ID   SPF30_PONAB             Reviewed;         238 AA.
AC   Q5R591;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Survival of motor neuron-related-splicing factor 30;
DE   AltName: Full=Survival motor neuron domain-containing protein 1;
GN   Name=SMNDC1; Synonyms=SPF30;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in spliceosome assembly (By similarity).
CC       {ECO:0000250|UniProtKB:O75940}.
CC   -!- SUBUNIT: Associates with spliceosomes. Associates with U4/U5/U6 tri-
CC       snRNP and with U2 snRNP (By similarity).
CC       {ECO:0000250|UniProtKB:O75940}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:O75940}.
CC       Nucleus, Cajal body {ECO:0000250|UniProtKB:O75940}. Note=Detected in
CC       nuclear speckles containing snRNP and in Cajal (coiled) bodies.
CC       {ECO:0000250|UniProtKB:O75940}.
CC   -!- DOMAIN: The Tudor domain mediates association with dimethylarginines,
CC       which are common in snRNP proteins. {ECO:0000250|UniProtKB:O75940}.
CC   -!- SIMILARITY: Belongs to the SMN family. {ECO:0000305}.
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DR   EMBL; CR860973; CAH93075.1; -; mRNA.
DR   RefSeq; NP_001126821.1; NM_001133349.1.
DR   AlphaFoldDB; Q5R591; -.
DR   BMRB; Q5R591; -.
DR   SMR; Q5R591; -.
DR   STRING; 9601.ENSPPYP00000003078; -.
DR   Ensembl; ENSPPYT00000003182; ENSPPYP00000003078; ENSPPYG00000002643.
DR   GeneID; 100173826; -.
DR   KEGG; pon:100173826; -.
DR   CTD; 10285; -.
DR   eggNOG; KOG3026; Eukaryota.
DR   GeneTree; ENSGT00940000153352; -.
DR   HOGENOM; CLU_069491_3_0_1; -.
DR   InParanoid; Q5R591; -.
DR   OMA; CMAVWSQ; -.
DR   OrthoDB; 1459016at2759; -.
DR   TreeFam; TF315413; -.
DR   Proteomes; UP000001595; Chromosome 10.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd04508; TUDOR; 1.
DR   InterPro; IPR010304; SMN_Tudor.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF06003; SMN; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Apoptosis; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Spliceosome.
FT   CHAIN           1..238
FT                   /note="Survival of motor neuron-related-splicing factor 30"
FT                   /id="PRO_0000347223"
FT   DOMAIN          72..132
FT                   /note="Tudor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   MOTIF           142..160
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75940"
FT   MOD_RES         219
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O75940"
SQ   SEQUENCE   238 AA;  26725 MW;  F4F09692E2083F5B CRC64;
     MSEDLAKQLA SYKAQLQQVE AALSGNGENE DLLKLKKDLQ EVIELTKDLL STQPSETLAS
     SDSFASTQPT HSWKVGDKCM AIWSEDGQCY EAEIEEIDEE NGTAAITFAG YGNAEVTPLL
     NLKPVEEGRK AKEDSGNKPM SKKEMIAQQR EYKKKKALKK AQRIKELEQE REDQKVKWQQ
     FNNRAYSKNK KGQVKRSIFA SPESVTGKVG VGTCGIADKP MTQYQDTSKY NVRHLMPQ