ID A0A1V4J2U0_PATFA Unreviewed; 1580 AA.
AC A0A1V4J2U0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Intersectin-1 isoform B {ECO:0000313|EMBL:OPJ66450.1};
GN Name=ITSN1 {ECO:0000313|EMBL:OPJ66450.1};
GN ORFNames=AV530_016513 {ECO:0000313|EMBL:OPJ66450.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ66450.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ66450.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ66450.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ66450.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ66450.1}.
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DR EMBL; LSYS01009367; OPJ66450.1; -; Genomic_DNA.
DR STRING; 372326.A0A1V4J2U0; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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; 1.
DR CDD; cd13264; PH_ITSN; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11987; SH3_Intersectin1_1; 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; 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; 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; 1.
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; SM00027; EH; 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; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 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 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:UP000190648};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 87..176
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 120..155
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 605..666
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 772..830
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 861..919
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 933..997
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1014..1073
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1096..1282
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1321..1430
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1438..1554
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 186..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 221..368
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 196..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1580 AA; 180081 MW; 75578072224BB6FB CRC64;
MAPMPVVGMS PPLVSSVPAA AVPPLANGAP AVIQPLPAFA HPATLPKSSS FSRSGPGSQL
NAKLQKAQSF DVASVPPVAE WAVPQSSRLK YRQLFNSHDK TMSGHLTGPQ ARTILMQSSL
PQAQLATIWN LSDIDQDGKL TAEEFILAMH LIDVAMSGQP LPPVLPPEFI PPSFRRVRSG
SGISAVSSVS VDQRLPEEPA LEEEQQQLEK KLPVTFEDKK RENFERGNLE LEKRRQALLE
QQRKEQERLA QLERAEQERK ERERQEQERK RQLELEKQLE KQRELERQRE EERRKEIERR
EAAKRELERQ RQLEWERNRR QELLNQRNKE QEDIVVLKAK KKTLEFELEA LNDKKNQLEG
KLQDIRSRLC TQRQDIESTN KSRELRIAEI THLQQQLQES QQMLGRLIPE KQLLNDQLKQ
VQQNSLHRDS LLTIKRALEA KELARQQLRD QLDEVEKETR SKLQEIDIFN NQLKELREIH
NKQQLQKQKN LEADRLKQKE QERKTVELEK QKEAQRRIQE RDKQRLDRVQ PEEQLQWPKN
IQEDEKQKRE EITKKNESEE KGKQEMQEKL SKLFQPHQEP IKPAVQAPWS NAEKAPLTIS
AQEDVKIVYY RALYPFESRS HDEITIQPGD IVMVDESQTG EPGWLGGELK GKTGWFPANY
AEKIPENEVP ASVKPTVEAA AAPKVSVHET TTSLGTSAST ECTTTANNWA DFSSTWPANS
SEKPETDNWD AWAAQPSLTV PSAGQLRQRS AFTPAAVTGS SPSPVLGQGE KVEGLQAQAL
YPWRAKKDNH LNFNKNDIIT VLEQQDMWWF GEVQGQKGWF PKSYVKLISG PIRKSTSMDS
GSSESPASLK RVASPATKAT MSGEEYIAMY TYESSEQGDL TFQQGDMILV TKKDGDWWTG
TLGDKSGVFP SNYVRLKDSE APGAAGKTGS LGKKPEIAQV IASYTATGPE QLTLAPGQLI
LIRKKNPGGW WEGELQARGK KRQIGWFPAN YVKLLSPGTS KTTPTDLPKS TALPSVCQVI
GMYDYTAQND DELAFNKGQI INVLNKEDPD WWKGEVNGQV GLFPSNYVKL TTDMDPSQQW
CADLHLLDML TPTERKRQGY IHELIVTEEN YVNDLQLVTE IFQKPLMESE LLTEKEVAMI
FVNWKELIMC NIKLLKALRV RKKMSGEKMP VKMIGDILTA QLPHMQPYIR FCSCQLNGAA
LIQQKTDEVP EFKEFVKRLA MDPRCKGMPL SSFLLKPMQR VTRYPLIIKN IIENTPENHP
DHSHLKHALE KAEELCSQVN EGVREKENSD RLEWIQAHVQ CEGLSEQLVF NSVTNCLGPR
KFLHSGKLYK AKSNKELYGF LFNDFLLLTQ IIKPLGSSGT DKVFSPKSNL QYKMYKTPIF
LNEVLVKLPT DPSGDEPIFH ISHIDRVYTL RAESINERTA WVQKIKAASE LYIETEKKKR
EKAYLVRSQR ATGIGRLMVN IVEGIELKPC RSHGKSNPYC EVTMGSQCHI TKTIQDTLNP
KWNSNCQFFI KDLEQDVLCI TVFERDQFSP DDFLGRTEIR VADIKKDQGS KGPVTKCLLL
HEVPTGEIVV RLDLQLFDEP
//
