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Centrosomal protein of 83 kDa (Cep83) (Coiled-coil domain-containing protein 41) (Renal carcinoma antigen NY-REN-58)

 CEP83_HUMAN             Reviewed;         693 AA.
Q9Y592; A4FVB1; Q08AP1;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
25-OCT-2017, entry version 115.
RecName: Full=Centrosomal protein of 83 kDa;
Short=Cep83;
AltName: Full=Coiled-coil domain-containing protein 41;
AltName: Full=Renal carcinoma antigen NY-REN-58;
Name=CEP83; Synonyms=CCDC41;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION AS A RENAL
CANCER ANTIGEN.
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-634 (ISOFORM 1).
TISSUE=Retinoblastoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-559 (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23348840; DOI=10.1101/gad.207043.112;
Tanos B.E., Yang H.J., Soni R., Wang W.J., Macaluso F.P., Asara J.M.,
Tsou M.F.;
"Centriole distal appendages promote membrane docking, leading to
cilia initiation.";
Genes Dev. 27:163-168(2013).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP164 AND IFT20.
PubMed=23530209; DOI=10.1073/pnas.1220927110;
Joo K., Kim C.G., Lee M.S., Moon H.Y., Lee S.H., Kim M.J., Kweon H.S.,
Park W.Y., Kim C.H., Gleeson J.G., Kim J.;
"CCDC41 is required for ciliary vesicle docking to the mother
centriole.";
Proc. Natl. Acad. Sci. U.S.A. 110:5987-5992(2013).
[7]
INTERACTION WITH CEP164 AND IFT20, VARIANTS NPHP18 PRO-79;
104-PRO--LEU-109 DEL; PRO-503; GLU-676 DEL AND GLN-684 DEL, AND
CHARACTERIZATION OF VARIANTS NPHP18 PRO-79; 104-PRO--LEU-109 DEL;
PRO-503; GLU-676 DEL AND GLN-684 DEL.
PubMed=24882706; DOI=10.1016/j.ajhg.2014.05.002;
Failler M., Gee H.Y., Krug P., Joo K., Halbritter J., Belkacem L.,
Filhol E., Porath J.D., Braun D.A., Schueler M., Frigo A., Alibeu O.,
Masson C., Brochard K., Hurault de Ligny B., Novo R., Pietrement C.,
Kayserili H., Salomon R., Gubler M.C., Otto E.A., Antignac C., Kim J.,
Benmerah A., Hildebrandt F., Saunier S.;
"Mutations of CEP83 cause infantile nephronophthisis and intellectual
disability.";
Am. J. Hum. Genet. 94:905-914(2014).
-!- FUNCTION: Component of the distal appendage region of the
centriole involved in the initiation of primary cilium assembly.
May collaborate with IFT20 in the trafficking of ciliary membrane
proteins from the Golgi complex to the cilium during the
initiation of primary cilium assembly.
{ECO:0000269|PubMed:23348840, ECO:0000269|PubMed:23530209}.
-!- SUBUNIT: Interacts with CEP164 and IFT20.
{ECO:0000269|PubMed:23530209, ECO:0000269|PubMed:24882706}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:23348840, ECO:0000269|PubMed:23530209}.
Note=Localizes specifically to the distal appendage region of the
centriole, which anchors the mother centriole to the plasma
membrane. Localizes to centrioles at all stages of the cell cycle,
including mitosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y592-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y592-2; Sequence=VSP_037760, VSP_037761, VSP_037762;
-!- DISEASE: Nephronophthisis 18 (NPHP18) [MIM:615862]: An autosomal
recessive disorder characterized by chronic tubulointerstitial
nephritis resulting in end-stage renal disease in early childhood.
Extrarenal manifestations, including intellectual disability or
liver changes, may occur in some patients.
{ECO:0000269|PubMed:24882706}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the CEP83 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD42881.1; Type=Frameshift; Positions=105, 590, 601; Evidence={ECO:0000305};
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EMBL; AF155115; AAD42881.1; ALT_FRAME; mRNA.
EMBL; AC073655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC053614; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC125086; AAI25087.1; -; mRNA.
EMBL; BC125087; AAI25088.1; -; mRNA.
EMBL; AK056316; -; NOT_ANNOTATED_CDS; mRNA.
RefSeq; NP_057206.2; NM_016122.2.
UniGene; Hs.279209; -.
UniGene; Hs.584845; -.
ProteinModelPortal; Q9Y592; -.
SMR; Q9Y592; -.
BioGrid; 119321; 23.
IntAct; Q9Y592; 22.
MINT; MINT-1790539; -.
STRING; 9606.ENSP00000344655; -.
iPTMnet; Q9Y592; -.
PhosphoSitePlus; Q9Y592; -.
BioMuta; CCDC41; -.
DMDM; 97045295; -.
EPD; Q9Y592; -.
PaxDb; Q9Y592; -.
PeptideAtlas; Q9Y592; -.
PRIDE; Q9Y592; -.
Ensembl; ENST00000547232; ENSP00000447783; ENSG00000173588. [Q9Y592-2]
GeneID; 51134; -.
KEGG; hsa:51134; -.
UCSC; uc058ruu.1; human. [Q9Y592-1]
CTD; 51134; -.
DisGeNET; 51134; -.
EuPathDB; HostDB:ENSG00000173588.14; -.
GeneCards; CEP83; -.
HGNC; HGNC:17966; CEP83.
HPA; HPA038161; -.
MalaCards; CEP83; -.
MIM; 615847; gene.
MIM; 615862; phenotype.
neXtProt; NX_Q9Y592; -.
OpenTargets; ENSG00000173588; -.
Orphanet; 93591; Infantile nephronophthisis.
PharmGKB; PA142672158; -.
eggNOG; ENOG410IH7C; Eukaryota.
eggNOG; ENOG410XX59; LUCA.
GeneTree; ENSGT00450000040638; -.
HOGENOM; HOG000111412; -.
HOVERGEN; HBG053993; -.
InParanoid; Q9Y592; -.
KO; K16754; -.
PhylomeDB; Q9Y592; -.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
GenomeRNAi; 51134; -.
PRO; PR:Q9Y592; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000173588; -.
CleanEx; HS_CCDC41; -.
ExpressionAtlas; Q9Y592; baseline and differential.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
GO; GO:0048278; P:vesicle docking; IMP:UniProtKB.
InterPro; IPR029631; Cep83.
PANTHER; PTHR23170:SF2; PTHR23170:SF2; 1.
1: Evidence at protein level;
Alternative splicing; Ciliopathy; Cilium biogenesis/degradation;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Nephronophthisis; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 693 Centrosomal protein of 83 kDa.
/FTId=PRO_0000234495.
COILED 32 626 {ECO:0000255}.
COILED 657 690 {ECO:0000255}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D5R3}.
VAR_SEQ 1 25 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037760.
VAR_SEQ 562 593 RKSLHENKLKRLQEKVEVLEAKKEELETENQV -> LEQDL
ELGCPSVTDTYRESVFPPPPLKRDLLK (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_037761.
VAR_SEQ 594 693 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037762.
VARIANT 70 70 Q -> R (in dbSNP:rs2271979).
/FTId=VAR_058397.
VARIANT 79 79 L -> P (in NPHP18; does not affect
interaction with CEP164 and IFT20).
{ECO:0000269|PubMed:24882706}.
/FTId=VAR_071266.
VARIANT 104 109 Missing (in NPHP18; does not affect
interaction with CEP164 and IFT20).
{ECO:0000269|PubMed:24882706}.
/FTId=VAR_071267.
VARIANT 503 503 R -> P (in NPHP18; does not interact with
CEP164 and IFT20).
{ECO:0000269|PubMed:24882706}.
/FTId=VAR_071268.
VARIANT 676 676 Missing (in NPHP18; accumulates in the
nucleus). {ECO:0000269|PubMed:24882706}.
/FTId=VAR_071269.
VARIANT 684 684 Missing (in NPHP18; accumulates in the
nucleus; does not interact with CEP164
and IFT20).
{ECO:0000269|PubMed:24882706}.
/FTId=VAR_071270.
CONFLICT 259 259 E -> G (in Ref. 1; AAD42881).
{ECO:0000305}.
CONFLICT 336 336 I -> L (in Ref. 1; AAD42881).
{ECO:0000305}.
CONFLICT 536 536 E -> D (in Ref. 1; AAD42881).
{ECO:0000305}.
CONFLICT 537 537 R -> C (in Ref. 3; AAI25087).
{ECO:0000305}.
SEQUENCE 693 AA; 82059 MW; 0310952944AE6970 CRC64;
MDTFPNNFPP GGDSGLTGSQ SEFQKMLIDE RLRCEHHKAN YQTLKAEHTR LQNEHVKLQN
ELKHLFNEKQ TQQEKLQLLL EELRGELVEK TKDLEEMKLQ ILTPQKLELL RAQIQQELET
PMRERFRNLD EEVEKYRAVY NKLRYEHTFL KSEFEHQKEE YARILDEGKI KYESEIARLE
EDKEELRNQL LNVDLTKDSK RVEQLAREKV YLCQKLKGLE AEVAELKAEK ENSEAQVENA
QRIQVRQLAE MQATVRSLEA EKQSANLRAE RLEKELQSSS EQNTFLINKL HKAEREINTL
SSKVKELKHS NKLEITDIKL ETARAKSELE RERNKIQSEL DGLQSDNEIL KAAVEHHKVL
LVEKDRELIR KVQAAKEEGY QKLVVLQDEK LELENRLADL EKMKVEHDVW RQSEKDQYEE
KLRASQMAEE ITRKELQSVR LKLQQQIVTI ENAEKEKNEN SDLKQQISSL QIQVTSLAQS
ENDLLNSNQM LKEMVERLKQ ECRNFRSQAE KAQLEAEKTL EEKQIQWLEE KHKLHERITD
REEKYNQAKE KLQRAAIAQK KRKSLHENKL KRLQEKVEVL EAKKEELETE NQVLNRQNVP
FEDYTRLQKR LKDIQRRHNE FRSLILVPNM PPTASINPVS FQSSAMVPSM ELPFPPHMQE
EQHQRELSLL RKRLEELETT QRKQLEELGS SGE


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