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Database: UniProt
Entry: A0A183BKM9_GLOPA
LinkDB: A0A183BKM9_GLOPA
Original site: A0A183BKM9_GLOPA 
ID   A0A183BKM9_GLOPA        Unreviewed;      1549 AA.
AC   A0A183BKM9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   18-JUL-2018, entry version 14.
DE   RecName: Full=U1 small nuclear ribonucleoprotein C {ECO:0000256|HAMAP-Rule:MF_03153};
DE            Short=U1 snRNP C {ECO:0000256|HAMAP-Rule:MF_03153};
DE            Short=U1-C {ECO:0000256|HAMAP-Rule:MF_03153};
DE            Short=U1C {ECO:0000256|HAMAP-Rule:MF_03153};
OS   Globodera pallida (Potato cyst nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Tylenchida;
OC   Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae; Globodera.
OX   NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000116000};
RN   [1] {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000116000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741,
RC   ECO:0000313|WBParaSite:GPLIN_000116000};
RA   Li W., Chetelat R.T.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000116000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741,
RC   ECO:0000313|WBParaSite:GPLIN_000116000};
RA   Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J.,
RA   Thorpe P., Tsai I.J., Beasley H., Blok V., Cock P.J.A.,
RA   Van den Akker S.E., Holroyd N., Hunt M., Mantelin S., Naghra H.,
RA   Pain A., Palomares-Rius J.E., Zarowiecki M., Berriman M., Jones J.T.,
RA   Urwin P.E.;
RT   "The genome and life-stage specific transcriptomes of Globodera
RT   pallida elucidate key aspects of plant parasitism by a cyst
RT   nematode.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:GPLIN_000116000}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- FUNCTION: Component of the spliceosomal U1 snRNP, which is
CC       essential for recognition of the pre-mRNA 5' splice-site and the
CC       subsequent assembly of the spliceosome. U1-C is directly involved
CC       in initial 5' splice-site recognition for both constitutive and
CC       regulated alternative splicing. The interaction with the 5'
CC       splice-site seems to precede base-pairing between the pre-mRNA and
CC       the U1 snRNA. Stimulates commitment or early (E) complex formation
CC       by stabilizing the base pairing of the 5' end of the U1 snRNA and
CC       the 5' splice-site region. {ECO:0000256|HAMAP-Rule:MF_03153}.
CC   -!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins B/B', D1,
CC       D2, D3, E, F and G that assemble in a heptameric protein ring on
CC       the Sm site of the small nuclear RNA to form the core snRNP, and
CC       at least 3 U1 snRNP-specific proteins U1-70K, U1-A and U1-C. U1-C
CC       interacts with U1 snRNA and the 5' splice-site region of the pre-
CC       mRNA. {ECO:0000256|HAMAP-Rule:MF_03153}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03153,
CC       ECO:0000256|SAAS:SAAS00591741}.
CC   -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C
CC       family. {ECO:0000256|HAMAP-Rule:MF_03153}.
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DR   WBParaSite; GPLIN_000116000; GPLIN_000116000; GPLIN_000116000.
DR   Proteomes; UP000050741; Unassembled WGS sequence.
DR   GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005685; C:U1 snRNP; IEA:UniProtKB-UniRule.
DR   GO; GO:0071004; C:U2-type prespliceosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030619; F:U1 snRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000395; P:mRNA 5'-splice site recognition; IEA:UniProtKB-UniRule.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03153; U1_C; 1.
DR   InterPro; IPR021930; Heparan_SO4_deacetylase.
DR   InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR037359; NST/OST.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   InterPro; IPR013085; U1-CZ_Znf_C2H2.
DR   InterPro; IPR017340; U1_snRNP-C.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR10605; PTHR10605; 3.
DR   Pfam; PF12062; HSNSD; 3.
DR   Pfam; PF00685; Sulfotransfer_1; 2.
DR   Pfam; PF06220; zf-U1; 1.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS50171; ZF_MATRIN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000050741};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03153,
KW   ECO:0000256|SAAS:SAAS00921506};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03153,
KW   ECO:0000256|SAAS:SAAS00520746};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050741};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_03153};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_03153};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_03153, ECO:0000256|SAAS:SAAS00921530};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_03153,
KW   ECO:0000256|SAAS:SAAS00921503}.
FT   DOMAIN     1389   1421       Matrin-type. {ECO:0000259|PROSITE:
FT                                PS50171}.
SQ   SEQUENCE   1549 AA;  175507 MW;  3469BE321C19EEF7 CRC64;
     MAEYFINPFT SATKTHNYFR LSMSEEKNQL NSATHKSIEN FIKYLKVPVL VESHLPGEHL
     LLELGGRARF SLVIFGDYRS YHLLSAGEKA LLREFCARHS AGVISFLELS TNGQRIEFAN
     FTVYGRQLVT KLAMSNASPI HHVAKAGVEY WTRNESNVEC TLFKPTLSRL NPILRAENEL
     GEQFAVALQL EERHVIFGAK PDQHWLIQIA LLDAIAFLAP TIHSEDLERF VQIDIDDVFV
     GTSGSRLVVD DVQSLHILQD KLREHIADFY FTLGFSGYFF RHGDSSEIRG DEILVNNANK
     FHWFPHMWRH NHAHEFSAEF LVALMTQNRV FAQNVGVLAN LSYAVSPQHS GVYPVYQPLY
     DAWATVWSVR VTSTEEYPHL RPASGRRAFV HGTVTVLPRQ TCGLFTHTQF FHAYPDGIDH
     FLSNVFGGEL FTSVLMNKFS IFMTHQQNFA NDRLGAFTFL NLAKFVECWT NLRLRWTSPT
     NLAELYLKRF PQERTLLYTN PCDDARHRQT MPSNFNCTSL KLPNLLILGP QKTGTSALGL
     FLSLHPNIST NAPISDSFEE LQFFGGPNYA RGLQWYTEQF ANAPSTTSVL FGKSANYFDN
     PKVPAAVHAL LPNAKLIHMR AHNNSAALRY SAEQLFANDT IDDEGLNKLR RRCLWPGLYA
     RHIDRWLDHF APSQLLFVDG LRLRSEPYFV LSELFAKLQL PPLDGLHRLL RYSPEKGFYC
     TVLVDKTDAK NLQQQQKDHQ RLRCLGRSKG RHYEPMSNKL RQHLETYLPE NVRMYYQAWM
     EEQAQKLIDA TTRAFTSQRM LPAAAPGFMP PVSVPVPTMI PPRGPFVNPM AMVRPPMMPP
     SMAGFFTPPV LPPGMLTAAA SGAIPLPAVT SAIPAPSTVV NANGAMPQQF VQIDIDDVFV
     GTSGSRLVVD DVQSLHILQD KLREHIADFY FTLGFSGYFF RHGDSSEIRG DEILVYPVYQ
     PLYDAWATVW SVRVTSTEEY PHLRPASGRR AFVHGTVTVL PRQTCGLFTH TQFFHAYPDG
     IDHFLSNVFG GELFTSVLMN KFSIFMTHQQ NFANDRLGAF TFLNLAKFVE CWTNLRLRWT
     SPTNLAELYL KRFPQERTLL YTNPCDDARH RQTMPSNFNC TSLKLPNLLI LGPQKTGTSA
     LGLFLSLHPN ISTNAPISDS FEELQFFGGP NYARGLQWYA EQFANAPSTT SVLFGKSANY
     FDNPKVPAAV HALLPNAKLI VILSDPAQRA YSWFQHMRAH NNSAALRYSA EQLFANDTID
     DEELNKLRRR CLWPGLYARH IDRWLDHFAP SQLLFVDGMR LRSEPYFVLS ELFAKLQLPP
     LDGLHRLLRY SPEKGFYCAV SVDKTDAKNL QQQQRDHQRL RCLGRSKGRH YEPMSNKLRQ
     HLETKMPKYY CDYCDAFLTH DSPSVRKTHN GGRKHKENVR MYYQAWMEEQ AQKLIDATTR
     AFTSQRMLPA AAPGFMPPVS VPVPTMIPPR GPFVNPMAMV RPPMMPPSMA GFFTPPVLPP
     GMLTAAASGA IPLPVVTSAI PAPSTVVNAN GAMPQQSPLR TAIKQQPDE
//
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