ID A0A091Q7R7_LEPDC Unreviewed; 1442 AA.
AC A0A091Q7R7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Intersectin-2 {ECO:0000313|EMBL:KFQ15596.1};
DE Flags: Fragment;
GN ORFNames=N330_03137 {ECO:0000313|EMBL:KFQ15596.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ15596.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ15596.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ15596.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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 EMBL; KK688463; KFQ15596.1; -; Genomic_DNA.
DR PhylomeDB; A0A091Q7R7; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd08375; C2_Intersectin; 1.
DR CDD; cd13264; PH_ITSN; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11988; SH3_Intersectin2_1; 1.
DR CDD; cd11990; SH3_Intersectin2_2; 1.
DR CDD; cd11992; SH3_Intersectin2_3; 1.
DR CDD; cd11994; SH3_Intersectin2_4; 1.
DR CDD; cd11996; SH3_Intersectin2_5; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 5.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR035737; Intersectin-2_SH3_1.
DR InterPro; IPR035738; Intersectin-2_SH3_2.
DR InterPro; IPR035739; Intersectin-2_SH3_3.
DR InterPro; IPR035740; Intersectin-2_SH3_4.
DR InterPro; IPR035741; Intersectin-2_SH3_5.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46006:SF9; INTERSECTIN-2 ISOFORM X1; 1.
DR PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF16652; PH_13; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 5.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..47
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 1..26
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 505..566
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 644..702
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 727..785
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 799..863
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 873..932
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 955..1141
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1180..1289
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1297..1413
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 51..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 299..326
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ15596.1"
FT NON_TER 1442
FT /evidence="ECO:0000313|EMBL:KFQ15596.1"
SQ SEQUENCE 1442 AA; 166519 MW; 84E7526AA1B80651 CRC64;
SLADIDGDGQ LKADEFVLAM HLTDMAKAGQ PLPLTLPLEL VPPSFRSGKY TENINGTLPS
YQPVQEEEPQ KKQPVTFEDK RKANYERGNM ELEKRRQVLL EQQQREAERK AQKEREEQER
RERERQEQER KKQLEMERQL ERQRELERQR EEERRKEIER REAAKQELER QRRLEWERIR
RQELLNQRAR EQEEIVRLTS KKKSLNLELE ALTDKHQQIS GRLQDIRNKK QVQKTELEAL
DRKYDQGIME VKQLQQQLQE YQNKLTYLVP EKQLLSEKIK NSSLENTQST GISSVHKKSL
EKEELCQRLK EQLDALEKET ASKLAEMDVF NSQLKCENMD DSVLQCLLSL LSCLNNLFLL
LKDLRESYST QQLALEQLHR IKQDKIRELE KRKAELAQKK RLEDEAARKA KREKENRWQE
NIRREEEEKK KRLEEERMQE KVQEKLKAEE AVALMREREN KQLHAEEEKN RQATVLRETE
QQRQRQLEED KRKQEQIAKE AEERLALVNY RALYPFEARN HDEMSFNTGD VIQVDEKTVG
EPGWLYGSFQ GHFGWFPCNY VEKIPEGERS LSPKKALLPP TVSLSTTSAA SEPLSPSKSA
EDSDYQNIPF SSLNVNAAWQ QKSAFTRTVS PGSVSPIHGQ GQPVENLKAQ ALCSWTAKKD
NHLNFSKNDI ITVLEQQENW WFGEVHGGRG WFPKSYVKLL PGSEIKKEEP EAVYAAVNKK
PSTQSYAAGE EYVALYSYSS SEPGDLTFTE GEEILVTQKE GEWWTGSIDS RTGIFPSNYV
RPKDQEASSN AGKTGTINKK PEIAQVTTAY AASGTEQLSL APGQLILILK KNASGWWQGE
LQARGKKRQK GWFPASHVKL LGPSSERTAS AAPSVCQVIA MYDYMANNED ELSFSKGQLI
NVLSKDDADW WQGEISGVTG LFPSNYVKMT TDSDPSQQWC ADLQSLDTMQ PMERKRQGYI
HELIQTEERY MDDLQLVLEV FQKPMADSGC LTEGEMGLIF VNWKELIMSN TKLLKALRVR
KKTGGEKMPV QMIGDILAAE LSHMQAYIRF CSCQLNGASL LQQKTDEDAD FKDYLKKLAL
DPRCKGMPLS SFLLKPMQRI TRYPLLIKSI LENTPENHPD HSNLKLALER AEELCSQVNE
GVREKENSDR LEWIQSHVQC EGLAEQPVFN SLTNCLGPRK LLHSGKLYKA KSSKELYGFL
FNDFLLLTYM VKQFVSSGSD KLFSPKSNSQ FKMYKMPVFL NEVLVKLPTD PSSDEPVFHI
SHIDRVYTLK TDNINERTAW VQKIKAASEQ YIETEKKKRE KAYQARSQKT SGIGRLMVHV
IEATELKACK PNGKSNPYCE ISMGSQSYTT RTLQDTLNPK WNFNCQFFIK DLYQDVLCIT
VFDRDQFSPD DFLGRTEVPV AKIRTEQESK GPVTKHLLLH EVPTGEVWVR FDLQLFDQKT
LL
//