ID F7I264_CALJA Unreviewed; 1663 AA.
AC F7I264;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000014630.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000014630.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000014630.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000014630.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSCJAT00000015430.5; ENSCJAP00000014630.4; ENSCJAG00000007772.5.
DR eggNOG; KOG1029; Eukaryota.
DR GeneTree; ENSGT00940000155936; -.
DR HOGENOM; CLU_002819_0_0_1; -.
DR TreeFam; TF324293; -.
DR Proteomes; UP000008225; Chromosome 14.
DR Bgee; ENSCJAG00000007772; Expressed in testis and 6 other cell types or tissues.
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 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; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 2.
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 Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 22..110
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 54..89
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 244..333
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 277..312
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 723..784
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 864..922
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 947..1005
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1019..1083
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1093..1152
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1175..1361
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1400..1510
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1518..1634
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 219..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1663 AA; 189631 MW; 0ACEDFA6AFCA2390 CRC64;
MMAQFPTAMN GGPNMWAITS EERTKHDRQF DNLKPSGGYI TGDQARNFFL QSGLPAPVLA
EIWALSDLNK DGKMDQQEFS IAMKLIKLKL QGQQLPVVLP PIMKQPPLFS PLISARFGMG
SMPNLSIPQP LPPAAPITSL SSATSGTSLP PLMMPTPLVP SISTSSLPNG TASLIQPLSI
PYSSSTLPHG SSYSLMMGGF GGASIQKAQS LIDLGSSSST SSTASLSGNS PKTGTSEWAV
PQPSRLKYRQ KFNSLDKSMS GYLSGFQARN ALLQSNLSQT QLATIWTLAD IDGDGQLKAE
EFILAMHLTD MAKAGQPLPL TLPPELVPPS FRGGKQIDSI NGTLPSYQKM QEEEPQKKLP
VTFEDKRKAN YERGNMELEK RRQALMEQQQ REAERKAQKE KEEWERKQRE LQEQEWKKQL
ELEKRLEKQR ELERQREEER RKEIERREAA KQELERQRRL EWERIRRQEL LNQKNREQEE
IVRLNSKKKS LHLELEALNG KHQQISGRLQ DVRLKKQTQK TELEVLDKQC DLEITEIKQL
LQELQEYQNK LIYLVPEKQL LNERIKNMQF SNTPDSGISL LHKKSLEKEE LCQRLKEQLD
ALEKETASKL SEMDSFNNQL KELRETYNTQ QLALEQLYKI KRDKLKEIER KRLELIQKKK
LEDEAARKAK QGKENLWKES LRKEEEEKQK RLQEEKTQEK IQEEERKAEE KQRKGKDKRE
TASVLVNYRA LYPFEARNHD EMSFNSGDII QVDEKTIGEP GWLYGSFQGH FGWFPCNYVE
KMPSSENEKA VSPKKALLPP TVSLSATSTS SEPLSSNQPA SVTDYQNVSF SNLTVNTSWQ
KKSAFTRTVS PGSVSPIHGQ GQVVENLKAQ ALCSWTAKKD NHLNFSKHDV ITVLEQQENW
WFGEVHGRRG WFPKSYVKII PGSEVKREEP ETLYAAVNKK PTSAVCSVGE EYIALYPYSS
VEPGDLTFTE GEEILVTQKD GEWWTGSIGN RSGIFPSNYV KPKDQESFGS ANKSGASNKK
PEIAQVTSAY VASGSEQLSL APGQLILILK KNTSGWWQGE LQARGKKRQK GWFPASHVKL
LGPSSERATP AFHPVCQVIA MYDYAANNED ELSFSKGQLI NVMNKDDPDW WQGEINGVTG
LFPSNYVKMT TDSDPSQQWC ADLQTLDTMQ PIERKRQGYI HELIQTEERY MGDLQLVVEV
FQKRMAESGF LTEGEMALIF VNWKELIMSN TKLLKALRVR KKTGGEKMPV QMIGDILAAE
LSHMQAYIRF CSCQLNGAAL LQQKTDEDTD FKEFLKKLAS DPRCKGMPLS SFLLKPMQRI
TRYPLLIRSI LENTPESHTD HFSLKLALER AEELCSQVNE GVREKENSDR LEWIQAHVQC
EGLAEQLIFN SLTNCLGPRK LLHSGKLYKT KSNKELHGFL FNDFLLLTYM VKQFAVSSGS
EKLFSSKSSA QFKMYKTPIF LNEVLVKLPT DPSSDEPVFH ISHIDRVYTL RTDNINERTA
WVQKIKAASE QYIDTEKKKR EKAYQARSQK TSGIGRLMVH VVEATELKAC KPNGKSNPYC
EISMGSQSYT TRTIQDTLNP KWNFNCQFFI KDLYQDVLCL TLFDRDQFSP DDFLGRTEVP
VAKIRTEQES KGPTTRRLLL HEVPTGEVWV RFDLQLFEQK TLL
//
