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SRRM3_MOUSE
ID   SRRM3_MOUSE             Reviewed;         648 AA.
AC   Q80WV7; Q9CUV5; Q9JJ91;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Serine/arginine repetitive matrix protein 3;
GN   Name=Srrm3; ORFNames=MNCb-4760;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT   oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-231.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May play a role in regulating breast cancer cell
CC       invasiveness. May be involved in RYBP-mediated breast cancer
CC       progression. {ECO:0000250|UniProtKB:A6NNA2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80WV7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80WV7-2; Sequence=VSP_034270, VSP_034271;
CC   -!- SIMILARITY: Belongs to the CWC21 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29002.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB041661; BAA95106.1; -; mRNA.
DR   EMBL; BC051947; AAH51947.1; -; mRNA.
DR   EMBL; AK013812; BAB29002.1; ALT_INIT; mRNA.
DR   CCDS; CCDS39319.2; -. [Q80WV7-1]
DR   RefSeq; NP_067378.2; NM_021403.3. [Q80WV7-1]
DR   RefSeq; XP_006504534.1; XM_006504471.1. [Q80WV7-1]
DR   RefSeq; XP_006504535.1; XM_006504472.2. [Q80WV7-1]
DR   AlphaFoldDB; Q80WV7; -.
DR   SMR; Q80WV7; -.
DR   BioGRID; 208393; 16.
DR   STRING; 10090.ENSMUSP00000115695; -.
DR   iPTMnet; Q80WV7; -.
DR   PhosphoSitePlus; Q80WV7; -.
DR   PaxDb; Q80WV7; -.
DR   PRIDE; Q80WV7; -.
DR   ProteomicsDB; 257403; -. [Q80WV7-1]
DR   ProteomicsDB; 257404; -. [Q80WV7-2]
DR   Antibodypedia; 8308; 61 antibodies from 9 providers.
DR   Ensembl; ENSMUST00000144211; ENSMUSP00000115695; ENSMUSG00000039860. [Q80WV7-1]
DR   GeneID; 58212; -.
DR   KEGG; mmu:58212; -.
DR   UCSC; uc008zza.1; mouse. [Q80WV7-2]
DR   UCSC; uc008zzc.1; mouse. [Q80WV7-1]
DR   CTD; 222183; -.
DR   MGI; MGI:1920309; Srrm3.
DR   VEuPathDB; HostDB:ENSMUSG00000039860; -.
DR   eggNOG; KOG1869; Eukaryota.
DR   GeneTree; ENSGT00940000162625; -.
DR   HOGENOM; CLU_027803_0_0_1; -.
DR   InParanoid; Q80WV7; -.
DR   OMA; CTEFEML; -.
DR   OrthoDB; 1397544at2759; -.
DR   PhylomeDB; Q80WV7; -.
DR   TreeFam; TF335721; -.
DR   BioGRID-ORCS; 58212; 5 hits in 72 CRISPR screens.
DR   ChiTaRS; Srrm3; mouse.
DR   PRO; PR:Q80WV7; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q80WV7; protein.
DR   Bgee; ENSMUSG00000039860; Expressed in retinal neural layer and 105 other tissues.
DR   ExpressionAtlas; Q80WV7; baseline and differential.
DR   Genevisible; Q80WV7; MM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   InterPro; IPR013170; mRNA_splic_Cwf21_dom.
DR   InterPro; IPR029360; SRRM_C.
DR   Pfam; PF08312; cwf21; 1.
DR   Pfam; PF15230; SRRM_C; 1.
DR   SMART; SM01115; cwf21; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Reference proteome.
FT   CHAIN           1..648
FT                   /note="Serine/arginine repetitive matrix protein 3"
FT                   /id="PRO_0000341376"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..185
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..239
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..412
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         112
FT                   /note="I -> M (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_034270"
FT   VAR_SEQ         113..648
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_034271"
FT   CONFLICT        93
FT                   /note="Q -> P (in Ref. 1; BAA95106)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   648 AA;  71104 MW;  AA30FC7A02C070AE CRC64;
     MSSTVNNGAT GMPAPPDAAN GFPQPGASSG SWPRAEEELR AAEPGLVKRA HREILDHERK
     RRVELKCMEL QEMMEEQGYS EEEIRQKVGT FRQMLMEKEG VLTREDRPGA HIVAETPRRM
     EGLEPGLEYP PFDEDDGPVD CDCPVSCYRG HRGYRTKHWS SSSASPPPKK KKKKKGSHRR
     SRKKRRLESE CSCGSASPLR KKKKNVKKHR RDRSDSGSRR KRRYRSRSLK SKRKEKNKER
     KRPHTESPGR RFHHHSSASS HSPSMSSHYS DSGSPSRLSP KHRDDGRKTG SQRSSGSRSP
     SPSGGSGWGS PQQNGGSRQR SGAHGGRPGS AHSPPDKPSS PRACDKAAAA PTPPARGKDS
     QSPRSAPSSQ GRGGRAAGGT ARRRRRRRRR RRSRSSANAP RRRGRRRTKP APPRGSSRSL
     SGAHSSSDSG GGAPGPGPEP CSERGHGGHG KRAKERPPRA RPASTSPSPG TRGRRGGPEG
     NSSSRSPGPH QGSWSSSRSP SKSHSRSPDK RTRSPSLSPS PKKPLGRDKD SEGRARHAEA
     EAARTRRRSR SYSPIRKRRR DSPSFMEPRR ITSARKRPIP YYRPSPSSSS SCLSTDYSSR
     SHSRSPSPGH SHGSYSSRSH GTRSRSCSAS RSRSPSYHSR SSSESGGF
 
 
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