TCP11_RAT
ID TCP11_RAT Reviewed; 566 AA.
AC Q5XI00;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=T-complex protein 11 homolog;
GN Name=Tcp11;
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-104 AND SER-461, 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 -!- FUNCTION: Plays a role in the process of sperm capacitation and
CC acrosome reactions. Probable receptor for the putative fertilization-
CC promoting peptide (FPP) at the sperm membrane that may modulate the
CC activity of the adenylyl cyclase cAMP pathway.
CC {ECO:0000250|UniProtKB:Q01755}.
CC -!- SUBUNIT: Found in a complex at least composed of MROH2B isoform 2,
CC PRKACA isoform 2 and TCP11. Interacts with MROH2B isoform 2. Interacts
CC with PRKACA isoform 2. Interacts with ODF1 (via leucine zipper motif).
CC {ECO:0000250|UniProtKB:Q01755, ECO:0000250|UniProtKB:Q8WWU5}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q01755}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q01755}. Note=Localizes on the
CC acrosomal cap region of acrosome-intact, but not acrosome-reacted
CC sperm. Colocalizes with MROH2B and PRKACA on the acrosome and tail
CC regions in round spermatids and spermatozoa regardless of the
CC capacitation status of the sperm. {ECO:0000250|UniProtKB:Q01755}.
CC -!- PTM: Constitutively phosphorylated on serine, threonine and tyrosine
CC residues within the head and tail regions of noncapacitated
CC spermatozoa. Phosphorylation on tyrosine residues increases upon sperm
CC capacitation within the acrosomal region in a protein kinase A (PKA)-
CC dependent signaling pathway. {ECO:0000250|UniProtKB:Q01755}.
CC -!- SIMILARITY: Belongs to the TCP11 family. {ECO:0000305}.
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DR EMBL; BC083899; AAH83899.1; -; mRNA.
DR RefSeq; NP_001007696.1; NM_001007695.1.
DR RefSeq; XP_017457133.1; XM_017601644.1.
DR AlphaFoldDB; Q5XI00; -.
DR SMR; Q5XI00; -.
DR STRING; 10116.ENSRNOP00000039755; -.
DR iPTMnet; Q5XI00; -.
DR PhosphoSitePlus; Q5XI00; -.
DR PaxDb; Q5XI00; -.
DR PRIDE; Q5XI00; -.
DR Ensembl; ENSRNOT00000045044; ENSRNOP00000039755; ENSRNOG00000000499.
DR GeneID; 309641; -.
DR KEGG; rno:309641; -.
DR UCSC; RGD:1359387; rat.
DR CTD; 6954; -.
DR RGD; 1359387; Tcp11.
DR eggNOG; KOG1981; Eukaryota.
DR GeneTree; ENSGT00940000161869; -.
DR HOGENOM; CLU_026469_0_0_1; -.
DR InParanoid; Q5XI00; -.
DR OMA; NQKVFGP; -.
DR OrthoDB; 1230328at2759; -.
DR PhylomeDB; Q5XI00; -.
DR TreeFam; TF313385; -.
DR PRO; PR:Q5XI00; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000499; Expressed in testis and 10 other tissues.
DR Genevisible; Q5XI00; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007281; P:germ cell development; ISO:RGD.
DR GO; GO:0045920; P:negative regulation of exocytosis; ISO:RGD.
DR GO; GO:0010737; P:protein kinase A signaling; ISS:UniProtKB.
DR GO; GO:1902490; P:regulation of sperm capacitation; ISS: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 homolog"
FT /id="PRO_0000324299"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..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..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 566 AA; 62612 MW; 647D0F4BE2D0AA16 CRC64;
MPDLKERAAR KEPGAAESAS RESRGGNTRE SASSAQGHRS RRFNRRSSTA ALTPGSAQGR
GVQTAPRAPV GHGGLRTGLT SRCPQPSARA KLPSVTRGAP LPPSPGKGHF GATPISHRLG
LTERVHDASK LDCHLEDRKS ASSLESRGKE VMPSDFWDHL KEQLSAVPPD FSCALELLKE
IKEILLSLLL PRQSRLRNEI EEALDMEFLH QQADRGDLNV SYLSKYILNM MVLLCAPVRD
EAVQRLENIS DPVRLLRGIF QVLGQMKMDM VNYTIQSLQP QLQEHSIQFE RAQFQERLNK
DPSLLNHTTK WLTQAATQLI APSGSCYDIQ DPSSSSGPSP SDIAIPEPLS PAMVLSQGFL
NLLTWDPENE EFPETLLADR SRLQELESQQ NQLTILASVL LVASSFSGSV LFGSPQFVDR
LKRITKSLVE DFNSRPEEVM QTVSDQVTEE IHQSLKNMGL SPLSSENTDS LIGQLQNIAK
KENCVRSVID QRIHLFLKCC FVLGVQRSLL DLPGGLSLIE AELAELGQKF VSLTHHNQQV
FAPYYTEILK TLINPVQTLT TKVGSL
