ID A0A087QRL5_APTFO Unreviewed; 1645 AA.
AC A0A087QRL5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Intersectin-2 {ECO:0000313|EMBL:KFM03869.1};
DE Flags: Fragment;
GN ORFNames=AS27_03842 {ECO:0000313|EMBL:KFM03869.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM03869.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM03869.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM03869.1};
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; KL225837; KFM03869.1; -; Genomic_DNA.
DR STRING; 9233.A0A087QRL5; -.
DR Proteomes; UP000053286; 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; cd00052; EH; 2.
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 CDD; cd22249; UDM1_RNF168_RNF169-like; 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; 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; PF12763; EF-hand_4; 2.
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; PS50010; DH_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
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 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:UP000053286};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 14..102
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 46..81
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 204..293
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 237..272
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 704..765
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 843..901
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 933..991
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1006..1070
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1080..1139
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1162..1348
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1387..1496
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1504..1620
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 297..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 545..572
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 297..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM03869.1"
FT NON_TER 1645
FT /evidence="ECO:0000313|EMBL:KFM03869.1"
SQ SEQUENCE 1645 AA; 187507 MW; 4606E42BD86A7DCF CRC64;
FLGGPNIWAI TSEERAKHDK QFDSLKPTGG YITGDQARTF FLQSGLPASI LAEIWTLSDL
NKDGKMDQQE FSIAMKLIKL KLQGQHLPAV LPPVMKQTPV FSPLMSARFG MGSMPNLSMP
TSMSTITPLA PMSLTSMTSI PPLVISAPLV PSVSTSSLPN GTSSLLQPLS VPFSSSNSNS
SSSASLAGNS PKIASSDWAV PQASRLKYRQ KFNSLDKSMS GYLSGFQARN ALLQSNLSQT
QLATIWSLAD IDGDGQLKAD EFVLAMHLTD MAKAGQPLPL TLPLELVPPS FRSGKYTENI
NGTLPSYQPM QEEEPQKKQP VTFEDKRKAN YERGNMELEK RRQVLLEQQQ REAERKAQKE
REEQERRERE RQEQERKKQL EMERQLERQR ELERQREEER RKEIERREAA KQELERQRRL
EWERIRRQEL LNQRNREQEE IVKLTSKKKS LNLELEALTD KHQQISGRLQ DVRSKKQIRK
TELEALDKKY DQGIMEVKQL QQQLQEYQNK LIYLVPEKQL LSERIKNAQL ENTQSTGIGS
VHKKSLEKEE LCQRLKEQLD ALEKETASKL AEMAAFNSQL KVHLFSKYLV LKWENKQQLR
SEEEKNRQAT ILRETEQQRQ RQLEEDKRKQ EQIAKEAEER RKQNEEIKKI KEVTNSQEVE
KRTSKLNINE KFADLLKPTE GKSLKPPWKN EGNAVSVSES RNSVALVNYR ALYPFEARNH
DEMSFNTGDI IQVDEKTVGE PGWLYGSFQG HFGWFPCNYV EKIPEGEKSL SPKKALLPPT
VSLSTTSAAP EPLSPSKSAE ESDYQNIPFS SLNVNTAWQQ KSAFTRTVSP GSVSPIHGQG
QPVENLKAQA LCSWTAKKDN HLNFSKNDII TVLEQQENWW FGEVHGGRGW FPKSYVKLLP
GSEIKKEELF FSFCRPEAIY AAVNKKPNTQ PYAAGEEYVA LYSYSSSEPG DLTFTEGEEI
LVTQKEGEWW TGSIDGRTGI FPSNYVRPKT DQEASSNAGK TGTINKKPEI AQVTTAYAAS
GTEQLSLAPG QLILILKKNA SGWWQGELQA RGKKRQKGWF PASHVKLLGP SSERTTSAAP
SVCQVIAMYD YMANNEDELS FSKGQLINVL SKDDADWWQG EINGVTGLFP SNYVKMTTDS
DPSQQWCADL QSLDTMQPME RKRQGYIHEL IQTEERYMDD LQLVLEVFQK PMADSGCLTE
GEMGLIFVNW KELIMSNTKL LKALRVRKKT GGEKMPVQMI GDILAAELSH MQAYIRFCSC
QLNGASLLQQ KTDEDADFKD YLKKLALDPR CKGMPLSSFL LKPMQRITRY PLLIKSILEN
TPENHPDHSN LKLALERAEE LCSQVNEGVR EKENSDRLEW IQSHVQCEGL AEQPVFNSLT
NCLGPRKLLH SGKLYKAKSS KELYGFLFND FLLLTYMVKQ FVSSGSDKLF SPKCNSQFKM
YKMPVFLNEV LVKLPTDPSS DEPVFHISHI DRVYTLKTDN INERTAWVQK IKAASEQYIE
TEKKKREKAY QARSQKTSGI GRLMVHVIEA TELKACKPNG KSNPYCEISM GSQSYTTRTL
QDTLNPKWNF NCQFFIKDLH QDVLCITMFD RDQFSPDDFL GRTEVPVAKI RTEQESKGPT
TKHLLLHEVP TGEVWVRFDL QLFDQ
//
