ID   ROP1_RAT                Reviewed;         212 AA.
AC   Q4KLL5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Ropporin-1;
DE   AltName: Full=Rhophilin-associated protein 1;
GN   Name=Ropn1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Important for male fertility. With ROPN1L, involved in
CC       fibrous sheath integrity and sperm motility, plays a role in PKA-
CC       dependent signaling processes required for spermatozoa capacitation.
CC       {ECO:0000250|UniProtKB:Q9ESG2}.
CC   -!- SUBUNIT: Homodimer. Interacts with AKAP3 (By similarity). May interact
CC       with SPA17 (By similarity). Interacts with RHPN1 (By similarity).
CC       Interacts with FSCB; the interaction increases upon spermatozoa
CC       capacitation conditions (By similarity). {ECO:0000250|UniProtKB:Q96C74,
CC       ECO:0000250|UniProtKB:Q9BZX4, ECO:0000250|UniProtKB:Q9ESG2}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000250|UniProtKB:Q9ESG2}. Note=In the sperm tail, found in the
CC       principal piece and in the cytoplasmic droplet located at the distal
CC       end of the midpiece. Inner surface of the fibrous sheath.
CC       {ECO:0000250|UniProtKB:Q9ESG2}.
CC   -!- DOMAIN: The RIIa domain mediates interaction with AKAP3. {ECO:0000250}.
CC   -!- PTM: Sumoylated, sumoylation decreases upon spermatozoa capacitation
CC       conditions. {ECO:0000250|UniProtKB:Q9ESG2}.
CC   -!- MISCELLANEOUS: 'Ropporin' comes from the Japanese word 'oppo' which
CC       means 'tail'.
CC   -!- SIMILARITY: Belongs to the ropporin family. {ECO:0000305}.
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DR   EMBL; BC099132; AAH99132.1; -; mRNA.
DR   RefSeq; NP_001020799.1; NM_001025628.1.
DR   RefSeq; XP_006248493.1; XM_006248431.3.
DR   AlphaFoldDB; Q4KLL5; -.
DR   STRING; 10116.ENSRNOP00000002975; -.
DR   iPTMnet; Q4KLL5; -.
DR   PhosphoSitePlus; Q4KLL5; -.
DR   PaxDb; Q4KLL5; -.
DR   Ensembl; ENSRNOT00000002975; ENSRNOP00000002975; ENSRNOG00000002187.
DR   GeneID; 288053; -.
DR   KEGG; rno:288053; -.
DR   UCSC; RGD:1310675; rat.
DR   CTD; 54763; -.
DR   RGD; 1310675; Ropn1.
DR   eggNOG; ENOG502R2JI; Eukaryota.
DR   GeneTree; ENSGT00390000012731; -.
DR   HOGENOM; CLU_069829_1_0_1; -.
DR   InParanoid; Q4KLL5; -.
DR   OMA; QWASDYF; -.
DR   OrthoDB; 1316863at2759; -.
DR   PhylomeDB; Q4KLL5; -.
DR   TreeFam; TF105421; -.
DR   PRO; PR:Q4KLL5; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000002187; Expressed in testis and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0031514; C:motile cilium; IBA:GO_Central.
DR   GO; GO:0097598; C:sperm cytoplasmic droplet; ISO:RGD.
DR   GO; GO:0097228; C:sperm principal piece; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0044782; P:cilium organization; ISS:UniProtKB.
DR   GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR   GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Flagellum; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..212
FT                   /note="Ropporin-1"
FT                   /id="PRO_0000307396"
FT   DOMAIN          12..43
FT                   /note="RIIa"
FT   REGION          209..212
FT                   /note="Interaction with RHPN1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   212 AA;  23961 MW;  E360019583B4C2C2 CRC64;
     MPQTDKQVCI PPELPELLKQ FTKAAIRTQP PDLIQWAAEY FGAMSRGEIP PVRERSEQVP
     LSNWAELTPE LLKVLHSRVG GRLIIHADEL AQMWKVLNLP TDLFNSVMNV GRFTEEIEWL
     KFLALACSSL GVTIAKTLKI VCEVLSCDHD GGPPRIPFST FQFLYTYIAE VDGEISSSHV
     TRMLNYIEQE VIGPDGLIKV NDFTQNPRVR LE