ID U3I1G5_ANAPP Unreviewed; 677 AA.
AC U3I1G5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Fermitin family member 1 {ECO:0000313|Ensembl:ENSAPLP00000001085.2};
GN Name=FERMT1 {ECO:0000313|Ensembl:ENSAPLP00000001085.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000001085.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000001085.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000001085.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the kindlin family.
CC {ECO:0000256|ARBA:ARBA00008052}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; U3I1G5; -.
DR STRING; 8840.ENSAPLP00000001085; -.
DR Ensembl; ENSAPLT00000001656.2; ENSAPLP00000001085.2; ENSAPLG00000001367.2.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; CLU_011611_0_0_1; -.
DR OMA; GMFFCAP; -.
DR Proteomes; UP000016666; Chromosome 3.
DR GO; GO:0071944; C:cell periphery; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0051546; P:keratinocyte migration; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0051886; P:negative regulation of timing of anagen; IEA:Ensembl.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0033625; P:positive regulation of integrin activation; IEA:Ensembl.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; IEA:Ensembl.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13205; FERM_C_fermitin; 1.
DR CDD; cd17180; FERM_F0_KIND1; 1.
DR CDD; cd17183; FERM_F1_KIND1; 1.
DR CDD; cd01237; PH_fermitin; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR037843; Kindlin/fermitin.
DR InterPro; IPR040790; Kindlin_2_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037837; PH_Kindlin/fermitin.
DR PANTHER; PTHR16160; FERMITIN 2-RELATED; 1.
DR PANTHER; PTHR16160:SF12; FERMITIN FAMILY HOMOLOG 1; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF18124; Kindlin_2_N; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF47031; Second domain of FERM; 2.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666}.
FT DOMAIN 377..473
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
SQ SEQUENCE 677 AA; 77432 MW; 0E246E5AF97C43AA CRC64;
MTSLGAYGSN SWELLVSVDH QNEEKQKEFT LQVTGDLHIG GVMLKLVEQI EMTQDWSDYA
LWWEQKKCWL LKTHWTLDKC GVQADAKLLF TTQHKMLRLR LPNMKTVRLK VSFSSVVFKA
VSDICKILNI RRSEELSLLK QSEDAIRKKK KKDKNNKEPV TEDILNLCNS PVSSGLSASP
GLYSKTMTPT YDPISGTPAS STITWFSDSP LTEQNCNILA FSHPICSPET LAEMYQPRTL
ADKARLNAGW LDSSRSLMEQ GILEDDQLLL RFKYYTFFDL NPKYDAVRIN QIYEQARWAI
LLEEVDCTEE EMLIFAALQY HISKLSSSSE TQNFPGESEV DEIEAALSNL EVALEGGKTS
NILEDITDIP KLADYLRLVR PRKLSIKSIK PYWFVFKDTS VSYFKNTESS HGEPIEKLNL
KGCEVVPDVN VAAKKFGIKL LIPVADGMNE LYLRCENENQ YARWMAACVL ASKGKTMADS
SYRPEVHKIL SFLKMKNWTM SPQAVSDPEN VDMKPECFVS LRYTKKYKSK QLAARILEAH
QNVSQMSLVE AKMRFIQAWQ SLPEFGLSYY IVRFKGSKKD DVLGVSYNRL IRIDIATGDP
ITTWRFSNMK QWNVNWEIRQ VAIEFDQNVS IAFTCLSADC KSIHEYIGGY IFLSTRSKDH
NETLDEELFH KLTGGQE
//