ID   F205C_RAT               Reviewed;         329 AA.
AC   Q642A3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Protein FAM205C {ECO:0000305};
GN   Name=Fam205c {ECO:0000250|UniProtKB:A6NFA0};
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-152 AND SER-153, AND
RP   IDENTIFICATION BY 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; BC082005; AAH82005.1; -; mRNA.
DR   RefSeq; NP_001019514.2; NM_001024343.2.
DR   AlphaFoldDB; Q642A3; -.
DR   STRING; 10116.ENSRNOP00000038393; -.
DR   iPTMnet; Q642A3; -.
DR   PhosphoSitePlus; Q642A3; -.
DR   PaxDb; Q642A3; -.
DR   GeneID; 500445; -.
DR   KEGG; rno:500445; -.
DR   UCSC; RGD:1561387; rat.
DR   CTD; 100129969; -.
DR   RGD; 1561387; Fam205c.
DR   eggNOG; ENOG502THPB; Eukaryota.
DR   InParanoid; Q642A3; -.
DR   OrthoDB; 1223253at2759; -.
DR   PhylomeDB; Q642A3; -.
DR   TreeFam; TF337856; -.
DR   PRO; PR:Q642A3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR027970; DUF4599.
DR   Pfam; PF15371; DUF4599; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..329
FT                   /note="Protein FAM205C"
FT                   /id="PRO_0000319054"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          149..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          58..85
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        201..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   329 AA;  36941 MW;  156AC64A7843FF9E CRC64;
     MLIPPFILWD VGYSVYTYGS IFIIALIIWQ VKRSHRGLRM GPTKSCAKCF RRIKQTPSDR
     ATRAKRTSKE EAEKLQKLLD TMKSQGWLPQ EGSVRRLLCP DPSCSICNAM TLEIQQLLGV
     ENKKTSSSLL RPSRSFSCLE ALSPSKSLAD RSSELTYQDT RDVSLSSRFP QSQETDQQST
     RSATPSIGDA VLQCYHSAPQ QQLDPQGSKM TQDAKGLSSS STDEPGVPAN QQKKRKKTKK
     LALKNQAAPT EVETENKMTF FSHWVNPEVK CDRQEESLVF SKYDTGAKPM TVEPEKTHSP
     VRDQAEGAEK KKKPECDLKA KPLRAKRNI