ID G3T9N5_LOXAF Unreviewed; 1079 AA.
AC G3T9N5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Folliculin interacting protein 2 {ECO:0000313|Ensembl:ENSLAFP00000010510.2};
GN Name=FNIP2 {ECO:0000313|Ensembl:ENSLAFP00000010510.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000010510.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000010510.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010510.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000010510.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010510.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004656}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the FNIP family.
CC {ECO:0000256|ARBA:ARBA00007541}.
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DR AlphaFoldDB; G3T9N5; -.
DR STRING; 9785.ENSLAFP00000010510; -.
DR Ensembl; ENSLAFT00000012571.2; ENSLAFP00000010510.2; ENSLAFG00000012570.2.
DR eggNOG; KOG3693; Eukaryota.
DR GeneTree; ENSGT00390000009391; -.
DR HOGENOM; CLU_003447_0_0_1; -.
DR InParanoid; G3T9N5; -.
DR OMA; IADTDKC; -.
DR TreeFam; TF324090; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:1990877; C:FNIP-folliculin RagC/D GAP; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042030; F:ATPase inhibitor activity; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR InterPro; IPR037545; DENN_FNIP1/2.
DR InterPro; IPR028086; FNIP_C_dom.
DR InterPro; IPR026156; FNIP_fam.
DR InterPro; IPR028085; FNIP_mid_dom.
DR InterPro; IPR028084; FNIP_N_dom.
DR PANTHER; PTHR21634:SF11; FOLLICULIN-INTERACTING PROTEIN 2; 1.
DR PANTHER; PTHR21634; UNCHARACTERIZED; 1.
DR Pfam; PF14638; FNIP_C; 1.
DR Pfam; PF14637; FNIP_M; 1.
DR Pfam; PF14636; FNIP_N; 2.
DR PRINTS; PR02073; FOLLICULNIP1.
DR PROSITE; PS51836; DENN_FNIP12; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT DOMAIN 7..1070
FT /note="UDENN FNIP1/2-type"
FT /evidence="ECO:0000259|PROSITE:PS51836"
FT REGION 55..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 118948 MW; 14D699EB3BCE9AD8 CRC64;
SWSCSEFDLN EIRLIVYQDC ERRGRQVLFD SKAVHKIEEV AAQNTEDDPL KMSAKCCHGS
GSSSHGSSGG SLQHAKEQLP KYQYMRPASD VNMLGEMMFG SVAMSYKGPT LKIHYIRSPP
QLMISKVFSA RMGSFCGSTN NLQDSFEYIN QDPNLGKLNT NQNSLGPCRT GSNLAHSTPV
DMPSRGQNED RDSGIARSAS LSSLLITPFP SPSPSTSSSS SYQRRWLRSQ TTSLENGIVP
RRSTDETFSL AEETCSSNPA IVRRKKIAIS IIFSLCEKEE AQRNFQDFFF SHFPLFESHM
NRLKSAIEKA MISCRKIAES SHRVQFYISR LMEALGEFRG TIWNLYSVPR IAEPIWLTMM
SSTLEKTQLC QRFLKEFTLL IEQINKNQFF AALLTAVLTY HLAWVPTVMP VDHPPIKAFS
EKRTSQSVNM LAKTHPYNPL WAQLGDLYGA IGSPVRLTRT VVVGKQKDLV QRILYVLTYF
LRCSELQENQ LTWSGHHGEG DQVLNGSKIT TALEKGEVEE SEYVVVTVRS EPALIPPVLP
LTTAQRRNLG PTGLAGTPEG TAITDLCPNL DKEESKRPEK SSKACSVGFQ EPALGSSWQH
QGTFCGDEGC EKEVPQDGSL RLSNSEVLEA GPKVSQQTAH EESKGEMPAK LSDRSVARPC
PDRHAREKAA LEKVTFQIGS SVSPESDLES RTKKMEEQLK ACRQCPESAG SPWAQSRVAA
AVAQDQQVSR CSFKPGFRKS VCCPQNQSSE EDEGEFDRCF AEDRNIRTNV AAGVAGQPSQ
PADPLAPPDL AAGTAESVLG KTGGLCLKDA EAPLLEPVPN RRVQQDSGFS VAADIPCGDA
NRRADFRTEA DIPRNESSDS ALGDSDDDTF ASATRSLGHC GDWTEASLEV ELPLPRSQSI
SNQSVRNFGR SLLAGYCPTY TPDLVLHGTS NDEKLKQCLM ADLVHTVHHP VLDEPIAEAV
CIVADTDKWS VQVATSQRKV ADGVKLGQDV LVSSQVSSLL QAVLQLYKLH FPADFCVMHL
EDRLQEMYFK SKMLSEYLRG HTRVHVKELG VVLGIESNDL PLLTAIASTH SPYVAQILL
//
