SMAG1_MACFA
ID SMAG1_MACFA Reviewed; 718 AA.
AC Q95LV5; Q95K80; Q95LZ8;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein Smaug homolog 1;
DE Short=Smaug 1;
DE AltName: Full=Sterile alpha motif domain-containing protein 4A;
GN Name=SAMD4A; Synonyms=SAMD4, SMAUG1;
GN ORFNames=QtrA-10501, QtsA-10881, QtsA-17616;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-417 (ISOFORM 1).
RC TISSUE=Temporal cortex, and Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
CC -!- FUNCTION: Acts as a translational repressor of SRE-containing
CC messengers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC dendrite {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
CC Note=Enriched in synaptoneurosomes. Shuttles between the nucleus and
CC the cytoplasm in a CRM1-dependent manner. Colocalizes throughout the
CC cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1. Also
CC frequently colocalizes in cytoplasmic stress granule-like foci with
CC ELAVL1, TIA1 and TIAL1 (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q95LV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95LV5-2; Sequence=VSP_037780, VSP_008206;
CC Name=3;
CC IsoId=Q95LV5-3; Sequence=VSP_037780;
CC -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
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DR EMBL; AB063088; BAB60796.1; -; mRNA.
DR EMBL; AB071043; BAB64436.1; -; mRNA.
DR EMBL; AB071086; BAB64480.1; -; mRNA.
DR RefSeq; XP_015309293.1; XM_015453807.1.
DR AlphaFoldDB; Q95LV5; -.
DR SMR; Q95LV5; -.
DR STRING; 9541.XP_005561352.1; -.
DR GeneID; 102138042; -.
DR CTD; 23034; -.
DR eggNOG; KOG3791; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0030371; F:translation repressor activity; IEA:InterPro.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:InterPro.
DR CDD; cd09557; SAM_Smaug; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.170; -; 2.
DR InterPro; IPR037093; PHAT_dom_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037634; Smaug_SAM.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Cytoplasm; Methylation;
KW Phosphoprotein; Reference proteome; Repressor; Synapse; Synaptosome;
KW Translation regulation.
FT CHAIN 1..718
FT /note="Protein Smaug homolog 1"
FT /id="PRO_0000097571"
FT DOMAIN 323..396
FT /note="SAM"
FT REGION 278..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU9"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU9"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU9"
FT MOD_RES 573
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBY1"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B5DF21"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12498619"
FT /id="VSP_037780"
FT VAR_SEQ 239..327
FT /note="ILSGQAHHSPLKRSVSLTPPMNVPNQPLGHGWMSHEDLRARGPQCLPSDHAP
FT LSPQSSVASSGSGGSEHLEDQATARNTFQEEGSGMKD -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12498619"
FT /id="VSP_008206"
FT CONFLICT 312
FT /note="A -> T (in Ref. 1; BAB60796)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="R -> G (in Ref. 1; BAB60796)"
FT /evidence="ECO:0000305"
FT CONFLICT 411..417
FT /note="ILTPIKA -> TLSLHNR (in Ref. 1; BAB60796)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="R -> C (in Ref. 1; BAB64436)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="D -> N (in Ref. 1; BAB64436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 79426 MW; 919C3727BE71B1AB CRC64;
MMFRDQVGVL AGWFKGWNEC EQTVALLSLL KRVSQTQARF LQLCLEHSLA DCVELHVLER
EANSPGIINQ WQQESKDKVI SLLLTHLPLL KPGNLDAKVE YMKLLPKILA HSIEHNQHIE
ESRQLLSYAL IHPATSLEDR SALAMWLNHL EDRTSTSFGG QNRGRSDSVD YGQTHYYHQR
QNSDDKLNGW QNSRDSGICI NASNWQDKSM GCENGHVPLY SSSSVPTTIN TIGTSTSTIL
SGQAHHSPLK RSVSLTPPMN VPNQPLGHGW MSHEDLRARG PQCLPSDHAP LSPQSSVASS
GSGGSEHLED QATARNTFQE EGSGMKDVPA WLKSLRLHKY AALFSQMTYE EMMALTECQL
EAQNVTKGAR HKIVISIQKL KERQNLLKSL ERDIIEGGSL RVPLQELHQM ILTPIKAYGS
PSTTPEARPR EPQAPRQPSL MGPESQSPDC KDGATATGAT ATPSAGASGG LQPHQLSSCD
GELAVAPLPE GDLPGQFTRV MGKVCTQLLV SRPDEENISS YLQLIDKRLI HEAFTETQKK
RLLSWKQQVQ KLFRSFPRKT LLDISGYRQQ RNRGFGQSDS LPTAGSMGSG MGRRNPRQYQ
IPSRNVPSAR LGLLGTSGFV SSNQRNTTAA PTIMKQGRQN LWFANPGGSN SMPSRTHSSV
QRTRSLPVHT SPQNMLMFQQ PEFQLPVTEP DINNRLESLC LSMTEHALGD GVDRTSTI
