SRSF5_HUMAN
ID SRSF5_HUMAN Reviewed; 272 AA.
AC Q13243; O14797; Q16662; Q49AD6; Q6FGE0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Serine/arginine-rich splicing factor 5;
DE AltName: Full=Delayed-early protein HRS;
DE AltName: Full=Pre-mRNA-splicing factor SRP40;
DE AltName: Full=Splicing factor, arginine/serine-rich 5;
GN Name=SRSF5; Synonyms=HRS, SFRS5, SRP40;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SRP40-1 AND SRP40-2).
RC TISSUE=Colon;
RX PubMed=7556075; DOI=10.1002/j.1460-2075.1995.tb00108.x;
RA Screaton G.R., Caceres J.F., Mayeda A., Bell M.V., Plebanski M.,
RA Jackson D.G., Bell J.I., Krainer A.R.;
RT "Identification and characterization of three members of the human SR
RT family of pre-mRNA splicing factors.";
RL EMBO J. 14:4336-4349(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP40-1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP40-2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP40-2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP40-2).
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP40-2).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP40-1).
RC TISSUE=Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192, AND ALTERNATIVE SPLICING.
RC TISSUE=Thymus;
RX PubMed=9434190; DOI=10.1016/s0378-1119(97)00552-0;
RA Du K., Taub R.;
RT "Alternative splicing and structure of the human and mouse SFRS5/HRS/SRp40
RT genes.";
RL Gene 204:243-249(1997).
RN [9]
RP PROTEIN SEQUENCE OF 130-158.
RX PubMed=1577277; DOI=10.1101/gad.6.5.837;
RA Zahler A.M., Lane W.S., Stolk J.A., Roth M.B.;
RT "SR proteins: a conserved family of pre-mRNA splicing factors.";
RL Genes Dev. 6:837-847(1992).
RN [10]
RP IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SRSF4; SNRNP70; SNRPA1;
RP SRRM1 AND SRRM2.
RX PubMed=9531537; DOI=10.1101/gad.12.7.996;
RA Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.;
RT "A coactivator of pre-mRNA splicing.";
RL Genes Dev. 12:996-1009(1998).
RN [11]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250 AND SER-253, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-229; SER-233;
RP SER-250 AND SER-253, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Plays a role in constitutive splicing and can modulate the
CC selection of alternative splice sites.
CC -!- SUBUNIT: Interacts (via RS domain) with PHF5A (via N-terminus) (By
CC similarity). Found in a pre-mRNA splicing complex with SRSF4/SFRS4,
CC SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. {ECO:0000250,
CC ECO:0000269|PubMed:9531537}.
CC -!- INTERACTION:
CC Q13243; P78362: SRPK2; NbExp=2; IntAct=EBI-720503, EBI-593303;
CC Q13243; Q15696: ZRSR2; NbExp=3; IntAct=EBI-720503, EBI-6657923;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=SRP40-1;
CC IsoId=Q13243-1; Sequence=Displayed;
CC Name=SRP40-2;
CC IsoId=Q13243-2; Sequence=VSP_005864, VSP_005865;
CC Name=SRP40-3;
CC IsoId=Q13243-4; Sequence=Not described;
CC Name=SRP40-4;
CC IsoId=Q13243-3; Sequence=VSP_005863;
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform SRP40-2]: May be produced at very low levels
CC due to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39543.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U30826; AAA93070.1; -; mRNA.
DR EMBL; U30884; AAA93074.1; -; mRNA.
DR EMBL; U30827; AAB60405.1; -; mRNA.
DR EMBL; BT007089; AAP35752.1; -; mRNA.
DR EMBL; AK311805; BAG34748.1; -; mRNA.
DR EMBL; CR542167; CAG46964.1; -; mRNA.
DR EMBL; CR542182; CAG46979.1; -; mRNA.
DR EMBL; BX640605; CAE45711.1; -; mRNA.
DR EMBL; AB451250; BAG70064.1; -; mRNA.
DR EMBL; BC018823; AAH18823.1; -; mRNA.
DR EMBL; BC040209; AAH40209.1; -; mRNA.
DR EMBL; AF020307; AAC39543.1; ALT_FRAME; Genomic_DNA.
DR CCDS; CCDS32109.1; -. [Q13243-1]
DR PIR; S59042; S59042.
DR RefSeq; NP_001034554.1; NM_001039465.1. [Q13243-1]
DR RefSeq; NP_001307143.1; NM_001320214.1. [Q13243-1]
DR RefSeq; NP_008856.2; NM_006925.4. [Q13243-1]
DR AlphaFoldDB; Q13243; -.
DR SMR; Q13243; -.
DR BioGRID; 112328; 443.
DR CORUM; Q13243; -.
DR DIP; DIP-46894N; -.
DR IntAct; Q13243; 65.
DR MINT; Q13243; -.
DR STRING; 9606.ENSP00000452123; -.
DR GlyGen; Q13243; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13243; -.
DR PhosphoSitePlus; Q13243; -.
DR SwissPalm; Q13243; -.
DR BioMuta; SRSF5; -.
DR DMDM; 3929378; -.
DR EPD; Q13243; -.
DR jPOST; Q13243; -.
DR MassIVE; Q13243; -.
DR MaxQB; Q13243; -.
DR PaxDb; Q13243; -.
DR PeptideAtlas; Q13243; -.
DR PRIDE; Q13243; -.
DR ProteomicsDB; 59247; -. [Q13243-1]
DR ProteomicsDB; 59248; -. [Q13243-2]
DR ProteomicsDB; 59249; -. [Q13243-3]
DR Antibodypedia; 25065; 117 antibodies from 26 providers.
DR DNASU; 6430; -.
DR Ensembl; ENST00000394366.6; ENSP00000377892.2; ENSG00000100650.16. [Q13243-1]
DR Ensembl; ENST00000553521.5; ENSP00000452123.1; ENSG00000100650.16. [Q13243-1]
DR Ensembl; ENST00000553635.5; ENSP00000451391.1; ENSG00000100650.16. [Q13243-3]
DR Ensembl; ENST00000557154.6; ENSP00000451088.1; ENSG00000100650.16. [Q13243-1]
DR GeneID; 6430; -.
DR KEGG; hsa:6430; -.
DR MANE-Select; ENST00000557154.6; ENSP00000451088.1; NM_001320214.2; NP_001307143.1.
DR UCSC; uc001xll.4; human. [Q13243-1]
DR CTD; 6430; -.
DR DisGeNET; 6430; -.
DR GeneCards; SRSF5; -.
DR HGNC; HGNC:10787; SRSF5.
DR HPA; ENSG00000100650; Low tissue specificity.
DR MIM; 600914; gene.
DR neXtProt; NX_Q13243; -.
DR OpenTargets; ENSG00000100650; -.
DR PharmGKB; PA35703; -.
DR VEuPathDB; HostDB:ENSG00000100650; -.
DR eggNOG; KOG0106; Eukaryota.
DR GeneTree; ENSGT00940000158275; -.
DR HOGENOM; CLU_012062_34_2_1; -.
DR InParanoid; Q13243; -.
DR OMA; SACTVYV; -.
DR PhylomeDB; Q13243; -.
DR TreeFam; TF351335; -.
DR PathwayCommons; Q13243; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q13243; -.
DR SIGNOR; Q13243; -.
DR BioGRID-ORCS; 6430; 42 hits in 1084 CRISPR screens.
DR ChiTaRS; SRSF5; human.
DR GeneWiki; SFRS5; -.
DR GenomeRNAi; 6430; -.
DR Pharos; Q13243; Tbio.
DR PRO; PR:Q13243; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q13243; protein.
DR Bgee; ENSG00000100650; Expressed in right uterine tube and 201 other tissues.
DR ExpressionAtlas; Q13243; baseline and differential.
DR Genevisible; Q13243; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0043422; F:protein kinase B binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0006376; P:mRNA splice site selection; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR CDD; cd12337; RRM1_SRSF4_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR035585; RRM1_SRSF4-like.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..272
FT /note="Serine/arginine-rich splicing factor 5"
FT /id="PRO_0000081927"
FT DOMAIN 4..74
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 108..181
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 73..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..227
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 167
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 43..45
FT /note="Missing (in isoform SRP40-4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005863"
FT VAR_SEQ 100..107
FT /note="NAPPVRTE -> YVKGGWLH (in isoform SRP40-2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:19054851,
FT ECO:0000303|PubMed:7556075, ECO:0000303|Ref.4"
FT /id="VSP_005864"
FT VAR_SEQ 108..272
FT /note="Missing (in isoform SRP40-2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:19054851,
FT ECO:0000303|PubMed:7556075, ECO:0000303|Ref.4"
FT /id="VSP_005865"
FT VARIANT 160
FT /note="A -> S (in dbSNP:rs1057683)"
FT /id="VAR_014713"
SQ SEQUENCE 272 AA; 31264 MW; F13AD79845ECBB16 CRC64;
MSGCRVFIGR LNPAAREKDV ERFFKGYGRI RDIDLKRGFG FVEFEDPRDA DDAVYELDGK
ELCSERVTIE HARARSRGGR GRGRYSDRFS SRRPRNDRRN APPVRTENRL IVENLSSRVS
WQDLKDFMRQ AGEVTFADAH RPKLNEGVVE FASYGDLKNA IEKLSGKEIN GRKIKLIEGS
KRHSRSRSRS RSRTRSSSRS RSRSRSRSRK SYSRSRSRSR SRSRSKSRSV SRSPVPEKSQ
KRGSSSRSKS PASVDRQRSR SRSRSRSVDS GN
