SMN_FELCA
ID SMN_FELCA Reviewed; 290 AA.
AC Q8HYB8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Survival of motor neuron protein;
GN Name=SMN1; Synonyms=SMN;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=15635053; DOI=10.1203/01.pdr.0000153625.46892.6f;
RA He Q., Lowrie C., Shelton G.D., Castellani R.J., Menotti-Raymond M.,
RA Murphy W., O'Brien S.J., Swanson W.F., Fyfe J.C.;
RT "Inherited motor neuron disease in domestic cats: a model of spinal
RT muscular atrophy.";
RL Pediatr. Res. 57:324-330(2005).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm ultimately triggers eviction of the SMN complex, thereby allowing
CC binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
CC Within the SMN complex, SMN1 acts as a structural backbone and together
CC with GEMIN2 it gathers the Sm complex subunits. Ensures the correct
CC splicing of U12 intron-containing genes that may be important for
CC normal motor and proprioceptive neurons development. Also required for
CC resolving RNA-DNA hybrids created by RNA polymerase II, that form R-
CC loop in transcription terminal regions, an important step in proper
CC transcription termination. May also play a role in the metabolism of
CC small nucleolar ribonucleoprotein (snoRNPs).
CC {ECO:0000250|UniProtKB:Q16637}.
CC -!- SUBUNIT: Homooligomer; may form higher order homooligomers in the dimer
CC to octamer range. Part of the core SMN complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and
CC STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG. Component of an import snRNP complex composed of
CC KPNB1, RNUT1, SMN1 and ZNF259. Interacts with DDX20, FBL, NOLA1, RNUT1,
CC SYNCRIP and with several spliceosomal snRNP core Sm proteins, including
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE and ILF3. Interacts with GEMIN2;
CC the interaction is direct. Interacts with GEMIN3; the interaction is
CC direct. Interacts with GEMIN8; the interaction is direct. Interacts
CC with SNRPB; the interaction is direct. Interacts (via Tudor domain)
CC with SNRPD1 (via C-terminus); the interaction is direct. Interacts with
CC SNRPD2; the interaction is direct. Interacts (via Tudor domain) with
CC SNRPD3 (via C-terminus); the interaction is direct. Interacts with
CC SNRPE; the interaction is direct. Interacts with OSTF1, LSM10, LSM11
CC and RPP20/POP7. Interacts (via C-terminal region) with ZPR1 (via C-
CC terminal region). Interacts (via Tudor domain) with COIL. Interacts
CC with SETX; recruits SETX to POLR2A. Interacts with POLR2A (via the C-
CC terminal domain (CTD)). Interacts with PRMT5. Interacts with XRN2.
CC Interacts (via C-terminus) with FMR1 (via C-terminus); the interaction
CC is direct and occurs in a RNA-independent manner. Interacts (via Tudor
CC domain) with SF3B2 ('Arg-508'-methylated form). Interacts with
CC WRAP53/TCAB1. Interacts (via Tudor domain) with ELAVL4 in an RNA-
CC independent manner; the interaction is required for localization of
CC ELAVL4 to RNA granules. Interacts with FRG1.
CC {ECO:0000250|UniProtKB:Q16637}.
CC -!- SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000250|UniProtKB:Q16637}.
CC Nucleus, Cajal body {ECO:0000250|UniProtKB:Q16637}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q16637}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q16637}. Perikaryon
CC {ECO:0000250|UniProtKB:Q16637}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q16637}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P97801}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:P97801}. Note=Colocalizes with actin and at the
CC Z-line of skeletal muscle (By similarity). Under stress conditions
CC colocalizes with RPP20/POP7 in punctuated cytoplasmic granules.
CC Colocalized and redistributed with ZPR1 from the cytoplasm to nuclear
CC gems (Gemini of coiled bodies) and Cajal bodies. Colocalizes with FMR1
CC in cytoplasmic granules in the soma and neurite cell processes (By
CC similarity). {ECO:0000250|UniProtKB:P97801,
CC ECO:0000250|UniProtKB:Q16637}.
CC -!- DOMAIN: The Tudor domain mediates association with dimethylarginines,
CC which are common in snRNP proteins. {ECO:0000250|UniProtKB:Q16637}.
CC -!- SIMILARITY: Belongs to the SMN family. {ECO:0000305}.
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DR EMBL; AY094503; AAM18209.1; -; mRNA.
DR RefSeq; NP_001009328.1; NM_001009328.1.
DR RefSeq; XP_006927841.1; XM_006927779.3.
DR AlphaFoldDB; Q8HYB8; -.
DR SMR; Q8HYB8; -.
DR STRING; 9685.ENSFCAP00000019138; -.
DR Ensembl; ENSFCAT00000035487; ENSFCAP00000032539; ENSFCAG00000028292.
DR GeneID; 493923; -.
DR KEGG; fca:493923; -.
DR CTD; 6607; -.
DR eggNOG; KOG4327; Eukaryota.
DR GeneTree; ENSGT00940000153352; -.
DR HOGENOM; CLU_077852_0_0_1; -.
DR InParanoid; Q8HYB8; -.
DR OrthoDB; 1316275at2759; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000028292; Expressed in embryonic head and 10 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006353; P:DNA-templated transcription, termination; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
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 Cell projection; Cytoplasm; Isopeptide bond; mRNA processing;
KW mRNA splicing; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..290
FT /note="Survival of motor neuron protein"
FT /id="PRO_0000333768"
FT DOMAIN 88..148
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 10..41
FT /note="P1 (binding site for GEMIN2)"
FT /evidence="ECO:0000250"
FT REGION 54..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..207
FT /note="Required for interaction with RPP20/POP7"
FT /evidence="ECO:0000250"
FT REGION 151..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..264
FT /note="P2 (binding site for SM B)"
FT /evidence="ECO:0000250"
FT REGION 276..290
FT /note="Required for interaction with SYNCRIP"
FT /evidence="ECO:0000250"
FT COMPBIAS 151..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16637"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16637"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16637"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16637"
FT MOD_RES 82
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q16637"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16637"
FT CROSSLNK 207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16637"
SQ SEQUENCE 290 AA; 31326 MW; E4D15F8447AA96AC CRC64;
MAMGGGSGVP EQEDSVLFRR GTGQSDDSDI WDDTALIKAY DKAVASFKHA LKNGDISEAS
DKPKGTPKRK PAKKNKSQKK NTTAALKQWK VGDKCSAIWS EDGCVYPATI ASIDFKRETC
VVVYTGYGNR EEQNVSDLLS PASAVDNNVE QNAQENENES QISTDESENS CRSPGNKSNN
VKSKATSWNS FLPPPPPMPG AGLGPAKPGL KFNGPPPPPP PPPHFLSCWL PPFPSGPPII
PPPPPICPDS LDDADALGSM LISWYMSGYH TGYYMGFKQN QKEGRCSHFN
