ID A0A2K5D2T3_AOTNA Unreviewed; 1598 AA.
AC A0A2K5D2T3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Intersectin 1 {ECO:0000313|Ensembl:ENSANAP00000015264.1};
GN Name=ITSN1 {ECO:0000313|Ensembl:ENSANAP00000015264.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000015264.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000015264.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSANAT00000033101.1; ENSANAP00000015264.1; ENSANAG00000025399.1.
DR GeneTree; ENSGT00940000157065; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
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 GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd08375; C2_Intersectin; 1.
DR CDD; cd00052; EH; 2.
DR CDD; cd13264; PH_ITSN; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11989; SH3_Intersectin1_2; 1.
DR CDD; cd11991; SH3_Intersectin1_3; 1.
DR CDD; cd11993; SH3_Intersectin1_4; 1.
DR CDD; cd11995; SH3_Intersectin1_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; 2.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR032140; INTAP.
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; PF12763; EF-hand_4; 2.
DR Pfam; PF16617; INTAP; 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 PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 2.
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; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 5.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 21..100
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 53..88
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 221..310
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 254..289
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 790..848
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 879..937
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 951..1015
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1032..1091
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1114..1300
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1339..1448
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1456..1572
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 322..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..509
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 330..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1598 AA; 180901 MW; B4055D561BC6A85C CRC64;
MAQFPTPFGG SLDIWAITVE ERAKHDQQFH SLKPISGFIT GDQARNFFFQ SGLPQPVLAQ
IWALADMNND GRMDQVEFSI AMKLIKLKLQ GYQLPSALPP VMKQQPVAIS SAPAFGMGGI
ASMPPLTAVA PVPMGSIPVV GMSPPLVSSV PTAAVPPLAN GAPPVIQPLP AFAHSAATLP
KSSSFSRSGP GSQLNTKLQK AQSFDVASVP PVAEWAVPQS SRLKYRQLFN SHDKTMSGHL
TGPQARTILM QSSLPQAQLA SIWNLSDIDQ DGKLTAEEFI LAMHLIDVAM SGQPLPPVLP
PEYIPPSFRR VRSGSGISVI SSTSVDQRLP EEPVLEDEQQ QLEKKLPVTF EDKKRENFER
GNLELEKRRQ ALLEQQRKEQ ERLAQLERAE QERKERERQE QERKRQLELE KQLEKQRELE
RQREEERRKE IERREAAKRE LERQRQLEWE RNRRQELLNQ RNKEQEDIVV LKAKKKTLEF
ELEALNDKKH QLEGKLQDVR CRLTTQRQEI ESTNKSRELR IAEITHLQQQ LQESQQMLGR
LIPEKQILND QLKQVQQNSL HRDSLVTLKR ALEAKEIARQ QLRDQLDEVE KETRSKLQEI
DIFNNQLKEL REIHSKQQLQ KQKSLEAERL KQKEQERKII ELEKQKEEAQ VDESQTGEPG
WLGGELKGKT GWFPANYAEK IPENEIPAPV KPVTDSTSAP APKLALRETP APLTVTSSEP
SMTTNNWADF SSTWPTSTNE KPETDNWDAW AAQPSLTVPS AGQLRQRSAF TPATATGSSP
SPVLGQGEKV EGLQAQALYP WRAKKDNHLN FNKNDVITVL EQQDMWWFGE VQGQKGWFPK
SYVKLISGPI RKSTSMESGS SESPASLKRV ASPAAKPAVS GEEFIAMYTY ESSEQGDLTF
QQGDVILVTK KDGDWWTGTV GDKSGVFPSN YVRLKDSEGS GTAGKTGSLG KKPEIAQVIA
SYTATGPEQL TLAPGQLILI RKKNPGGWWE GELQARGKKR QIGWFPANYV KLLSPGTSKI
TPTEPPKSTA LAAVCQVIGM YDYIAQNDDE LAFNKGQIIN VLNKEDPDWW KGEVNGQVGL
FPSNYVKLTT DMDPSQQWCS DLHLLDMLTP TERKRQGYIH ELIVTEENYV NDLQLVTEIF
QKPLMESELL TEKEVAMIFV NWKELIMCNI KLLKALRVRK KMSGEKMPVK MIGDILSAQL
PHMQPYIRFC SRQLNGAALI QQKTDEAPDF KEFVKRLAMD PRCKGMPLSS FILKPMQRVT
RYPLIIKNIL ENTPENHPDH SHLKHALEKA EELCSQVNEG VREKENSDRL EWIQAHVQCE
GLSEQLVFNS VTNCLGPRKF LHSGKLYKAK SNKELYGFLF NDFLLLTQIT KPLGSSGTDK
VFSPKSNLQY KMYKTPIFLN EVLVKLPTDP SGDEPIFHIS HIDRVYTLRA ESINERTAWV
QKIKAASELY IETEKKKREK AYLVRSQRAT GIGRLMVNVV EGIELKPCRS HGKSNPYCEV
TMGSQCHITK TIQDTLNPKW NSNCQFFIRD LEQEVLCITV FERDQFSPDD FLGRTEIRVA
DIKKDQGSKG PVTKCLLLHE VPTGEIVVRL DLQLFDEP
//
