ID   RBY1C_HUMAN             Reviewed;         496 AA.
AC   P0DJD4; Q15376; Q15377; Q15414; Q6NSB5; Q86VU6; Q8NHR0;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   13-SEP-2023, entry version 51.
DE   RecName: Full=RNA-binding motif protein, Y chromosome, family 1 member C;
GN   Name=RBMY1C;
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 [GENOMIC DNA] OF 1-220 AND 332-496.
RX   PubMed=9598316; DOI=10.1006/geno.1998.5255;
RA   Chai N.-N., Zhou H., Hernandez J., Najmabadi H., Bhasin S., Yen P.H.;
RT   "Structure and organization of the RBMY genes on the human Y chromosome:
RT   transposition and amplification of an ancestral autosomal hnRNPG gene.";
RL   Genomics 49:283-289(1998).
RN   [2]
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=9108067; DOI=10.1073/pnas.94.8.3848;
RA   Elliott D.J., Millar M.R., Oghene K., Ross A., Kiesewetter F., Pryor J.,
RA   McIntyre M., Hargreave T.B., Saunders P.T.K., Vogt P.H., Chandley A.C.,
RA   Cooke H.;
RT   "Expression of RBM in the nuclei of human germ cells is dependent on a
RT   critical region of the Y chromosome long arm.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3848-3853(1997).
RN   [3]
RP   INTERACTION WITH KHDRBS3.
RX   PubMed=10332027; DOI=10.1093/hmg/8.6.959;
RA   Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J.,
RA   Cooke H.J., Artzt K., Eperon I.C.;
RT   "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
RT   binding protein implicated in spermatogenesis.";
RL   Hum. Mol. Genet. 8:959-969(1999).
RN   [4]
RP   INTERACTION WITH TRA2B.
RC   TISSUE=Testis;
RX   PubMed=10749975; DOI=10.1093/hmg/9.5.685;
RA   Venables J.P., Elliott D.J., Makarova O.V., Makarov E.M., Cooke H.J.,
RA   Eperon E.C.;
RT   "RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins
RT   interact with Tra2beta and affect splicing.";
RL   Hum. Mol. Genet. 9:685-694(2000).
RN   [5]
RP   INTERACTION WITH KHDRBS1.
RX   PubMed=15595951; DOI=10.1111/j.1365-2605.2004.00496.x;
RA   Elliott D.J.;
RT   "The role of potential splicing factors including RBMY, RBMX, hnRNPG-T and
RT   STAR proteins in spermatogenesis.";
RL   Int. J. Androl. 27:328-334(2004).
CC   -!- FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Required
CC       for sperm development. Acts additively with TRA2B to promote exon 7
CC       inclusion of the survival motor neuron SMN. Binds non-specifically to
CC       mRNAs.
CC   -!- SUBUNIT: Interacts with splicing factor proteins SFRS3/SRP20,
CC       TRA2B/SFRS10, KHDRBS1/SAM68 and KHDRBS3. {ECO:0000269|PubMed:10332027,
CC       ECO:0000269|PubMed:10749975, ECO:0000269|PubMed:15595951}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9108067}.
CC   -!- TISSUE SPECIFICITY: Testis-specific.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all of the transcriptionally active
CC       stages of germ cell development from spermatogonia through
CC       spermatocytes to round spermatids. {ECO:0000269|PubMed:9108067}.
CC   -!- MISCELLANEOUS: The RBMY1 proteins are encoded by repeated regions of
CC       the Y chromosome, mostly within the AZFb region. The exact number of
CC       functional copies is unclear and may vary between individuals, and some
CC       of them may represent pseudogenes. The proteins are very similar, which
CC       makes the characterization of each protein difficult. Thus, most
CC       experiments do not discriminate between the different members. One can
CC       therefore suppose that reported interactions with a RBMY1 protein
CC       involve all the proteins.
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DR   EMBL; U36608; AAC16917.1; -; Genomic_DNA.
DR   EMBL; U36604; AAC16917.1; JOINED; Genomic_DNA.
DR   EMBL; U36605; AAC16917.1; JOINED; Genomic_DNA.
DR   EMBL; U36606; AAC16917.1; JOINED; Genomic_DNA.
DR   EMBL; U36607; AAC16917.1; JOINED; Genomic_DNA.
DR   EMBL; U36610; AAC16918.1; -; Genomic_DNA.
DR   EMBL; U36609; AAC16918.1; JOINED; Genomic_DNA.
DR   PIR; A49418; A49418.
DR   AlphaFoldDB; P0DJD4; -.
DR   SMR; P0DJD4; -.
DR   iPTMnet; P0DJD4; -.
DR   PhosphoSitePlus; P0DJD4; -.
DR   BioMuta; HGNC:9914; -.
DR   DMDM; 378522970; -.
DR   jPOST; P0DJD4; -.
DR   MassIVE; P0DJD4; -.
DR   PeptideAtlas; P0DJD4; -.
DR   ProteomicsDB; 52543; -.
DR   AGR; HGNC:9914; -.
DR   GeneCards; RBMY1C; -.
DR   HGNC; HGNC:9914; RBMY1C.
DR   MIM; 400006; gene.
DR   neXtProt; NX_P0DJD4; -.
DR   InParanoid; P0DJD4; -.
DR   PathwayCommons; P0DJD4; -.
DR   Pharos; P0DJD4; Tdark.
DR   PRO; PR:P0DJD4; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; P0DJD4; Protein.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd12382; RRM_RBMX_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR012604; RBM1CTR.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR48034:SF17; RNA-BINDING MOTIF PROTEIN, Y CHROMOSOME, FAMILY 1 MEMBER A1-RELATED; 1.
DR   PANTHER; PTHR48034; TRANSFORMER-2 SEX-DETERMINING PROTEIN-RELATED; 1.
DR   Pfam; PF08081; RBM1CTR; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Activator; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..496
FT                   /note="RNA-binding motif protein, Y chromosome, family 1
FT                   member C"
FT                   /id="PRO_0000415665"
FT   DOMAIN          8..85
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          80..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  55784 MW;  F912A0248CE0282E CRC64;
     MVEADHPGKL FIGGLNRETN EKMLKAVFGK HGPISEVLLI KDRTSKSRGF AFITFENPAD
     AKNAAKDMNG KSLHGKAIKV EQAQKPSFQS GGRRRPPASS RNRSPSGSLR SARGSRGGTR
     GWLPSHEGHL DDGGYTPDLK MSYSRGLIPV KRGPSSRSGG PPPKKSAPSA VARSNSWMGS
     QGPMSQRREN YGVPPRRATI SSWRNDRMST RHDGYATNDG NHPSCQETRD YAPPSRGYAY
     RDNGHSNRDE HSSRGYRNHR SSRETRDYAP PSRGHAYRDY GHSRRDESYS RGYRNRRSSR
     ETREYAPPSR GHGYRDYGHS RRHESYSRGY RNHPSSRETR DYAPPHRDYA YRDYGHSSWD
     EHSSRGYSYH DGYGEALGRD HSEHLSGSSY RDALQRYGTS HGAPPARGPR MSYGGSTCHA
     YSNTRDRYGR SWESYSSCGD FHYCDREHVC RKDQRNPPSL GRVLPDPREA CGSSSYVASI
     VDGGESRSEK GDSSRY
//