ID   CE120_HUMAN             Reviewed;         986 AA.
AC   Q8N960; Q6AI52; Q6AW89; Q8IWB5; Q8N9Y0; Q8NDE8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Centrosomal protein of 120 kDa;
DE            Short=Cep120;
DE   AltName: Full=Coiled-coil domain-containing protein 100;
GN   Name=CEP120; Synonyms=CCDC100;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-870 (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 401-986 (ISOFORMS 1/2), AND VARIANT VAL-602.
RC   TISSUE=Brain, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-346 AND 498-986 (ISOFORMS
RP   1/2).
RC   TISSUE=Salivary gland, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   INVOLVEMENT IN SRTD13, AND VARIANT SRTD13 PRO-199.
RX   PubMed=25361962; DOI=10.1093/hmg/ddu555;
RG   UK10K Consortium;
RA   Shaheen R., Schmidts M., Faqeih E., Hashem A., Lausch E., Holder I.,
RA   Superti-Furga A., Mitchison H.M., Almoisheer A., Alamro R., Alshiddi T.,
RA   Alzahrani F., Beales P.L., Alkuraya F.S.;
RT   "A founder CEP120 mutation in Jeune asphyxiating thoracic dystrophy expands
RT   the role of centriolar proteins in skeletal ciliopathies.";
RL   Hum. Mol. Genet. 24:1410-1419(2015).
RN   [9]
RP   FUNCTION.
RX   PubMed=27185865; DOI=10.1242/jcs.186338;
RA   Chang C.W., Hsu W.B., Tsai J.J., Tang C.J., Tang T.K.;
RT   "CEP295 interacts with microtubules and is required for centriole
RT   elongation.";
RL   J. Cell Sci. 129:2501-2513(2016).
RN   [10]
RP   INVOLVEMENT IN JBTS31, VARIANTS JBTS31 ALA-194; VAL-549; PHE-712 AND
RP   PRO-726, AND VARIANTS PRO-199 AND SER-975.
RX   PubMed=27208211; DOI=10.1136/jmedgenet-2016-103832;
RA   Roosing S., Romani M., Isrie M., Rosti R.O., Micalizzi A., Musaev D.,
RA   Mazza T., Al-Gazali L., Altunoglu U., Boltshauser E., D'Arrigo S.,
RA   De Keersmaecker B., Kayserili H., Brandenberger S., Kraoua I., Mark P.R.,
RA   McKanna T., Van Keirsbilck J., Moerman P., Poretti A., Puri R.,
RA   Van Esch H., Gleeson J.G., Valente E.M.;
RT   "Mutations in CEP120 cause Joubert syndrome as well as complex ciliopathy
RT   phenotypes.";
RL   J. Med. Genet. 53:608-615(2016).
CC   -!- FUNCTION: Plays a role in the microtubule-dependent coupling of the
CC       nucleus and the centrosome. Involved in the processes that regulate
CC       centrosome-mediated interkinetic nuclear migration (INM) of neural
CC       progenitors and for proper positioning of neurons during brain
CC       development. Also implicated in the migration and selfrenewal of neural
CC       progenitors. Required for centriole duplication and maturation during
CC       mitosis and subsequent ciliogenesis (By similarity). Required for the
CC       recruitment of CEP295 to the proximal end of new-born centrioles at the
CC       centriolar microtubule wall during early S phase in a PLK4-dependent
CC       manner (PubMed:27185865). {ECO:0000250|UniProtKB:Q7TSG1,
CC       ECO:0000269|PubMed:27185865}.
CC   -!- SUBUNIT: Interacts with TACC2, TACC3, CCDC52, TALPID3.
CC       {ECO:0000250|UniProtKB:Q7TSG1}.
CC   -!- INTERACTION:
CC       Q8N960; Q5TB80: CEP162; NbExp=6; IntAct=EBI-2563015, EBI-1059012;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:14654843}. Note=Regulates the
CC       localization of TACC3 to the centrosome in neural progenitors in vivo.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8N960-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N960-2; Sequence=VSP_035123;
CC       Name=3;
CC         IsoId=Q8N960-3; Sequence=VSP_035124, VSP_035125;
CC   -!- DISEASE: Short-rib thoracic dysplasia 13 with or without polydactyly
CC       (SRTD13) [MIM:616300]: A form of short-rib thoracic dysplasia, a group
CC       of autosomal recessive ciliopathies that are characterized by a
CC       constricted thoracic cage, short ribs, shortened tubular bones, and a
CC       'trident' appearance of the acetabular roof. Polydactyly is variably
CC       present. Non-skeletal involvement can include cleft lip/palate as well
CC       as anomalies of major organs such as the brain, eye, heart, kidneys,
CC       liver, pancreas, intestines, and genitalia. Some forms of the disease
CC       are lethal in the neonatal period due to respiratory insufficiency
CC       secondary to a severely restricted thoracic cage, whereas others are
CC       compatible with life. Disease spectrum encompasses Ellis-van Creveld
CC       syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-
CC       Saldino syndrome, and short rib-polydactyly syndrome.
CC       {ECO:0000269|PubMed:25361962}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Joubert syndrome 31 (JBTS31) [MIM:617761]: A form of Joubert
CC       syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC       apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC       delay. Neuroradiologically, it is characterized by cerebellar vermian
CC       hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC       peduncles, and an abnormally large interpeduncular fossa, giving the
CC       appearance of a molar tooth on transaxial slices (molar tooth sign).
CC       Additional variable features include retinal dystrophy, renal disease,
CC       liver fibrosis, and polydactyly. JBTS31 inheritance is autosomal
CC       recessive. {ECO:0000269|PubMed:27208211}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CEP120 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC04155.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAH10561.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC010369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC106792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC040527; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK093409; BAC04155.1; ALT_INIT; mRNA.
DR   EMBL; AK095646; BAC04596.1; -; mRNA.
DR   EMBL; AL833929; CAD38785.2; -; mRNA.
DR   EMBL; BX648687; CAH10561.1; ALT_INIT; mRNA.
DR   EMBL; CR627324; CAH10371.1; -; mRNA.
DR   CCDS; CCDS4134.2; -. [Q8N960-1]
DR   CCDS; CCDS54890.1; -. [Q8N960-2]
DR   RefSeq; NP_001159698.1; NM_001166226.1. [Q8N960-2]
DR   RefSeq; NP_694955.2; NM_153223.3. [Q8N960-1]
DR   RefSeq; XP_011541487.1; XM_011543185.2. [Q8N960-2]
DR   RefSeq; XP_011541488.1; XM_011543186.2.
DR   RefSeq; XP_016864574.1; XM_017009085.1.
DR   PDB; 4ICW; X-ray; 2.20 A; A=1-151.
DR   PDB; 4ICX; X-ray; 2.70 A; A/B/C=1-151.
DR   PDB; 6FLJ; X-ray; 1.75 A; A=1-151.
DR   PDB; 6FLK; X-ray; 1.60 A; A/B=450-610.
DR   PDBsum; 4ICW; -.
DR   PDBsum; 4ICX; -.
DR   PDBsum; 6FLJ; -.
DR   PDBsum; 6FLK; -.
DR   AlphaFoldDB; Q8N960; -.
DR   SMR; Q8N960; -.
DR   BioGRID; 127486; 107.
DR   IntAct; Q8N960; 100.
DR   STRING; 9606.ENSP00000303058; -.
DR   MoonDB; Q8N960; Predicted.
DR   iPTMnet; Q8N960; -.
DR   PhosphoSitePlus; Q8N960; -.
DR   BioMuta; CEP120; -.
DR   DMDM; 205696377; -.
DR   EPD; Q8N960; -.
DR   jPOST; Q8N960; -.
DR   MassIVE; Q8N960; -.
DR   MaxQB; Q8N960; -.
DR   PaxDb; 9606-ENSP00000303058; -.
DR   PeptideAtlas; Q8N960; -.
DR   ProteomicsDB; 72491; -. [Q8N960-1]
DR   ProteomicsDB; 72492; -. [Q8N960-2]
DR   ProteomicsDB; 72493; -. [Q8N960-3]
DR   Pumba; Q8N960; -.
DR   Antibodypedia; 25668; 95 antibodies from 17 providers.
DR   DNASU; 153241; -.
DR   Ensembl; ENST00000306467.10; ENSP00000303058.6; ENSG00000168944.17. [Q8N960-1]
DR   Ensembl; ENST00000306481.11; ENSP00000307419.6; ENSG00000168944.17. [Q8N960-2]
DR   Ensembl; ENST00000328236.10; ENSP00000327504.5; ENSG00000168944.17. [Q8N960-1]
DR   Ensembl; ENST00000508442.7; ENSP00000421620.3; ENSG00000168944.17. [Q8N960-2]
DR   Ensembl; ENST00000513565.6; ENSP00000422089.2; ENSG00000168944.17. [Q8N960-3]
DR   GeneID; 153241; -.
DR   KEGG; hsa:153241; -.
DR   MANE-Select; ENST00000306467.10; ENSP00000303058.6; NM_001375405.1; NP_001362334.1.
DR   UCSC; uc003ktk.4; human. [Q8N960-1]
DR   AGR; HGNC:26690; -.
DR   CTD; 153241; -.
DR   DisGeNET; 153241; -.
DR   GeneCards; CEP120; -.
DR   GeneReviews; CEP120; -.
DR   HGNC; HGNC:26690; CEP120.
DR   HPA; ENSG00000168944; Low tissue specificity.
DR   MalaCards; CEP120; -.
DR   MIM; 613446; gene.
DR   MIM; 616300; phenotype.
DR   MIM; 617761; phenotype.
DR   neXtProt; NX_Q8N960; -.
DR   OpenTargets; ENSG00000168944; -.
DR   Orphanet; 474; Jeune syndrome.
DR   Orphanet; 475; Joubert syndrome.
DR   Orphanet; 220493; Joubert syndrome with ocular defect.
DR   PharmGKB; PA164717857; -.
DR   VEuPathDB; HostDB:ENSG00000168944; -.
DR   eggNOG; ENOG502QPT0; Eukaryota.
DR   GeneTree; ENSGT00390000009378; -.
DR   HOGENOM; CLU_723528_0_0_1; -.
DR   InParanoid; Q8N960; -.
DR   OMA; HTNQPEF; -.
DR   OrthoDB; 5484815at2759; -.
DR   PhylomeDB; Q8N960; -.
DR   TreeFam; TF329430; -.
DR   PathwayCommons; Q8N960; -.
DR   SignaLink; Q8N960; -.
DR   BioGRID-ORCS; 153241; 34 hits in 1167 CRISPR screens.
DR   ChiTaRS; CEP120; human.
DR   GeneWiki; CEP120; -.
DR   GenomeRNAi; 153241; -.
DR   Pharos; Q8N960; Tbio.
DR   PRO; PR:Q8N960; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q8N960; Protein.
DR   Bgee; ENSG00000168944; Expressed in calcaneal tendon and 183 other cell types or tissues.
DR   ExpressionAtlas; Q8N960; baseline and differential.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030953; P:astral microtubule organization; IEA:Ensembl.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR   GO; GO:0022027; P:interkinetic nuclear migration; IBA:GO_Central.
DR   GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR   GO; GO:1903724; P:positive regulation of centriole elongation; IMP:UniProtKB.
DR   GO; GO:0010825; P:positive regulation of centrosome duplication; ISS:UniProtKB.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR   GO; GO:1904951; P:positive regulation of establishment of protein localization; IMP:UniProtKB.
DR   CDD; cd00030; C2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR039893; CEP120-like.
DR   InterPro; IPR022136; DUF3668.
DR   PANTHER; PTHR21574:SF0; CENTROSOMAL PROTEIN OF 120 KDA; 1.
DR   PANTHER; PTHR21574; UNCHARACTERIZED; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF12416; DUF3668; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS50004; C2; 2.
DR   Genevisible; Q8N960; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Ciliopathy; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Disease variant; Joubert syndrome; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..986
FT                   /note="Centrosomal protein of 120 kDa"
FT                   /id="PRO_0000348262"
FT   DOMAIN          1..112
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          433..566
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          350..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          669..925
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        351..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         935
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TSG1"
FT   VAR_SEQ         1..26
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_035123"
FT   VAR_SEQ         347..380
FT                   /note="SLIELKTQNEHEPEHSKKKVLTPIKEKTLTGPKS -> DAFWYSALDIIFPL
FT                   FIFLFLVLDAIRKFANYEEK (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035124"
FT   VAR_SEQ         381..986
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035125"
FT   VARIANT         194
FT                   /note="V -> A (in JBTS31; uncertain significance;
FT                   dbSNP:rs1554104276)"
FT                   /evidence="ECO:0000269|PubMed:27208211"
FT                   /id="VAR_077553"
FT   VARIANT         199
FT                   /note="A -> P (in SRTD13; also found in a patient with more
FT                   complex ciliopathy; dbSNP:rs367600930)"
FT                   /evidence="ECO:0000269|PubMed:25361962,
FT                   ECO:0000269|PubMed:27208211"
FT                   /id="VAR_073672"
FT   VARIANT         549
FT                   /note="A -> V (in JBTS31; uncertain significance;
FT                   dbSNP:rs775080726)"
FT                   /evidence="ECO:0000269|PubMed:27208211"
FT                   /id="VAR_077554"
FT   VARIANT         602
FT                   /note="L -> V (in dbSNP:rs6595440)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_046126"
FT   VARIANT         712
FT                   /note="L -> F (in JBTS31; uncertain significance;
FT                   dbSNP:rs114280473)"
FT                   /evidence="ECO:0000269|PubMed:27208211"
FT                   /id="VAR_077555"
FT   VARIANT         726
FT                   /note="L -> P (in JBTS31; uncertain significance;
FT                   dbSNP:rs1554102026)"
FT                   /evidence="ECO:0000269|PubMed:27208211"
FT                   /id="VAR_077556"
FT   VARIANT         879
FT                   /note="Q -> H (in dbSNP:rs1047437)"
FT                   /id="VAR_046127"
FT   VARIANT         936
FT                   /note="V -> I (in dbSNP:rs2303721)"
FT                   /id="VAR_046128"
FT   VARIANT         947
FT                   /note="R -> H (in dbSNP:rs2303720)"
FT                   /id="VAR_046129"
FT   VARIANT         975
FT                   /note="I -> S (found in a patient with Meckel syndrome;
FT                   uncertain significance; dbSNP:rs1554098663)"
FT                   /evidence="ECO:0000269|PubMed:27208211"
FT                   /id="VAR_077557"
FT   CONFLICT        212
FT                   /note="L -> F (in Ref. 3; BAC04596)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="E -> G (in Ref. 3; BAC04596)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301
FT                   /note="H -> R (in Ref. 4; CAH10371)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        785
FT                   /note="Q -> L (in Ref. 3; BAC04596)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..6
FT                   /evidence="ECO:0007829|PDB:4ICX"
FT   STRAND          8..19
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          27..34
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          51..60
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   HELIX           62..71
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          74..83
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   TURN            84..87
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          88..98
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          125..134
FT                   /evidence="ECO:0007829|PDB:6FLJ"
FT   STRAND          452..465
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          472..478
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   HELIX           481..483
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          495..497
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          502..504
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          509..516
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   HELIX           518..527
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          530..536
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          544..551
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   HELIX           553..558
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          562..565
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          569..584
FT                   /evidence="ECO:0007829|PDB:6FLK"
FT   STRAND          592..607
FT                   /evidence="ECO:0007829|PDB:6FLK"
SQ   SEQUENCE   986 AA;  112640 MW;  97B96A09962B0862 CRC64;
     MVSKSDQLLI VVSILEGRHF PKRPKHMLVV EAKFDGEQLA TDPVDHTDQP EFATELAWEI
     DRKALHQHRL QRTPIKLQCF ALDPVTSAKE TIGYIVLDLR TAQETKQAPK WYQLLSNKYT
     KFKSEIQISI ALETDTKPPV DSFKAKGAPP RDGKVPAILA GLDPRDIVAV LNEEGGYHQI
     GPAEYCTDSF IMSVTIAFAT QLEQLIPCTM KLPERQPEFF FYYSLLGNDV TNEPFNDLIN
     PNFEPERASV RIRSSVEILR VYLALQSKLQ IHLCCGDQSL GSTEIPLTGL LKKGSTEINQ
     HPVTVEGAFT LDPPNRAKQK LAPIPVELAP TVGVSVALQR EGIDSQSLIE LKTQNEHEPE
     HSKKKVLTPI KEKTLTGPKS PTVSPVPSHN QSPPTKDDAT ESEVESLQYD KDTKPNPKAS
     SSVPASLAQL VTTSNASEVA SGQKIAVPAT SHHFCFSIDL RSIHALEIGF PINCILRYSY
     PFFGSAAPIM TNPPVEVRKN MEVFLPQSYC AFDFATMPHQ LQDTFLRIPL LVELWHKDKM
     SKDLLLGIAR IQLSNILSSE KTRFLGSNGE QCWRQTYSES VPVIAAQGSN NRIADLSYTV
     TLEDYGLVKM REIFISDSSQ GVSAVQQKPS SLPPAPCPSE IQTEPRETLE YKAALELEMW
     KEMQEDIFEN QLKQKELAHM QALAEEWKKR DRERESLVKK KVAEYTILEG KLQKTLIDLE
     KREQQLASVE SELQREKKEL QSERQRNLQE LQDSIRRAKE DCIHQVELER LKIKQLEEDK
     HRLQQQLNDA ENKYKILEKE FQQFKDQQNN KPEIRLQSEI NLLTLEKVEL ERKLESATKS
     KLHYKQQWGR ALKELARLKQ REQESQMARL KKQQEELEQM RLRYLAAEEK DTVKTERQEL
     LDIRNELNRL RQQEQKQYQD STEIASGKKD GPHGSVLEEG LDDYLTRLIE ERDTLMRTGV
     YNHEDRIISE LDRQIREILA KSNASN
//