GGYF2_XENLA
ID GGYF2_XENLA Reviewed; 1239 AA.
AC Q5U236;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=GRB10-interacting GYF protein 2;
DE AltName: Full=PERQ amino acid-rich with GYF domain-containing protein 2;
GN Name=gigyf2; Synonyms=perq2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key component of the 4EHP-GYF2 complex, a multiprotein
CC complex that acts as a repressor of translation initiation.
CC {ECO:0000250|UniProtKB:Q6Y7W6, ECO:0000250|UniProtKB:Q6Y7W8}.
CC -!- SUBUNIT: Component of the 4EHP-GYF2 complex (By similarity).
CC {ECO:0000250|UniProtKB:Q6Y7W6, ECO:0000250|UniProtKB:Q6Y7W8}.
CC -!- SIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.
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DR EMBL; BC086295; AAH86295.1; -; mRNA.
DR RefSeq; NP_001088645.1; NM_001095176.1.
DR AlphaFoldDB; Q5U236; -.
DR SMR; Q5U236; -.
DR BioGRID; 105778; 1.
DR IntAct; Q5U236; 1.
DR GeneID; 495698; -.
DR KEGG; xla:495698; -.
DR CTD; 495698; -.
DR Xenbase; XB-GENE-5870341; gigyf2.S.
DR OrthoDB; 412069at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 495698; Expressed in testis and 19 other tissues.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..1239
FT /note="GRB10-interacting GYF protein 2"
FT /id="PRO_0000270840"
FT DOMAIN 488..536
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 105..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1239 AA; 141636 MW; 9C55179440DC8301 CRC64;
MTAETQTLNF GPEWLRALSS GGSVISPPLS PALPKYKLAD FRYGREEMLA LYVKDNKVPS
DLLDKEFLPI LNDEPLLPLA LVSFTEEEQR NFSMSVNSAA VLRLTNRGSS GGGGTVVGVP
RGRSSSRGRG RGRGESGFYQ RSFDEVESGF GRGAREMHRS QSWEERGDRR FEKPARKEPD
GVRGSAWREI PDRRRRFDYD LRESKDERGY RRPRSGSGIA EDERDSLPEW CLDDAEDETG
TFDSSGAFLS SKPSKKVQKE PIPEEQEIDF HPSVDGAEVS DSDGSQTEEA KETDPVQSQN
QDDDLSRNDH TVQAAPSPDH KTSSPVRRTD MTLDTAHQKA VSPHLSCKMD AKSQSPSSPP
TPSKHKEDAA SASHQGTREK AGPCLPHPQS PALSQRSPAR QPDPHIVPAM SSVPVPQLDT
PTVPIHSSVC AAPGMEPVPP EPDEDGLEHL EQQAQQMVAY LQDGTLDDDH LLTKVLDQRV
KGPSLDNQQK WYYKDPQGEI QGPFSNREMA EWYQAGYFPM TLLLRRVCDE TFQPLGDIFK
KWGRVPFSTP PTPRLGDLDP ERLSRQQEIT ALYQMRHLHY QQLLFQQQYA VLAQQQKVAL
SSQQQQLPLP LQPLSMRIPE HTVIPPVVRA LSVPESTSLW ELPPAPTQPA VWEGSSVWDL
PVEPTTQGTT REQLAQMDKV KAAKMEQERR EAELRAKQEE EEQHRRKEAE EERKRREEEE
LARRKQEEAL QRQKELALQK QMEEEERQRK KELQLLEERM RQEEERKRLE EERRRQEEER
RKQLEERKRA EEERRRREEE KKREEDERRQ LEEIQRKQEE AARWAREEEE AVRLLLEEAR
LKAEEEERNK REEAQRQKEL QRQRQQQQEA LRRLQLQQQQ QQLAQMKLPS SSTWGQQVTP
SAASQSALSL AEIQKLEEER ERQKLQEQRH QQQELKALQQ QQQQQQQKIP GWGTMSKPTG
TTKSLLEIQQ EEAGQMQKNH QQPGRNRPAN ISLPVAPVVN NHISSPTVGN SGSSVWGSLN
NNLSPQWSSD SMSSIWGSTD VKGSSVGFWD DAVKEVAPRN ATSKNKNNAS KSAGSNSRQS
KKVEQEEKLL RLFQGANKCQ DDFTQWCEKT MHAINTAHSL DVPTFVSFLR EVESPYEVHD
YVCAYLGDTP EAKDFSKQFI ERRTKQKTSQ HRPQQDVAWV TCQTSQANSQ PITLEAVQCA
GRKKKKQKMV RADPSLLGFS VNASSERLNM GEIETAEDY