CYFP2_PONAB
ID CYFP2_PONAB Reviewed; 1253 AA.
AC Q5R414; Q5R6T9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Cytoplasmic FMR1-interacting protein 2;
GN Name=CYFIP2 {ECO:0000250|UniProtKB:Q96F07};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH93502.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAH93502.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in T-cell adhesion and p53-dependent induction of
CC apoptosis. Does not bind RNA (By similarity). As component of the WAVE1
CC complex, required for BDNF-NTRK2 endocytic trafficking and signaling
CC from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q5SQX6,
CC ECO:0000250|UniProtKB:Q96F07}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP2, BRK1,
CC NCKAP1 and WASF1/WAVE1. Interacts with RAC1 (activated form) which
CC causes the complex to dissociate, releasing activated WASF1. The
CC complex can also be activated by NCK1. Interacts with SHANK3; the
CC interaction mediates the association of SHANK3 with the WAVE1 complex.
CC Interacts with FMR1; the interaction occurs in a RNA-dependent manner.
CC Interacts with FXR1 and FXR2. Interacts with TMEM108 (via N-terminus);
CC the interaction associates TMEM108 with the WAVE1 complex (By
CC similarity). {ECO:0000250|UniProtKB:Q5SQX6,
CC ECO:0000250|UniProtKB:Q96F07}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96F07}. Nucleus
CC {ECO:0000250|UniProtKB:Q96F07}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q5SQX6}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q5SQX6}. Note=Highly expressed in the
CC perinuclear regionand enriched in synaptosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q5SQX6}.
CC -!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
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DR EMBL; CR860395; CAH92521.1; -; mRNA.
DR EMBL; CR861446; CAH93502.1; -; mRNA.
DR RefSeq; NP_001126478.1; NM_001133006.1.
DR AlphaFoldDB; Q5R414; -.
DR SMR; Q5R414; -.
DR STRING; 9601.ENSPPYP00000017891; -.
DR PRIDE; Q5R414; -.
DR GeneID; 100173465; -.
DR KEGG; pon:100173465; -.
DR CTD; 26999; -.
DR eggNOG; KOG3534; Eukaryota.
DR InParanoid; Q5R414; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR InterPro; IPR009828; CYRIA/CYRIB_Rac1-bd.
DR InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR PANTHER; PTHR12195; PTHR12195; 1.
DR Pfam; PF07159; DUF1394; 1.
DR Pfam; PF05994; FragX_IP; 1.
DR PIRSF; PIRSF008153; FMR1_interacting; 1.
DR PRINTS; PR01698; CYTOFMRPINTP.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Cell adhesion; Cytoplasm; Nucleus;
KW Reference proteome; RNA editing; Synapse; Synaptosome.
FT CHAIN 1..1253
FT /note="Cytoplasmic FMR1-interacting protein 2"
FT /id="PRO_0000279711"
FT MOD_RES 1037
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96F07"
FT CONFLICT 467
FT /note="M -> T (in Ref. 1; CAH92521)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="C -> F (in Ref. 1; CAH92521)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="R -> C (in Ref. 1; CAH92521)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="E -> K (in Ref. 1; CAH92521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1253 AA; 145689 MW; 675760BE3E025212 CRC64;
MTTHVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSIMYQA NFDTNFEDRN AFVTGIARYI
EQATVHSSMN EMLEEGHEYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT
KLMKFMYFQR KAIERFCSEV KRLCHAERRK DFVSEAYLLT LGKFINMFAV LDELKNMKCS
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNRI TQCLHQQLEV IPGYEELLAD
IVNICVDYYE NKMYLTPSEK HMLLKVMGFG LYLMDGNVSN IYKLDAKKRI NLSKIDKFFK
QLQVVPLFGD MQIELARYIE TSAHYEENKS KWTCTQSSIS PQYNICEQMV QIRDDHIRFI
SELARYSNSE VVTGSGLDSQ KSDEEYRELF DLALRGLQLL SKWSAHVMEV YSWKLVHPTD
KFCNKDCPGT AEEYERATRY NYTSEEKFAF VEVIAMIKGL QVLMGRMESV FNQAIRNTIY
AALQDFAQVT LREPLRQAVR KKKNVLISVL QAIRKTICDW EGGREPPNDP CLRGEKDPKG
GFDIKVPRRA VGPSSTQLYM VRTMLESLIA DKSGSKKTLR SSLDGPIVLA IEDFHKQSFF
FTHLLNISEA LQQCCDLSQL WFREFFLELT MGRRIQFPIE MSMPWILTDH ILETKEPSMM
EYVLYPLDLY NDSAYYALTK FKKQFLYDEI EAEVNLCFDQ FVYKLADQIF AYYKAMAGSV
LLDKRFRAEC KNYGVIIPYP PSNRYETLLK QRHVQLLGRS IDLNRLITQR ISAAMYKSLD
QAISRFESED LTSIVELEWL LEINRLTHRL LCKHMTLDSF DAMFREANHN VSAPYGRITL
HVFWELNFDF LPNYCYNGST NRFVRTAIPF TQEPQRDKPA NIQPYYLYGS KPLNIAYSHI
YSSYRNFVGP PHFKTICRLL GYQGIAVVME ELLKIVESLL QGTILQYVKT LIEVMPKICR
LPRHEYGSPG ILEFFHHQLK DIIEYAELKT DVFQSLREVG NAILFCLLIE QALSQEEVCD
LLHAAPFQNI LPRVYIKEGE RLEVRMKRLE AKYAPLHLVP LIERLGTPQQ IAIAREGDLL
TKERLCCGLS MFEVILTRIR SYLQDPIWRG PPPTNGVMHV DECVEFHRLW SAMQFVYCIP
VGTNEFTAEQ CFGDGLNWAG CSIIVLLGQQ RRFDLFDFCY HLLKVQRQDG KDEIIKNVPL
KKMADRIRKY QILNNEVFAI LNKYMKSVET DSSTVEHVRC FQPPIHQSLA TTC
