ID DC2L1_HUMAN Reviewed; 351 AA. AC Q8TCX1; A8MVJ5; Q53F57; Q6PDB2; Q8IWA3; Q96B03; Q96J00; Q9Y370; Q9Y3S9; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=Cytoplasmic dynein 2 light intermediate chain 1; DE Short=Dynein 2 light intermediate chain {ECO:0000303|PubMed:11907264}; GN Name=DYNC2LI1; GN Synonyms=D2LIC {ECO:0000303|PubMed:11907264}, LIC3 GN {ECO:0000303|PubMed:31451806}; ORFNames=CGI-60; 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 SUBCELLULAR LOCATION. RX PubMed=11907264; DOI=10.1091/mbc.01-08-0402; RA Grissom P.M., Vaisberg E.A., McIntosh J.R.; RT "Identification of a novel light intermediate chain (D2LIC) for mammalian RT cytoplasmic dynein 2."; RL Mol. Biol. Cell 13:817-829(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-33 AND RP LEU-230. RC TISSUE=Testis; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5), AND VARIANT RP SER-58. RC TISSUE=Brain, Kidney, Testis, and Urinary bladder; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-351 (ISOFORM 3), AND VARIANTS RP SER-33 AND LEU-230. RC TISSUE=Brain; 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 2 COMPLEX. RX PubMed=25205765; DOI=10.1242/jcs.159038; RA Asante D., Stevenson N.L., Stephens D.J.; RT "Subunit composition of the human cytoplasmic dynein-2 complex."; RL J. Cell Sci. 127:4774-4787(2014). RN [10] RP FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN SRTD15, AND VARIANT SRTD15 RP VAL-117. RX PubMed=26077881; DOI=10.1038/ncomms8092; RG University of Washington Center for Mendelian Genomics Consortium; RA Taylor S.P., Dantas T.J., Duran I., Wu S., Lachman R.S., Nelson S.F., RA Cohn D.H., Vallee R.B., Krakow D.; RT "Mutations in DYNC2LI1 disrupt cilia function and cause short rib RT polydactyly syndrome."; RL Nat. Commun. 6:7092-7092(2015). RN [11] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN SRTD15, RP AND VARIANT SRTD15 ILE-220. RX PubMed=26130459; DOI=10.1038/srep11649; RA Kessler K., Wunderlich I., Uebe S., Falk N.S., Giessl A., RA Brandstaetter J.H., Popp B., Klinger P., Ekici A.B., Sticht H., Doerr H.G., RA Reis A., Roepman R., Seemanova E., Thiel C.T.; RT "DYNC2LI1 mutations broaden the clinical spectrum of dynein-2 defects."; RL Sci. Rep. 5:11649-11649(2015). RN [12] RP SUBUNIT, FUNCTION, INTERACTION WITH DYNC2H1, AND SUBCELLULAR LOCATION. RX PubMed=29742051; DOI=10.1091/mbc.e18-03-0173; RA Hamada Y., Tsurumi Y., Nozaki S., Katoh Y., Nakayama K.; RT "Interaction of WDR60 intermediate chain with TCTEX1D2 light chain of the RT dynein-2 complex is crucial for ciliary protein trafficking."; RL Mol. Biol. Cell 29:1628-1639(2018). RN [13] {ECO:0007744|PDB:6RLB, ECO:0007744|PDB:6SC2} RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF THE CYTOPLASMIC DYNEIN RP 2 COMPLEX. RX PubMed=31451806; DOI=10.1038/s41594-019-0286-y; RA Toropova K., Zalyte R., Mukhopadhyay A.G., Mladenov M., Carter A.P., RA Roberts A.J.; RT "Structure of the dynein-2 complex and its assembly with intraflagellar RT transport trains."; RL Nat. Struct. Mol. Biol. 26:823-829(2019). CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of CC the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein CC complex that drives the movement of cargos along microtubules within CC cilia and flagella in concert with the intraflagellar transport (IFT) CC system, facilitating the assembly of these organelles CC (PubMed:29742051). Involved in the regulation of ciliary length CC (PubMed:26077881, PubMed:26130459). {ECO:0000269|PubMed:26077881, CC ECO:0000269|PubMed:26130459, ECO:0000269|PubMed:29742051}. CC -!- SUBUNIT: Light intermediate chain of the cytoplasmic dynein complex 2, CC a multisubunit complex composed at least of eleven different proteins. CC The cytoplasmic dynein 2 complex consists of two catalytic heavy chains CC (HCs) and a number of non-catalytic subunits presented by intermediate CC chains (ICs), light intermediate chains (LICs) and light chains (LCs). CC Among them, a heavy chain (DYNC2H1), two intermediate chains (DYNC2I2 CC and DYNC2I1), a light intermediate chain (DYNC2LI1), and a light chain CC (DYNLT2B) are unique to the dynein-2 complex, but a subset of light CC chains are also shared by dynein-1 and dynein-2 complexes CC (PubMed:31451806, PubMed:29742051). Dynein-2 complex is built around CC two copies of cytoplasmic dynein 2 heavy chain 1 (DYNC2H1). The C- CC terminal region of DYNC2H1 forms the motor domain, which converts the CC energy from ATP hydrolysis into movement. Its N-terminal region forms CC the tail, an extended structure that binds the other subunits and holds CC the two heavy chains in a homodimer. Interacts with DYNC2H1 (via N- CC terminus); this interaction stabilizes the dynein-2 complex structure CC (PubMed:29742051). {ECO:0000269|PubMed:29742051, CC ECO:0000269|PubMed:31451806}. CC -!- INTERACTION: CC Q8TCX1; P00441: SOD1; NbExp=3; IntAct=EBI-8568003, EBI-990792; CC Q8TCX1-2; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-8568452, EBI-10303987; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11907264}. CC Cytoplasm {ECO:0000269|PubMed:26130459}. Cell projection, cilium CC {ECO:0000269|PubMed:26130459, ECO:0000269|PubMed:29742051}. Cytoplasm, CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:26130459, CC ECO:0000269|PubMed:29742051}. Cytoplasm, cytoskeleton, cilium axoneme CC {ECO:0000250|UniProtKB:Q8K0T2}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:26130459}. CC Note=Localizes to the apical cytoplasm. {ECO:0000250|UniProtKB:Q8K0T2}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q8TCX1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TCX1-2; Sequence=VSP_031289; CC Name=3; CC IsoId=Q8TCX1-3; Sequence=VSP_031292; CC Name=4; CC IsoId=Q8TCX1-4; Sequence=VSP_031290, VSP_031291; CC Name=5; CC IsoId=Q8TCX1-5; Sequence=VSP_031287, VSP_031288; CC -!- TISSUE SPECIFICITY: Expressed in bone, brain, kidney, and cartilage CC (PubMed:26077881, PubMed:26130459). Lower expression in heart, liver, CC lung, placenta and thymus (PubMed:26077881). CC {ECO:0000269|PubMed:26077881, ECO:0000269|PubMed:26130459}. CC -!- DISEASE: Short-rib thoracic dysplasia 15 with polydactyly (SRTD15) CC [MIM:617088]: A form of short-rib thoracic dysplasia, a group of CC 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:26077881, ECO:0000269|PubMed:26130459}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD34055.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY083346; AAL99216.1; -; mRNA. DR EMBL; AF151818; AAD34055.1; ALT_FRAME; mRNA. DR EMBL; AK223432; BAD97152.1; -; mRNA. DR EMBL; AC011242; AAY14702.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00289.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00290.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00291.1; -; Genomic_DNA. DR EMBL; BC006969; AAH06969.1; -; mRNA. DR EMBL; BC016324; AAH16324.1; -; mRNA. DR EMBL; BC040558; AAH40558.1; -; mRNA. DR EMBL; BC058823; AAH58823.1; -; mRNA. DR EMBL; AL050006; CAB43233.1; -; mRNA. DR CCDS; CCDS1813.1; -. [Q8TCX1-1] DR CCDS; CCDS46270.1; -. [Q8TCX1-4] DR CCDS; CCDS62903.1; -. [Q8TCX1-2] DR PIR; T08695; T08695. DR RefSeq; NP_001180393.1; NM_001193464.1. [Q8TCX1-2] DR RefSeq; NP_056337.1; NM_015522.3. [Q8TCX1-4] DR RefSeq; NP_057092.2; NM_016008.3. [Q8TCX1-1] DR PDB; 6RLB; EM; 4.50 A; E/F=1-351. DR PDB; 6SC2; EM; 3.90 A; E/F=1-351. DR PDBsum; 6RLB; -. DR PDBsum; 6SC2; -. DR AlphaFoldDB; Q8TCX1; -. DR EMDB; EMD-4918; -. DR SMR; Q8TCX1; -. DR BioGRID; 119644; 45. DR CORUM; Q8TCX1; -. DR IntAct; Q8TCX1; 20. DR MINT; Q8TCX1; -. DR STRING; 9606.ENSP00000474032; -. DR GlyGen; Q8TCX1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8TCX1; -. DR PhosphoSitePlus; Q8TCX1; -. DR BioMuta; DYNC2LI1; -. DR DMDM; 74715850; -. DR EPD; Q8TCX1; -. DR jPOST; Q8TCX1; -. DR MassIVE; Q8TCX1; -. DR MaxQB; Q8TCX1; -. DR PaxDb; 9606-ENSP00000474032; -. DR PeptideAtlas; Q8TCX1; -. DR ProteomicsDB; 74183; -. [Q8TCX1-1] DR ProteomicsDB; 74184; -. [Q8TCX1-2] DR ProteomicsDB; 74185; -. [Q8TCX1-3] DR ProteomicsDB; 74186; -. [Q8TCX1-4] DR ProteomicsDB; 74187; -. [Q8TCX1-5] DR Pumba; Q8TCX1; -. DR Antibodypedia; 47397; 106 antibodies from 21 providers. DR DNASU; 51626; -. DR Ensembl; ENST00000260605.12; ENSP00000260605.8; ENSG00000138036.18. [Q8TCX1-1] DR Ensembl; ENST00000398823.6; ENSP00000381804.2; ENSG00000138036.18. [Q8TCX1-5] DR Ensembl; ENST00000406852.7; ENSP00000385738.3; ENSG00000138036.18. [Q8TCX1-4] DR Ensembl; ENST00000605786.5; ENSP00000474032.1; ENSG00000138036.18. [Q8TCX1-2] DR GeneID; 51626; -. DR KEGG; hsa:51626; -. DR MANE-Select; ENST00000260605.12; ENSP00000260605.8; NM_016008.4; NP_057092.2. DR UCSC; uc002rth.4; human. [Q8TCX1-1] DR AGR; HGNC:24595; -. DR CTD; 51626; -. DR DisGeNET; 51626; -. DR GeneCards; DYNC2LI1; -. DR GeneReviews; DYNC2LI1; -. DR HGNC; HGNC:24595; DYNC2LI1. DR HPA; ENSG00000138036; Low tissue specificity. DR MalaCards; DYNC2LI1; -. DR MIM; 617083; gene. DR MIM; 617088; phenotype. DR neXtProt; NX_Q8TCX1; -. DR OpenTargets; ENSG00000138036; -. DR Orphanet; 289; Ellis Van Creveld syndrome. DR Orphanet; 474; Jeune syndrome. DR PharmGKB; PA142671919; -. DR VEuPathDB; HostDB:ENSG00000138036; -. DR eggNOG; KOG3929; Eukaryota. DR GeneTree; ENSGT00390000010498; -. DR HOGENOM; CLU_1492733_0_0_1; -. DR InParanoid; Q8TCX1; -. DR OMA; FWEIAQG; -. DR OrthoDB; 313424at2759; -. DR PhylomeDB; Q8TCX1; -. DR TreeFam; TF314138; -. DR PathwayCommons; Q8TCX1; -. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR SignaLink; Q8TCX1; -. DR BioGRID-ORCS; 51626; 18 hits in 1150 CRISPR screens. DR ChiTaRS; DYNC2LI1; human. DR GenomeRNAi; 51626; -. DR Pharos; Q8TCX1; Tbio. DR PRO; PR:Q8TCX1; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8TCX1; Protein. DR Bgee; ENSG00000138036; Expressed in right uterine tube and 204 other cell types or tissues. DR ExpressionAtlas; Q8TCX1; baseline and differential. DR GO; GO:0045177; C:apical part of cell; ISS:BHF-UCL. DR GO; GO:0005930; C:axoneme; ISS:BHF-UCL. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. DR GO; GO:0097542; C:ciliary tip; TAS:Reactome. DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB. DR GO; GO:0005929; C:cilium; ISS:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; ISS:BHF-UCL. DR GO; GO:0045504; F:dynein heavy chain binding; IDA:UniProtKB. DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl. DR GO; GO:0035721; P:intraciliary retrograde transport; IBA:GO_Central. DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB. DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB. DR InterPro; IPR040045; DYNC2LI1. DR InterPro; IPR022780; Dynein_light_int_chain. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR13236:SF0; CYTOPLASMIC DYNEIN 2 LIGHT INTERMEDIATE CHAIN 1; 1. DR PANTHER; PTHR13236; DYNEIN 2 LIGHT INTERMEDIATE CHAIN, ISOFORM 2; 1. DR Pfam; PF05783; DLIC; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q8TCX1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; Cilium; KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; KW Developmental protein; Disease variant; Dynein; Golgi apparatus; KW Microtubule; Motor protein; Reference proteome. FT CHAIN 1..351 FT /note="Cytoplasmic dynein 2 light intermediate chain 1" FT /id="PRO_0000318750" FT VAR_SEQ 108..144 FT /note="TFSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMK -> SWQLSSLLPVS FT MNLTTPVPHINEIIHYLSFCYLFHLA (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031287" FT VAR_SEQ 145..351 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031288" FT VAR_SEQ 169 FT /note="P -> PQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031289" FT VAR_SEQ 170..201 FT /note="DHELIDPFPVPLVIIGSKYDVFQDFESEKRKV -> VSCCLGLLLESLVPFI FT VNDNITNNFFRFLCMT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031290" FT VAR_SEQ 202..351 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031291" FT VAR_SEQ 332..351 FT /note="ELEQYKRSSSKSWKQIELDS -> VLS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_031292" FT VARIANT 33 FT /note="F -> S (in dbSNP:rs2288709)" FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.3" FT /id="VAR_038874" FT VARIANT 58 FT /note="P -> S (in dbSNP:rs17854966)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_038875" FT VARIANT 117 FT /note="L -> V (in SRTD15; dbSNP:rs201948500)" FT /evidence="ECO:0000269|PubMed:26077881" FT /id="VAR_077814" FT VARIANT 220 FT /note="T -> I (in SRTD15; dbSNP:rs886037860)" FT /evidence="ECO:0000269|PubMed:26130459" FT /id="VAR_077815" FT VARIANT 230 FT /note="I -> L (in dbSNP:rs11556157)" FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.3" FT /id="VAR_038876" FT CONFLICT 29 FT /note="I -> F (in Ref. 7; CAB43233)" FT /evidence="ECO:0000305" SQ SEQUENCE 351 AA; 39625 MW; BB4BB8B528D4A99A CRC64; MPSETLWEIA KAEVEKRGIN GSEGDGAEIA EKFVFFIGSK NGGKTTIILR CLDRDEPPKP TLALEYTYGR RAKGHNTPKD IAHFWELGGG TSLLDLISIP ITGDTLRTFS LVLVLDLSKP NDLWPTMENL LQATKSHVDK VIMKLGKTNA KAVSEMRQKI WNNMPKDHPD HELIDPFPVP LVIIGSKYDV FQDFESEKRK VICKTLRFVA HYYGASLMFT SKSEALLLKI RGVINQLAFG IDKSKSICVD QNKPLFITAG LDSFGQIGSP PVPENDIGKL HAHSPMELWK KVYEKLFPPK SINTLKDIKD PARDPQYAEN EVDEMRIQKD LELEQYKRSS SKSWKQIELD S //