ID   PIRC1_HUMAN             Reviewed;         136 AA.
AC   Q5BN46; Q5T897; Q8WU44;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   24-JUL-2024, entry version 124.
DE   RecName: Full=Piercer of microtubule wall 1 protein {ECO:0000305};
DE            Short=Pierce1;
DE   AltName: Full=UPF0691 protein C9orf116;
DE   AltName: Full=p53-induced expression in RB-null cells protein 1;
GN   Name=PIERCE1 {ECO:0000312|HGNC:HGNC:28435};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX   PubMed=18182857; DOI=10.1016/s1016-8478(23)07357-0;
RA   Sung Y.H., Kim H.J., Lee H.W.;
RT   "Identification of a novel Rb-regulated gene associated with the cell
RT   cycle.";
RL   Mol. Cells 24:409-415(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [4] {ECO:0007744|PDB:7UNG}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=36191189; DOI=10.1073/pnas.2207605119;
RA   Gui M., Croft J.T., Zabeo D., Acharya V., Kollman J.M., Burgoyne T.,
RA   Hoog J.L., Brown A.;
RT   "SPACA9 is a lumenal protein of human ciliary singlet and doublet
RT   microtubules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 119:e2207605119-e2207605119(2022).
CC   -!- FUNCTION: Microtubule inner protein involved in the attachment of outer
CC       dynein arms (ODAs) to dynein-decorated doublet microtubules (DMTs) in
CC       cilia axoneme, which is required for motile cilia beating
CC       (PubMed:36191189). Functions at the initial step of left-right
CC       asymmetry specification of the visceral organs.
CC       {ECO:0000250|UniProtKB:Q5BN45, ECO:0000269|PubMed:36191189}.
CC   -!- SUBUNIT: Interacts with CFAP53, ODAD1 and ODAD3; the interactions link
CC       the outer dynein arms docking complex (ODA-DC) to the internal
CC       microtubule inner proteins (MIP) in cilium axoneme.
CC       {ECO:0000250|UniProtKB:Q32P67}.
CC   -!- INTERACTION:
CC       Q5BN46; Q13643: FHL3; NbExp=3; IntAct=EBI-10243636, EBI-741101;
CC       Q5BN46-2; Q13643: FHL3; NbExp=3; IntAct=EBI-12305735, EBI-741101;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:36191189}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5BN46-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5BN46-2; Sequence=VSP_014466, VSP_014467;
CC   -!- TISSUE SPECIFICITY: Expressed in airway epithelial cells.
CC       {ECO:0000269|PubMed:36191189}.
CC   -!- DEVELOPMENTAL STAGE: May be up-regulated during progression from G1 to
CC       S phase of the cell cycle. Maximal expression in S or G2 phase.
CC       {ECO:0000269|PubMed:18182857}.
CC   -!- SIMILARITY: Belongs to the PIERCE1 family. {ECO:0000305}.
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DR   EMBL; AY927868; AAX22217.1; -; mRNA.
DR   EMBL; AL161452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021261; AAH21261.1; -; mRNA.
DR   CCDS; CCDS43899.1; -. [Q5BN46-1]
DR   CCDS; CCDS6989.1; -. [Q5BN46-2]
DR   RefSeq; NP_001041730.1; NM_001048265.1. [Q5BN46-1]
DR   RefSeq; NP_653255.1; NM_144654.2. [Q5BN46-2]
DR   PDB; 7UNG; EM; 3.60 A; y/z=1-136.
DR   PDB; 8J07; EM; 4.10 A; 4S/4T=1-136.
DR   PDBsum; 7UNG; -.
DR   PDBsum; 8J07; -.
DR   AlphaFoldDB; Q5BN46; -.
DR   EMDB; EMD-26624; -.
DR   EMDB; EMD-35888; -.
DR   SMR; Q5BN46; -.
DR   BioGRID; 126503; 2.
DR   IntAct; Q5BN46; 2.
DR   STRING; 9606.ENSP00000395281; -.
DR   iPTMnet; Q5BN46; -.
DR   PhosphoSitePlus; Q5BN46; -.
DR   BioMuta; C9orf116; -.
DR   MassIVE; Q5BN46; -.
DR   PaxDb; 9606-ENSP00000395281; -.
DR   PeptideAtlas; Q5BN46; -.
DR   ProteomicsDB; 62718; -. [Q5BN46-1]
DR   ProteomicsDB; 62719; -. [Q5BN46-2]
DR   Antibodypedia; 18585; 67 antibodies from 19 providers.
DR   DNASU; 138162; -.
DR   Ensembl; ENST00000371789.7; ENSP00000360854.3; ENSG00000160345.13. [Q5BN46-2]
DR   Ensembl; ENST00000371791.5; ENSP00000360856.1; ENSG00000160345.13. [Q5BN46-2]
DR   Ensembl; ENST00000429260.7; ENSP00000395281.2; ENSG00000160345.13. [Q5BN46-1]
DR   GeneID; 138162; -.
DR   KEGG; hsa:138162; -.
DR   MANE-Select; ENST00000429260.7; ENSP00000395281.2; NM_001048265.2; NP_001041730.1.
DR   UCSC; uc004cfs.2; human. [Q5BN46-1]
DR   AGR; HGNC:28435; -.
DR   CTD; 138162; -.
DR   DisGeNET; 138162; -.
DR   GeneCards; PIERCE1; -.
DR   HGNC; HGNC:28435; PIERCE1.
DR   HPA; ENSG00000160345; Tissue enhanced (choroid plexus, fallopian tube, testis).
DR   MIM; 614502; gene.
DR   neXtProt; NX_Q5BN46; -.
DR   OpenTargets; ENSG00000160345; -.
DR   VEuPathDB; HostDB:ENSG00000160345; -.
DR   eggNOG; ENOG502S22V; Eukaryota.
DR   GeneTree; ENSGT00940000154745; -.
DR   HOGENOM; CLU_135708_0_0_1; -.
DR   InParanoid; Q5BN46; -.
DR   OMA; MFRNNTF; -.
DR   OrthoDB; 201693at2759; -.
DR   PhylomeDB; Q5BN46; -.
DR   TreeFam; TF323876; -.
DR   PathwayCommons; Q5BN46; -.
DR   SignaLink; Q5BN46; -.
DR   BioGRID-ORCS; 138162; 17 hits in 1144 CRISPR screens.
DR   ChiTaRS; C9orf116; human.
DR   GenomeRNAi; 138162; -.
DR   Pharos; Q5BN46; Tdark.
DR   PRO; PR:Q5BN46; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q5BN46; Protein.
DR   Bgee; ENSG00000160345; Expressed in bronchial epithelial cell and 111 other cell types or tissues.
DR   ExpressionAtlas; Q5BN46; baseline and differential.
DR   GO; GO:0160111; C:axonemal A tubule inner sheath; IEA:Ensembl.
DR   GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR   GO; GO:0071494; P:cellular response to UV-C; IEA:Ensembl.
DR   GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR   GO; GO:0061966; P:establishment of left/right asymmetry; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR   InterPro; IPR026507; PIRC1/2.
DR   PANTHER; PTHR20899; PIERCE HOMOLOG; 1.
DR   PANTHER; PTHR20899:SF5; PIERCER OF MICROTUBULE WALL 1 PROTEIN; 1.
DR   Pfam; PF14892; PIRC1_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW   Cytoskeleton; Reference proteome.
FT   CHAIN           1..136
FT                   /note="Piercer of microtubule wall 1 protein"
FT                   /id="PRO_0000089728"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         75..92
FT                   /note="KVFYPNSNKFSQQLAAGG -> RVECSGTILSMFTWRKAS (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014466"
FT   VAR_SEQ         93..136
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014467"
SQ   SEQUENCE   136 AA;  15260 MW;  40EF2889FC52E775 CRC64;
     MAEECPRACA EPVAPKATAP PERTSDYYRV SADLPGRFNN PGWFRGYRTQ KAVSVYRTSN
     QAYGSRAPTV HEMPKVFYPN SNKFSQQLAA GGMFRNNTLN VYLEKSIVTG PDNCITSCDR
     LNFHPSYNIN RPSICD
//