ID F4X5V6_ACREC Unreviewed; 1258 AA.
AC F4X5V6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2 {ECO:0000313|EMBL:EGI58196.1};
DE Flags: Fragment;
GN ORFNames=G5I_13747 {ECO:0000313|EMBL:EGI58196.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI58196.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL888742; EGI58196.1; -; Genomic_DNA.
DR AlphaFoldDB; F4X5V6; -.
DR STRING; 103372.F4X5V6; -.
DR EnsemblMetazoa; XM_011067833.1; XP_011066135.1; LOC105153152.
DR eggNOG; KOG2642; Eukaryota.
DR InParanoid; F4X5V6; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR CDD; cd11779; SH3_Irsp53_BAIAP2L; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2; 1.
DR PANTHER; PTHR14206:SF7; INSULIN RECEPTOR SUBSTRATE 53 KDA, ISOFORM A; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..157
FT /note="IMD"
FT /evidence="ECO:0000259|PROSITE:PS51338"
FT DOMAIN 267..328
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 161..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGI58196.1"
SQ SEQUENCE 1258 AA; 144132 MW; C9034B770FFEAC80 CRC64;
LKAFYVDLLV PLETNLEKDT KVVQSEQKKF LQQHKTRSET YSKAAATMKK QRKKSRAANK
SGLAMDKELK NMQILEEEKT KLDAFCEQSL KNAMTQERRR YGFVLERQCS LAKHYASFHE
VALAALHPSV DKWREVAATR EYLPQSVEDM FASRLRQTSF WPEDEENGGS ELTTMSSQLR
KTRSMDSSCL ELRLGPLPGN PPSGGHLGPA LHLPTALSRA RSEANLHAST LSLGPEVPET
PPRPRSMAPP TSRSSAGGTG IGAGGWSDAP LARALFAYLS SGENQLSFLE GDLIALMGDR
QKGWQFGENL RTQSSGWFPL AYTEIIIDDT LGSPSHGASH GRTPEPQAIP PCKPPPSRPP
VTPASIDESS GGTPGAGSSS ANNNTNANNN SSSNAGTPTN TASVLATPTA RQSKSIRPSG
TLPAVLAGGR RVQPPVPPVP PPAMTSLHSS NDSGFSNEPP VQPDVDYSDD EALRRRRKPR
SGEDRPSSKD EKRSKDWEND SWKTIPRDEK SWQLYRTAMD LWAESKANQV SEEDSKKYFE
MENGEFTLEN GDTKKRKNKK AAQALNERPN PNQRTKMTDE RNAPAATRRG DQRRVDKRTQ
VETEEDELEE DEEDFVAEYR SNNKYYADNQ EAQQERRGGG SFEAEKYAKS TSSSSNSDDE
STITIPEPGR KVEHIAQKLE QTAQKYAREH SPPKFLDRRE RSTAAEYKSL ERETREMALS
RDRRERLVME YKSLERARDS GQKNLEQARR DDKMRLRDDK RARDDKHSLE RSSREDKTNF
DRTRDDKQSF ERSREEKQNL ERTREDKQGF ERSREDKAFD RPREDKQSFQ RTREDTQSYE
RARTRSKNEQ DRGYVDQRKE VMGYERTFEK NRNRTIERLS SRRFERPRPP SQEAPERPSM
GPYRERRYSD KEEAIYGETG RYGISSLERD RGYESNFETK LERTKAIERH GYTGLHGSDL
QKQNVSRINE RSNGDTNNNT LKVERKSVLP RQAAAMGHLV QTERAFDESK SPKLVKRTKS
FWKFRRDSEV LEGMALWQHR SLVDIPKMIR KEDKTAENEE RQRNSEGGSP NSSLGNSEGT
ITNEHRHEEP KPAERSHVPD KTDYFEDFPT PAERSKITER SEYRMQHQPQ EERTYFIGNV
SRKAIIEKER RRSLEAKRNM IVAELKENNE NKRHGMARSR RNYDEEDATL NFSETEASDE
ESTYSCIVVK DQSIPEKTLL PRTKLRRESD RDRNNCGPWY DLWGMDASVN KKKKQKQQ
//
