TCP11_MOUSE
ID TCP11_MOUSE Reviewed; 566 AA.
AC Q01755;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=T-complex protein 11;
DE AltName: Full=Testis-specific protein PBS13;
GN Name=Tcp11; Synonyms=Tcp-11;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CBA/CaJ; TISSUE=Testis;
RX PubMed=1893875; DOI=10.1242/dev.111.2.561;
RA Mazarakis N.D., Nelki D., Lyon M.F., Evans E.P., Ruddy S., Freemont P.,
RA Dudley K.;
RT "Isolation and characterisation of a testis-expressed developmentally
RT regulated gene from the distal inversion of the mouse T-complex.";
RL Development 111:561-571(1991).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9322250;
RX DOI=10.1002/(sici)1098-2795(199711)48:3<375::aid-mrd11>3.0.co;2-v;
RA Fraser L.R., Hosseini R., Hanyalogou A., Talmor A., Dudley R.K.;
RT "TCP-11, the product of a mouse t-complex gene, plays a role in stimulation
RT of capacitation and inhibition of the spontaneous acrosome reaction.";
RL Mol. Reprod. Dev. 48:375-382(1997).
RN [3]
RP FUNCTION.
RX PubMed=9820206;
RX DOI=10.1002/(sici)1098-2795(199812)51:4<468::aid-mrd14>3.0.co;2-6;
RA Adeoya-Osiguwa S.A., Dudley R.K., Hosseini R., Fraser L.R.;
RT "FPP modulates mammalian sperm function via TCP-11 and the adenylyl
RT cyclase/cAMP pathway.";
RL Mol. Reprod. Dev. 51:468-476(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 IDENTIFICATION IN A COMPLEX WITH MROH2B AND PRKACA, INTERACTION WITH MROH2B
RP AND PRKACA, AND SUBCELLULAR LOCATION.
RX PubMed=27105888; DOI=10.1096/fj.201500136r;
RA Stanger S.J., Law E.A., Jamsai D., O'Bryan M.K., Nixon B., McLaughlin E.A.,
RA Aitken R.J., Roman S.D.;
RT "A novel germ cell protein, SPIF (sperm PKA interacting factor), is
RT essential for the formation of a PKA/TCP11 complex that undergoes
RT conformational and phosphorylation changes upon capacitation.";
RL FASEB J. 30:2777-2791(2016).
CC -!- FUNCTION: Plays a role in the process of sperm capacitation and
CC acrosome reactions (PubMed:9322250, PubMed:9820206). Probable receptor
CC for the putative fertilization-promoting peptide (FPP) at the sperm
CC membrane that may modulate the activity of the adenylyl cyclase cAMP
CC pathway (PubMed:9322250, PubMed:9820206). {ECO:0000269|PubMed:9322250,
CC ECO:0000269|PubMed:9820206}.
CC -!- SUBUNIT: Found in a complex at least composed of MROH2B isoform 2,
CC PRKACA isoform 2 and TCP11 (PubMed:27105888). Interacts with MROH2B
CC isoform 2 (PubMed:27105888). Interacts with PRKACA isoform 2
CC (PubMed:27105888). Interacts with ODF1 (via leucine zipper motif) (By
CC similarity). {ECO:0000250|UniProtKB:Q8WWU5,
CC ECO:0000269|PubMed:27105888}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:27105888, ECO:0000269|PubMed:9322250}. Cytoplasmic
CC vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:27105888,
CC ECO:0000269|PubMed:9322250}. Note=Localizes on the acrosomal cap region
CC of acrosome-intact, but not acrosome-reacted sperm (PubMed:9322250).
CC Colocalizes with MROH2B and PRKACA on the acrosome and tail regions in
CC round spermatids and spermatozoa regardless of the capacitation status
CC of the sperm (PubMed:27105888). {ECO:0000269|PubMed:27105888,
CC ECO:0000269|PubMed:9322250}.
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:1893875). Expressed in
CC mature epididymal spermatozoa (at protein level) (PubMed:9322250).
CC {ECO:0000269|PubMed:1893875, ECO:0000269|PubMed:9322250}.
CC -!- DEVELOPMENTAL STAGE: First expressed in the pachytene spermatocyte
CC stage (PubMed:1893875).
CC -!- PTM: Constitutively phosphorylated on serine, threonine and tyrosine
CC residues within the head and tail regions of noncapacitated spermatozoa
CC (PubMed:27105888). Phosphorylation on tyrosine residues increases upon
CC sperm capacitation within the acrosomal region in a protein kinase A
CC (PKA)-dependent signaling pathway (PubMed:27105888).
CC {ECO:0000269|PubMed:27105888}.
CC -!- SIMILARITY: Belongs to the TCP11 family. {ECO:0000305}.
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DR EMBL; X52128; CAA36374.1; -; mRNA.
DR PIR; S22933; S22933.
DR AlphaFoldDB; Q01755; -.
DR SMR; Q01755; -.
DR STRING; 10090.ENSMUSP00000038590; -.
DR iPTMnet; Q01755; -.
DR PhosphoSitePlus; Q01755; -.
DR MaxQB; Q01755; -.
DR PaxDb; Q01755; -.
DR PRIDE; Q01755; -.
DR ProteomicsDB; 263263; -.
DR MGI; MGI:98544; Tcp11.
DR eggNOG; KOG1981; Eukaryota.
DR InParanoid; Q01755; -.
DR ChiTaRS; Tcp11; mouse.
DR PRO; PR:Q01755; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q01755; protein.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045920; P:negative regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling; IDA:UniProtKB.
DR GO; GO:1902490; P:regulation of sperm capacitation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR008862; Tcp11.
DR PANTHER; PTHR12832; PTHR12832; 1.
DR Pfam; PF05794; Tcp11; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cytoplasmic vesicle; Developmental protein;
KW Differentiation; Flagellum; Membrane; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..566
FT /note="T-complex protein 11"
FT /id="PRO_0000065650"
FT TRANSMEM 393..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI00"
SQ SEQUENCE 566 AA; 61970 MW; 2FA8F83AF1015C49 CRC64;
MPDVKERAAR KEPGAAESAS RESRGGNTRE SASSARGTDR VGSTVARARP PSPQGPRRGA
VKTAPRGPVG HGGLRTGPTS RCPQPSARAK LPSVTRGAPL PPSPGKGHLG GTPSSHRLGM
TERVHDASKL DCQLEERSLS SSSLKGKVKD TMPSDFWEHL NEQLSAVPPD FSCALELLKE
IKEILLSLLL PRQSRLKNEI EEALDMEFLQ QQADRGDLNV SYLSKYILNM MVLLCAPIRD
EAVQRLENIS DPVRLLRGIF QVLGQMKMDM VNYTIQSLQP QLQEHSVQFE RAQFQERLNK
EPRLLNHTTK WLTQAATQLI APSASSSDLQ DCSSSAGPSP SDVAVPEPLS PAMVLSQGFL
NLLTWDPENE EFPETLVADR PRLQELESQQ SQLTILASVL LVASSFSDSG LFSSPQFVDK
LKQITKSLVE DFNSRPEEVM QSVSEQVVEE VHQGLESMGL AALSSENTAS LVGQLQNIAK
KENCVRSVID QRIHLFLKCC FVLGVQRSLL DLPGGLTLIE AELAELGQKF VSLTHHNQQV
FAPYYTEILK TLISPAQTLA TKGGSL
