CC136_MOUSE
ID CC136_MOUSE Reviewed; 1136 AA.
AC Q3TVA9; Q923E5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Coiled-coil domain-containing protein 136;
GN Name=Ccdc136;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-1136 (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 396-1029 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, FUNCTION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=27076447; DOI=10.1177/1933719116641762;
RA Geng Q., Ni L., Ouyang B., Hu Y., Zhao Y., Guo J.;
RT "A novel testis-specific gene, Ccdc136, is required for acrosome formation
RT and fertilization in mice.";
RL Reprod. Sci. 23:1387-1396(2016).
CC -!- FUNCTION: May play a role in acrosome formation in spermatogenesis and
CC in fertilization. {ECO:0000269|PubMed:27076447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000269|PubMed:27076447}; Single-pass membrane protein
CC {ECO:0000305}. Note=Exclusively localized on a peripheral part of
CC acrosome membrane (Golgi phase), localized on the equatorial segment of
CC the acrosome (maturation phase). {ECO:0000269|PubMed:27076447}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TVA9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TVA9-2; Sequence=VSP_027846, VSP_027847, VSP_027848;
CC -!- TISSUE SPECIFICITY: Present at high level in testis (at protein level).
CC {ECO:0000269|PubMed:27076447}.
CC -!- DEVELOPMENTAL STAGE: Increased in an age-dependent manner from
CC postnatal 3 to 8 weeks. {ECO:0000269|PubMed:27076447}.
CC -!- DISRUPTION PHENOTYPE: Males are infertile, due to severe defect of
CC disrupting acrosome formation. {ECO:0000269|PubMed:27076447}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06583.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE35710.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE35710.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC044807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006583; AAH06583.1; ALT_INIT; mRNA.
DR EMBL; AK160245; BAE35710.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001188307.1; NM_001201378.1.
DR RefSeq; NP_663549.3; NM_145574.3.
DR AlphaFoldDB; Q3TVA9; -.
DR SMR; Q3TVA9; -.
DR STRING; 10090.ENSMUSP00000093789; -.
DR iPTMnet; Q3TVA9; -.
DR PhosphoSitePlus; Q3TVA9; -.
DR jPOST; Q3TVA9; -.
DR MaxQB; Q3TVA9; -.
DR PaxDb; Q3TVA9; -.
DR PRIDE; Q3TVA9; -.
DR ProteomicsDB; 265692; -. [Q3TVA9-1]
DR ProteomicsDB; 265693; -. [Q3TVA9-2]
DR DNASU; 232664; -.
DR GeneID; 232664; -.
DR KEGG; mmu:232664; -.
DR UCSC; uc009bdl.1; mouse. [Q3TVA9-1]
DR CTD; 64753; -.
DR MGI; MGI:1918128; Ccdc136.
DR eggNOG; ENOG502RZUE; Eukaryota.
DR InParanoid; Q3TVA9; -.
DR PhylomeDB; Q3TVA9; -.
DR BioGRID-ORCS; 232664; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Ccdc136; mouse.
DR PRO; PR:Q3TVA9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3TVA9; protein.
DR GO; GO:0002080; C:acrosomal membrane; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0001675; P:acrosome assembly; IMP:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasmic vesicle; Differentiation;
KW Fertilization; Membrane; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..1136
FT /note="Coiled-coil domain-containing protein 136"
FT /id="PRO_0000300640"
FT TRANSMEM 1112..1132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 293..631
FT /evidence="ECO:0000255"
FT COILED 681..730
FT /evidence="ECO:0000255"
FT COILED 839..972
FT /evidence="ECO:0000255"
FT COILED 1017..1057
FT /evidence="ECO:0000255"
FT COMPBIAS 11..31
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1089
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 361
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027846"
FT VAR_SEQ 917..951
FT /note="IKELQTKLRELQLQYQASMDEQGRLLAVQEQLEGQ -> NMFGMWKPMVFLA
FT IAAVALYVLPNMRPQESEYYMK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027847"
FT VAR_SEQ 952..1136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027848"
FT CONFLICT 412
FT /note="S -> N (in Ref. 2; AAH06583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1136 AA; 131930 MW; 6C289387FF214D41 CRC64;
MQAMDGEVLL PALYEEEEEE EEEEEEVEEE QVEKGGSLGS LSMGKHRGLS LTETELEELR
AQVLQLVAEL EETRELAGQH EDDSLELQGL LEDERLASAQ QAEVFTKQIQ QLQGELQHLR
EEISLLEHEK ESELKEMEQE LHLAQAEIQN LRQAAADSAT EHESDIASLQ DDLCRLQNDL
DDMERIRGDY EMEIASLRAE MELKTSEPSN LSISDFSGIQ DELHHLRERY NLLNEEYQAL
RESNSSLTGQ LAELESDRTR RATERWLESH LLRSTMSSES QTSELDFPEP DPVMQLLRQQ
LLGAEEQMQD MQDKCKNLYC ELEELQHHRR TSEEEQKRLQ RELKCAQNEV LRFQTSHSTQ
QHEELKSRLC TLQQKYDASQ DEHSELLKVQ MQLETELQQL RLLRCTPVES QSEKELMCRL
QKLQAQHQCS VNEKEQLLEV QHHLHDKLRC HESEVHRLRS MVDCLREKNE KNSGIHLQLQ
EMKGLYQFSR DELERQKHMY DQLEQDFLLC QQELTELKSS QSLCEENGNC SNKCDALLAR
LTELQDKFKA SQEEIGHLQM EQCELLEDQR RLQEEQGQLQ EELHRLTFPQ PKCGILQKSQ
ELLSKLQDLC EMQLLYQNMQ EQQRKLTQNQ ECVLKEQLEA HKHLRGFKES HFQEVLANPQ
DARGPKSSSC ENKFKVLMDQ LQALQVLYDT SQKQQEVLQR EHGRLMEERK RLQAELQLCM
EEMQVLQTQS PMIKRSFEYC GKNSGSRAPS TENFHRSYES SIDENEGYQK SYVSSQPSTE
TFLKSYDSST SANEAFEKSY CSSSTSVSYK KSYGSVSSGE TLHRSYASSS TDEDPAEPED
LEHFEETVAK VLTKLQAVKA LYQVSQEEHC QLQQRMHRLL AKQKELTEEL QCCEKELREC
MESLGKPLPP QSDKCEIKEL QTKLRELQLQ YQASMDEQGR LLAVQEQLEG QLQCCQEELR
QLKENRPSIS SEARGKNVNK NMNKNANGVR NKKLSMACSE DLENGFENEK NLEVMLYYKA
SQRRLDELMK EEKEIEEARK KEREKKAKKD LCKLATNPAA DPRAEPEPTE DEEENFEEYR
EGEDESCEAA EEGNPLKLSE SKKPSPAPDP PIFSLPLVGL VVISALLWCW WAETSS
