ID A0A1I8JSV8_ANOAL Unreviewed; 1149 AA.
AC A0A1I8JSV8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AALB015869-PA};
OS Anopheles albimanus (New world malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB015869-PA, ECO:0000313|Proteomes:UP000069272};
RN [1] {ECO:0000313|EnsemblMetazoa:AALB015869-PA}
RP IDENTIFICATION.
RC STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB015869-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell projection, rhabdomere
CC {ECO:0000256|ARBA:ARBA00043944}.
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DR AlphaFoldDB; A0A1I8JSV8; -.
DR STRING; 7167.A0A1I8JSV8; -.
DR EnsemblMetazoa; AALB015869-RA; AALB015869-PA; AALB015869.
DR EnsemblMetazoa; AALB015869-RB; AALB015869-PB; AALB015869.
DR VEuPathDB; VectorBase:AALB015869; -.
DR VEuPathDB; VectorBase:AALB20_025891; -.
DR Proteomes; UP000069272; Chromosome 2R.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13193; FERM_C_FARP1-like; 1.
DR CDD; cd17098; FERM_F1_FARP1_like; 1.
DR CDD; cd13235; PH2_FARP1-like; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FA.
DR InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45858; FERM DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45858:SF5; MOESIN_EZRIN_RADIXIN HOMOLOG 1; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 3.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658}.
FT DOMAIN 50..335
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 656..840
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 869..960
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1031..1128
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 378..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 130622 MW; 1DB8637F88A92049 CRC64;
MSLDSMGPSA GGGSSGVGTL SGTRMIHSLS TPSGVDGSVS ASHSRSGKKL AVRIQMLDDS
VTMFQVQAKA TGKVLFEQVC RQLNLLEADY FGLEYQEAST GTKYWLDLEK SLNRQVGLSL
VEPMLRFCVK FYTPDPLQLE EEYTRYLFCL QVKRDLATGS LQCNDNTAAL MASYIVQASC
GDYAVEDYPD HTYLSSYRFV PQQDHTMQRR IMENHKKHVG QSPAEADLNL LETARRCELY
GMKMHPAKDH DGVPLNLAVA HMGIAVFQGI TRINTFSWAK IRKISFKRKR FLIKLHPENY
VYHKDTVEFF FEGRNECKNF WKKCVENHGF FRCTAVQNVQ RRKARVLSRG SSFRYSGKTQ
KQIIEFVRDN YVKRQTFQRS QSFRQGPLHS SNRSQSRTSC NVNQSISAHP LLPIETAEWE
RRSQNNVLRT PSQTRRQADT VADHRPSSPT GLTRSQLTEA QVETYPMKSY TQMGMESRES
GPMHHNQDSS QSASPGGTWS SPYHNNSHSS SHAREADRAR ARQDGHSSDD YHGINGNVSL
DRRSEIVQSP NRFELALGTA DKSNNNSLSR ETGSYDLSSA EARARNGHFG GSNGGALHTV
DENVINNNYQ NTQSLTAGNG GSGGRGEAGV GTGPNNSGTL RSMDEELRKK KWPTDRAYFL
AKELLMTERT YKKDLDVINT WFREELTPED LENLQPLFQY FESMLEHHSV FLRDLEHRIL
LWEGRGGHET HRIGDVMLKN MVVLPIYDEY VESHREILER LNDLYDNDDK FQQTYRDFEQ
QKVCYLPICY FILKPLHRLL HYELLLELLL AHYGDDHFDR TDCHGTLMML TRTTEVIRRE
LTASENHSLL CEIQRDIEGY DSLVQPDRKL IRQGCLLKHS KRGLQQRMFF LFSDILLYAV
KSPVTQTFKV LGHVPVRSLL TENAEHNAFV IFGGQRALTV SAGTTIEKTL WLEELAKAAN
SLKYKPQTQL PIVTIKTCTS SEENLEACGL NSALVPQKPV KPPSSRNNTA LHVCWHRGVT
ICLDDHLRSG RNQISGYLLR KFKNSSGWQK LWVVLTSFCL YFYKSYSDDA ALASLPLLGY
TVGPPGIQDA VQKEYVFKLS FKNHTYFFRA ESEHTYNRWM EVLRSATQIQ ESRASPSITS
LGNSNNGSK
//
