGFGL EILPKLKDVK SRDNRINLVD
YVVIYYLRHC DKEAGTDKSI FPLPEPQDFF QASQVKFEDL IKDLRKLKRD LEASEKQMKL
VCRESSEEHL QPFKEKLEEF FQKAKEERKK EESSLENAQK CFEETVGYFG IKPKPGEKEI
TPNYVFTVWY EFCSDFKTIW KRESKSISKE RIKVAQQSVS KLTAEKKVET KKINPTASLK
ERLRQKEANV NAN
