ID A0A2K5MRB3_CERAT Unreviewed; 1720 AA.
AC A0A2K5MRB3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Intersectin 1 {ECO:0000313|Ensembl:ENSCATP00000027783.1};
GN Name=ITSN1 {ECO:0000313|Ensembl:ENSCATP00000027783.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000027783.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000027783.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_011892528.1; XM_012037138.1.
DR RefSeq; XP_011892529.1; XM_012037139.1.
DR Ensembl; ENSCATT00000052030.1; ENSCATP00000027783.1; ENSCATG00000036969.1.
DR GeneID; 105575387; -.
DR KEGG; caty:105575387; -.
DR CTD; 6453; -.
DR GeneTree; ENSGT00940000157065; -.
DR OrthoDB; 2910300at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000036969; Expressed in frontal cortex and 12 other cell types or tissues.
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 Pfam; PF14604; SH3_9; 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; 5.
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:UP000233060};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 21..109
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 220..309
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 253..288
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 739..805
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 912..970
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1001..1059
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1073..1137
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1154..1213
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1236..1422
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1461..1570
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1578..1694
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 321..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..508
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 329..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1720 AA; 195388 MW; D6D2726C086FF389 CRC64;
MAQFPTPFGG SLDIWAITVE ERAKHDQQFH SLKPISGFIT GDQARNFFFQ SGLPQPVLAQ
IWALADMNND GRMDQVEFSI AMKLIKLKLQ GYQLPSALPP VMKQQPAISS APAFGMGGIA
SMPPLTAVAP VPMGSIPVVG MSPPLVSSVP TAAVPPLANG APPVIQPLPA FAHPAATLPK
SSSFSRSGPG SQLNTKLQKA QSFDVASVPP VAEWAVPQSS RLKYRQLFNS HDKTMSGHLT
GPQARTILMQ SSLPQAQLAS IWNLSDIDQD GKLTAEEFIL AMHLIDVAMS GQPLPPVLPP
EYIPPSFRRV RSGSGISVIS STSVDQRLPE EPVLEDEQQQ LEKKLPVTFE DKKRENFERG
NLELEKRRQA LLEQQRKEQE RLAQLERAEQ ERKERERQEQ ERKRQLELEK QLEKQRELER
QREEERRKEI ERREAAKREL ERQRQLEWER NRRQELLNQR NKEQEDIVVL KAKKKTLEFE
LEALNDKKHQ LEGKLQDIRC RLTTQRQEIE STNKSRELRI AEITHLQQQL QESQQMLGRL
IPEKQILNDQ LKQVQQNSLH RDSLITLKRA LEAKELARQQ LRDQLDEVEK ETRSKLQEID
IFNNQLKELR EIHNKQQLQK QKSMEAERLK QKEQERKIIE LEKQKEEAQR RAQERDKQWL
EHVQQEDEHQ RPRKLHEEEK LKREESIKKK DGEEKGKQEA QDKLGRLFHQ HQEPAKPAVQ
APWSTSEKGP LTISAQENVK VVYYRALYPF ESRSHDEITI QPGDIVMVKG EWVDESQTGE
PGWLGGELKG KTGWFPANYA EKIPENEVPA PVKTVTDSTS APAPKLALRE TPAPLAVTSS
EPSTTPNNWA DFSSTWPTST NEKPETDNWD AWAAQPSLTV PSAGQLRQRS AFTPATATGS
SPSPVLGQGE KVEGLQAQAL YPWRAKKDNH LNFNKNDVIT VLEQQDMWWF GEVQGQKGWF
PKSYVKLISG PIRKSTSMES GSSESPASLK RVASPAAKPV VSGEEFIAMY TYESSEQGDL
TFQQGDVILV TKKDGDWWTG TVGDKSGVFP SNYVRLKDSE GSGTAGKTGS LGKKPEIAQV
IASYTATGPE QLTLAPGQLI LIRKKNPGGW WEGELQARGK KRQIGWFPAN YVKLLSPGTS
KITPTEPPKS TALAAVCQVI GMYDYTAQND DELAFNKGQI INVLNKEDPD WWKGEVNGQV
GLFPSNYVKL TTDMDPSQQW CSDLHLLDML TPTERKRQGY IHELIVTEEN YVNDLQLVTE
IFQKPLMESE LLTEKEVAMI FVNWKELIMC NIKLLKALRV RKKMSGEKMP VKMIGDILSA
QLPHMQPYIR FCSRQLNGAA LIQQKTDEAP DFKEFVKRLA MDPRCKGMPL SSFILKPMQR
VTRYPLIIKN ILENTPENHP DHSHLKHALE KAEELCSQVN EGVREKENSD RLEWIQAHVQ
CEGLSEQLVF NSVTNCLGPR KFLHSGKLYK AKSNKELYGF LFNDFLLLTQ ITKPLGSSGT
DKVFSPKSNL QYKMYKTPIF LNEVLVKLPT DPSGDEPIFH ISHIDRVYTL RAESINERTA
WVQKIKAASE LYIETEKKKR EKAYLVRSQR ATGIGRLMVN VVEGIELKPC RSHGKSNPYC
EVTMGSQCHI TKTIQDTLNP KWNSNCQFFI RDLEQEVLCI TVFERDQFSP DDFLGRTEIR
VADIKKDQGS KGPVTKCLLL HEVPTGEIVV RLDLQLFDEP
//