ID G1MFK8_AILME Unreviewed; 992 AA.
AC G1MFK8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Formin like 2 {ECO:0000313|Ensembl:ENSAMEP00000018138.2};
GN Name=FMNL2 {ECO:0000313|Ensembl:ENSAMEP00000018138.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000018138.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000018138.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000018138.2}
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; G1MFK8; -.
DR Ensembl; ENSAMET00000018874.2; ENSAMEP00000018138.2; ENSAMEG00000017147.2.
DR GeneTree; ENSGT00940000155515; -.
DR HOGENOM; CLU_003597_0_0_1; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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; 1.
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:SF5; FORMIN-LIKE PROTEIN 2; 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; 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:UP000008912}.
FT DOMAIN 1..437
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 514..905
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 489..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..446
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 879..910
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 489..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 113895 MW; A84DBD48D240CC61 CRC64;
MLIKDALNAM NLPPDKARLL RQYDNEKKWE LICDQERFQV KNPPHTYIQK LKGYLDPAVT
RKKFRRRVQE STQVLRELEI SLRTNHIGWV REFLNEENRG LDVLVEYLSF AQYAVTFDFE
SVESAVESSV DKSKPWSRSI EDLHRGSNLP SPVGNSVSRS GRHSALRYNT LPSRRTLKNS
RLVSKKDDVH VCIMCLRAIM NYQYGFNMVM SHPHAVNEIA LSLNNKNPRT KALVLELLAA
VCLVRGGHEI ILSAFDNFKE VCGEKQRFEK LMEHFRNEDN NIDFMVASMQ FINIVVHSVE
DMNFRVHLQY EFTKLGLDEY LDKLKHTESD KLQVQIQAYL DNVFDVGALL EDAETKNAAL
ERVEELEENI SHLSEKLQDT ENEAMSKIVE LEKQLMQRNK ELDVVREIYK DANTQVHTLR
KMVKEKEEAI QRQSTLEKKI HELEKQGTIK IQKKGDGDIA ILPVVASGTL STGSEVAVGN
FVGPVTGVAP SGPLPPPPPP LPPSSDTPEA AVKIKKPIKT KFRMPVFNWV ALKPNQINGT
VFNEIDDERI LEDLNVDEFE EIFKTKAQGP AIDLSSSKQK ITQKGSNKVT LLEANRAKNL
AITLRKAGKT ADEICKAIHV FDLKTLPVDF VECLMRFLPT ENEVKVFRLY ERERKPLENL
SDEDRFMMQF SKIERLMQKM TIMAFIGNFA ESIQMLTPQL HSIIAASVSI KSSQKLKKIL
EIILALGNYM NSSKRGAVYG FKLQSLDLLL DTKSTDRKQT LLHYISNVVK EKYHQVSLFY
NELHYVEKAA AVSLENVLLD VKELQRGMDL TKREYTMHDH NTLLKEFILN NEGKLKQLQD
DAKIAQDAFD DVVKYFGENP KTTPPSVFFP VFVRFVKAYK QAEEENELRR KQEQALMEKL
LEQEALMEQQ DPKSPSHKSK RQQQELIAEL RRRQVKDNRH VYEGKDGAIE DIITALKKNN
ITKFPNVHSR VRISSSTPVV EDTQSWQASL FT
//
