ID   IF172_HUMAN             Reviewed;        1749 AA.
AC   Q9UG01; A5PKZ0; B2RNU5; Q86X44; Q96HW4; Q9UFJ9; Q9ULP1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   02-SEP-2026, entry version 176.
DE   RecName: Full=Intraflagellar transport protein 172 homolog;
GN   Name=IFT172; Synonyms=KIAA1179;
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=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, and Lung;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-1749 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1203-1737 (ISOFORM 2).
RC   TISSUE=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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 660-1749 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [6]
RP   SUMOYLATION AT LYS-4, AND ACETYLATION AT MET-1.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20388717; DOI=10.1074/jbc.m110.106955;
RA   Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA   Eriksson J.E., Sistonen L.;
RT   "In vivo identification of sumoylation sites by a signature tag and
RT   cysteine-targeted affinity purification.";
RL   J. Biol. Chem. 285:19324-19329(2010).
RN   [7]
RP   SUBCELLULAR LOCATION, AND VARIANTS SRTD10 TRP-296; ASN-411; 464-ASP-ILE-465
RP   DEL; PRO-1536; CYS-1544 AND ARG-1727.
RX   PubMed=24140113; DOI=10.1016/j.ajhg.2013.09.012;
RG   UK10K Consortium;
RA   Halbritter J., Bizet A.A., Schmidts M., Porath J.D., Braun D.A., Gee H.Y.,
RA   McInerney-Leo A.M., Krug P., Filhol E., Davis E.E., Airik R.,
RA   Czarnecki P.G., Lehman A.M., Trnka P., Nitschke P., Bole-Feysot C.,
RA   Schueler M., Knebelmann B., Burtey S., Szabo A.J., Tory K., Leo P.J.,
RA   Gardiner B., McKenzie F.A., Zankl A., Brown M.A., Hartley J.L., Maher E.R.,
RA   Li C., Leroux M.R., Scambler P.J., Zhan S.H., Jones S.J., Kayserili H.,
RA   Tuysuz B., Moorani K.N., Constantinescu A., Krantz I.D., Kaplan B.S.,
RA   Shah J.V., Hurd T.W., Doherty D., Katsanis N., Duncan E.L., Otto E.A.,
RA   Beales P.L., Mitchison H.M., Saunier S., Hildebrandt F.;
RT   "Defects in the IFT-B component IFT172 cause Jeune and Mainzer-Saldino
RT   syndromes in humans.";
RL   Am. J. Hum. Genet. 93:915-925(2013).
RN   [8]
RP   VARIANTS RP71 PRO-257 AND GLU-1605, VARIANT BBS20 GLN-1567,
RP   CHARACTERIZATION OF VARIANTS RP71 PRO-257 AND GLU-1605, CHARACTERIZATION OF
RP   VARIANT BBS20 GLN-1567, INVOLVEMENT IN RP71, AND INVOLVEMENT IN BBS20.
RX   PubMed=25168386; DOI=10.1093/hmg/ddu441;
RA   Bujakowska K.M., Zhang Q., Siemiatkowska A.M., Liu Q., Place E., Falk M.J.,
RA   Consugar M., Lancelot M.E., Antonio A., Lonjou C., Carpentier W.,
RA   Mohand-Said S., den Hollander A.I., Cremers F.P., Leroy B.P., Gai X.,
RA   Sahel J.A., van den Born L.I., Collin R.W., Zeitz C., Audo I., Pierce E.A.;
RT   "Mutations in IFT172 cause isolated retinal degeneration and Bardet-Biedl
RT   syndrome.";
RL   Hum. Mol. Genet. 24:230-242(2015).
RN   [9]
RP   VARIANTS BBS20 ARG-493 AND TYR-719.
RX   PubMed=32451492; DOI=10.1038/s10038-020-0778-y;
RA   Hirano M., Satake W., Moriyama N., Saida K., Okamoto N., Cha P.C.,
RA   Suzuki Y., Kusunoki S., Toda T.;
RT   "Bardet-Biedl syndrome and related disorders in Japan.";
RL   J. Hum. Genet. 65:847-853(2020).
CC   -!- FUNCTION: Required for the maintenance and formation of cilia. Plays an
CC       indirect role in hedgehog (Hh) signaling, cilia being required for all
CC       activity of the hedgehog pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with IFT88 (By similarity). Interacts with IFT57 (By
CC       similarity). Interacts with RABL2/RABL2A; binds preferentially to GDP-
CC       bound RABL2 (By similarity). {ECO:0000250|UniProtKB:Q6VH22}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000269|PubMed:24140113}. Note=Localized to the axoneme and around
CC       the base of the cilium.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UG01-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UG01-2; Sequence=VSP_032848, VSP_032849;
CC       Name=3;
CC         IsoId=Q9UG01-3; Sequence=VSP_054428, VSP_054429;
CC   -!- DISEASE: Short-rib thoracic dysplasia 10 with or without polydactyly
CC       (SRTD10) [MIM:615630]: 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:24140113}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Retinitis pigmentosa 71 (RP71) [MIM:616394]: A retinal
CC       dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC       pigmentosa is characterized by retinal pigment deposits visible on
CC       fundus examination and primary loss of rod photoreceptor cells followed
CC       by secondary loss of cone photoreceptors. Patients typically have night
CC       vision blindness and loss of midperipheral visual field. As their
CC       condition progresses, they lose their far peripheral visual field and
CC       eventually central vision as well. {ECO:0000269|PubMed:25168386}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- DISEASE: Bardet-Biedl syndrome 20 (BBS20) [MIM:619471]: A form of
CC       Bardet-Biedl syndrome, a syndrome characterized by usually severe
CC       pigmentary retinopathy, early-onset obesity, polydactyly,
CC       hypogenitalism, renal malformation and intellectual disability.
CC       Secondary features include diabetes mellitus, hypertension and
CC       congenital heart disease. Bardet-Biedl syndrome inheritance is
CC       autosomal recessive, but three mutated alleles (two at one locus, and a
CC       third at a second locus) may be required for clinical manifestation of
CC       some forms of the disease. {ECO:0000269|PubMed:25168386,
CC       ECO:0000269|PubMed:32451492}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the IFT172 family. {ECO:0000305}.
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DR   EMBL; AC074117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471053; EAX00573.1; -; Genomic_DNA.
DR   EMBL; BC008024; AAH08024.1; -; mRNA.
DR   EMBL; BC047294; AAH47294.1; -; mRNA.
DR   EMBL; BC137126; AAI37127.1; -; mRNA.
DR   EMBL; BC142675; AAI42676.1; -; mRNA.
DR   EMBL; BC142729; AAI42730.1; -; mRNA.
DR   EMBL; AL110218; CAB53678.1; -; mRNA.
DR   EMBL; AL117421; CAB55914.2; -; mRNA.
DR   EMBL; AB033005; BAA86493.1; -; mRNA.
DR   CCDS; CCDS1755.1; -. [Q9UG01-1]
DR   PIR; T14758; T14758.
DR   PIR; T17224; T17224.
DR   RefSeq; NP_056477.1; NM_015662.3. [Q9UG01-1]
DR   PDB; 9H2D; X-ray; 2.10 A; A/B=1471-1742.
DR   AlphaFoldDB; Q9UG01; -.
DR   SMR; Q9UG01; -.
DR   BioGRID; 117589; 56.
DR   ComplexPortal; CPX-5022; Intraflagellar transport complex B.
DR   CORUM; Q9UG01; -.
DR   FunCoup; Q9UG01; 488.
DR   IntAct; Q9UG01; 49.
DR   MINT; Q9UG01; -.
DR   NDEx; IQUERY-CP-IFT172; 7 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000260570; -.
DR   GlyGen; Q9UG01; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UG01; -.
DR   PhosphoSitePlus; Q9UG01; -.
DR   BioMuta; IFT172; -.
DR   DMDM; 182662418; -.
DR   jPOST; Q9UG01; -.
DR   MassIVE; Q9UG01; -.
DR   PaxDb; 9606-ENSP00000260570; -.
DR   PeptideAtlas; Q9UG01; -.
DR   ProteomicsDB; 726; -.
DR   ProteomicsDB; 84196; -. [Q9UG01-1]
DR   ProteomicsDB; 84197; -. [Q9UG01-2]
DR   Pumba; Q9UG01; -.
DR   Antibodypedia; 28528; 85 antibodies from 20 providers.
DR   DNASU; 26160; -.
DR   Ensembl; ENST00000260570.8; ENSP00000260570.3; ENSG00000138002.17. [Q9UG01-1]
DR   Ensembl; ENST00000359466.10; ENSP00000352443.6; ENSG00000138002.17. [Q9UG01-3]
DR   Ensembl; ENST00000674701.1; ENSP00000502275.1; ENSG00000138002.17. [Q9UG01-3]
DR   GeneID; 26160; -.
DR   KEGG; hsa:26160; -.
DR   MANE-Select; ENST00000260570.8; ENSP00000260570.3; NM_015662.3; NP_056477.1.
DR   UCSC; uc002rku.4; human. [Q9UG01-1]
DR   AGR; HGNC:30391; -.
DR   ClinPGx; PA142671666; -.
DR   CTD; 26160; -.
DR   DisGeNET; 26160; -.
DR   GeneCards; IFT172; -.
DR   GeneReviews; IFT172; -.
DR   HGNC; HGNC:30391; IFT172.
DR   HPA; ENSG00000138002; Low tissue specificity.
DR   MalaCards; IFT172; -.
DR   MIM; 607386; gene.
DR   MIM; 615630; phenotype.
DR   MIM; 616394; phenotype.
DR   MIM; 619471; phenotype.
DR   OpenTargets; ENSG00000138002; -.
DR   Orphanet; 110; Bardet-Biedl syndrome.
DR   Orphanet; 474; Jeune syndrome.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   Orphanet; 140969; Saldino-Mainzer syndrome.
DR   VEuPathDB; HostDB:ENSG00000138002; -.
DR   eggNOG; KOG3616; Eukaryota.
DR   GeneTree; ENSGT00940000153417; -.
DR   HOGENOM; CLU_002716_0_0_1; -.
DR   InParanoid; Q9UG01; -.
DR   OMA; LKRTIWQ; -.
DR   OrthoDB; 2186662at2759; -.
DR   PAN-GO; Q9UG01; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9UG01; -.
DR   PathwayCommons; Q9UG01; -.
DR   Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR   Reactome; R-HSA-5620924; Intraflagellar transport.
DR   SignaLink; Q9UG01; -.
DR   SIGNOR; Q9UG01; -.
DR   Agora; ENSG00000138002; -.
DR   BioGRID-ORCS; 26160; 14 hits in 1155 CRISPR screens.
DR   ChiTaRS; IFT172; human.
DR   GenomeRNAi; 26160; -.
DR   Pharos; Q9UG01; Tbio.
DR   PRO; PR:Q9UG01; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9UG01; protein.
DR   Bgee; ENSG00000138002; Expressed in right uterine tube and 158 other cell types or tissues.
DR   ExpressionAtlas; Q9UG01; baseline and differential.
DR   GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR   GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR   GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR   GO; GO:0030991; C:intraciliary transport particle A; IDA:MGI.
DR   GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal.
DR   GO; GO:0097598; C:sperm cytoplasmic droplet; IEA:Ensembl.
DR   GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR   GO; GO:0097228; C:sperm principal piece; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IDA:UniProtKB.
DR   GO; GO:0035720; P:intraciliary anterograde transport; NAS:ComplexPortal.
DR   GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   FunFam; 1.25.40.470:FF:000008; Intraflagellar transport protein 172 homolog; 1.
DR   FunFam; 1.25.40.470:FF:000012; intraflagellar transport protein 172 homolog; 1.
DR   FunFam; 1.25.40.470:FF:000013; intraflagellar transport protein 172 homolog; 1.
DR   FunFam; 2.130.10.10:FF:000345; intraflagellar transport protein 172 homolog; 1.
DR   FunFam; 2.130.10.10:FF:000387; intraflagellar transport protein 172 homolog; 1.
DR   Gene3D; 1.25.40.470; -; 3.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR060769; EIF3B-like_beta-prop_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR056168; TPR_IF140/IFT172/WDR19.
DR   InterPro; IPR056157; TPR_IFT80_172_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR15722; IFT140/172-RELATED; 1.
DR   PANTHER; PTHR15722:SF2; INTRAFLAGELLAR TRANSPORT PROTEIN 172 HOMOLOG; 1.
DR   Pfam; PF24762; TPR_IF140-IFT172; 1.
DR   Pfam; PF23387; TPR_IFT80_172; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PDBsum; 9H2D; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Bardet-Biedl syndrome;
KW   Cell projection; Ciliopathy; Cilium; Developmental protein;
KW   Disease variant; Isopeptide bond; Methylation; Obesity;
KW   Proteomics identification; Reference proteome; Repeat;
KW   Retinitis pigmentosa; TPR repeat; Ubl conjugation; WD repeat.
FT   CHAIN           1..1749
FT                   /note="Intraflagellar transport protein 172 homolog"
FT                   /id="PRO_0000328941"
FT   REPEAT          14..53
FT                   /note="WD 1"
FT   REPEAT          64..103
FT                   /note="WD 2"
FT   REPEAT          110..148
FT                   /note="WD 3"
FT   REPEAT          150..191
FT                   /note="WD 4"
FT   REPEAT          195..233
FT                   /note="WD 5"
FT   REPEAT          238..278
FT                   /note="WD 6"
FT   REPEAT          284..323
FT                   /note="WD 7"
FT   REPEAT          483..520
FT                   /note="WD 8"
FT   REPEAT          521..559
FT                   /note="WD 9"
FT   REPEAT          593..624
FT                   /note="TPR 1"
FT   REPEAT          692..725
FT                   /note="TPR 2"
FT   REPEAT          809..842
FT                   /note="TPR 3"
FT   REPEAT          854..887
FT                   /note="TPR 4"
FT   REPEAT          912..945
FT                   /note="TPR 5"
FT   REPEAT          947..970
FT                   /note="TPR 6"
FT   REPEAT          971..1004
FT                   /note="TPR 7"
FT   REPEAT          1042..1075
FT                   /note="TPR 8"
FT   REPEAT          1142..1175
FT                   /note="TPR 9"
FT   REPEAT          1276..1309
FT                   /note="TPR 10"
FT   REPEAT          1345..1378
FT                   /note="TPR 11"
FT   REPEAT          1411..1445
FT                   /note="TPR 12"
FT   REPEAT          1447..1477
FT                   /note="TPR 13"
FT   REPEAT          1574..1607
FT                   /note="TPR 14"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:20388717"
FT   MOD_RES         672
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6VH22"
FT   CROSSLNK        4
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT   VAR_SEQ         509..532
FT                   /note="LHLYDIESCSKTMILNFCSYMQWV -> VRRATKALGIGWPTEGVRQAATRD
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054428"
FT   VAR_SEQ         533..1749
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054429"
FT   VAR_SEQ         1514..1525
FT                   /note="CENLVKSSEANS -> AVLSPSSSVKTW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_032848"
FT   VAR_SEQ         1526..1749
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_032849"
FT   VARIANT         257
FT                   /note="L -> P (in RP71; represents a null allele;
FT                   dbSNP:rs786205857)"
FT                   /evidence="ECO:0000269|PubMed:25168386"
FT                   /id="VAR_073800"
FT   VARIANT         296
FT                   /note="R -> W (in SRTD10; dbSNP:rs145541911)"
FT                   /evidence="ECO:0000269|PubMed:24140113"
FT                   /id="VAR_070956"
FT   VARIANT         411
FT                   /note="I -> N (in SRTD10; dbSNP:rs587777085)"
FT                   /evidence="ECO:0000269|PubMed:24140113"
FT                   /id="VAR_070957"
FT   VARIANT         464..465
FT                   /note="Missing (in SRTD10)"
FT                   /evidence="ECO:0000269|PubMed:24140113"
FT                   /id="VAR_070958"
FT   VARIANT         493
FT                   /note="L -> R (in BBS20; uncertain significance;
FT                   dbSNP:rs1282056614)"
FT                   /evidence="ECO:0000269|PubMed:32451492"
FT                   /id="VAR_086152"
FT   VARIANT         719
FT                   /note="H -> Y (in BBS20; uncertain significance;
FT                   dbSNP:rs144645349)"
FT                   /evidence="ECO:0000269|PubMed:32451492"
FT                   /id="VAR_086153"
FT   VARIANT         953
FT                   /note="R -> H (in dbSNP:rs704793)"
FT                   /id="VAR_042581"
FT   VARIANT         1536
FT                   /note="L -> P (in SRTD10; dbSNP:rs587777080)"
FT                   /evidence="ECO:0000269|PubMed:24140113"
FT                   /id="VAR_070959"
FT   VARIANT         1544
FT                   /note="R -> C (in SRTD10; dbSNP:rs587777079)"
FT                   /evidence="ECO:0000269|PubMed:24140113"
FT                   /id="VAR_070960"
FT   VARIANT         1567
FT                   /note="H -> Q (in BBS20; hypomorphic mutation;
FT                   dbSNP:rs786205855)"
FT                   /evidence="ECO:0000269|PubMed:25168386"
FT                   /id="VAR_073801"
FT   VARIANT         1605
FT                   /note="D -> E (in RP71; hypomorphic mutation;
FT                   dbSNP:rs786205856)"
FT                   /evidence="ECO:0000269|PubMed:25168386"
FT                   /id="VAR_073802"
FT   VARIANT         1727
FT                   /note="C -> R (in SRTD10; dbSNP:rs149614625)"
FT                   /evidence="ECO:0000269|PubMed:24140113"
FT                   /id="VAR_070961"
FT   CONFLICT        1475
FT                   /note="P -> L (in Ref. 4; CAB55914)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1478..1489
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   STRAND          1491..1493
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1497..1499
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1500..1520
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1526..1548
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1551..1553
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1554..1564
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1565..1567
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1573..1586
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1590..1609
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1618..1620
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1630..1632
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1639..1652
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   STRAND          1668..1670
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   TURN            1677..1679
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   TURN            1687..1689
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   STRAND          1695..1699
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   STRAND          1706..1708
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1709..1722
FT                   /evidence="ECO:0007829|PDB:9H2D"
FT   HELIX           1725..1738
FT                   /evidence="ECO:0007829|PDB:9H2D"
SQ   SEQUENCE   1749 AA;  197576 MW;  78AA83802D79E3CE CRC64;
     MHLKHLRTLL SPQDGAAKVT CMAWSQNNAK FAVCTVDRVV LLYDEHGERR DKFSTKPADM
     KYGRKSYMVK GMAFSPDSTK IAIGQTDNII YVYKIGEDWG DKKVICNKFI QTSAVTCLQW
     PAEYIIVFGL AEGKVRLANT KTNKSSTIYG TESYVVSLTT NCSGKGILSG HADGTIVRYF
     FDDEGSGESQ GKLVNHPCPP YALAWATNSI VAAGCDRKIV AYGKEGHMLQ TFDYSRDPQE
     REFTTAVSSP GGQSVVLGSY DRLRVFNWIP RRSIWEEAKP KEITNLYTIT ALAWKRDGSR
     LCVGTLCGGV EQFDCCLRRS IYKNKFELTY VGPSQVIVKN LSSGTRVVLK SHYGYEVEEV
     KILGKERYLV AHTSETLLLG DLNTNRLSEI AWQGSGGNEK YFFENENVCM IFNAGELTLV
     EYGNNDTLGS VRTEFMNPHL ISVRINERCQ RGTEDNKKLA YLIDIKTIAI VDLIGGYNIG
     TVSHESRVDW LELNETGHKL LFRDRKLRLH LYDIESCSKT MILNFCSYMQ WVPGSDVLVA
     QNRNSLCVWY NIEAPERVTM FTIRGDVIGL ERGGGKTEVM VMEGVTTVAY TLDEGLIEFG
     TAIDDGNYIR ATAFLETLEM TPETEAMWKT LSKLALEARQ LHIAERCFSA LGQVAKARFL
     HETNEIADQV SREYGGEGTD FYQVRARLAM LEKNYKLAEM IFLEQNAVEE AMGMYQELHR
     WDECIAVAEA KGHPALEKLR RSYYQWLMDT QQEERAGELQ ESQGDGLAAI SLYLKAGLPA
     KAARLVLTRE ELLANTELVE HITAALIKGE LYERAGDLFE KIHNPQKALE CYRKGNAFMK
     AVELARLAFP VEVVKLEEAW GDHLVQQKQL DAAINHYIEA RCSIKAIEAA LGARQWKKAI
     YILDLQDRNT ASKYYPLVAQ HYASLQEYEI AEELYTKGDR TKDAIDMYTQ AGRWEQAHKL
     AMKCMRPEDV SVLYITQAQE MEKQGKYREA ERLYVTVQEP DLAITMYKKH KLYDDMIRLV
     GKHHPDLLSD THLHLGKELE AEGRLQEAEY HYLEAQEWKA TVNMYRASGL WEEAYRVART
     QGGANAHKHV AYLWAKSLGG EAAVRLLNKL GLLEAAVDHA ADNCSFEFAF ELSRLALKHK
     TPEVHLKYAM FLEDEGKFEE AEAEFIRAGK PKEAVLMFVH NQDWEAAQRV AEAHDPDSVA
     EVLVGQARGA LEEKDFQKAE GLLLRAQRPG LALNYYKEAG LWSDALRICK DYVPSQLEAL
     QEEYEREATK KGARGVEGFV EQARHWEQAG EYSRAVDCYL KVRDSGNSGL AEKCWMKAAE
     LSIKFLPPQR NMEVVLAVGP QLIGIGKHSA AAELYLNLDL VKEAIDAFIE GEEWNKAKRV
     AKELDPRYED YVDQHYKEFL KNQGKVDSLV GVDVIAALDL YVEQGQWDKC IETATKQNYK
     ILHKYVALYA THLIREGSSA QALALYVQHG APANPQNFNI YKRIFTDMVS SPGTNCAEAY
     HSWADLRDVL FNLCENLVKS SEANSPAHEE FKTMLLIAHY YATRSAAQSV KQLETVAARL
     SVSLLRHTQL LPVDKAFYEA GIAAKAVGWD NMAFIFLNRF LDLTDAIEEG TLDGLDHSDF
     QDTDIPFEVP LPAKQHVPEA EREEVRDWVL TVSMDQRLEQ VLPRDERGAY EASLVAASTG
     VRALPCLITG YPILRNKIEF KRPGKAANKD NWNKFLMAIK TSHSPVCQDV LKFISQWCGG
     LPSTSFSFQ
//