DC2L1_HUMAN
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 03-AUG-2022, entry version 135.
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},
GN LIC3 {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};
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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 SMR; Q8TCX1; -.
DR BioGRID; 119644; 34.
DR CORUM; Q8TCX1; -.
DR IntAct; Q8TCX1; 20.
DR MINT; Q8TCX1; -.
DR STRING; 9606.ENSP00000474032; -.
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; Q8TCX1; -.
DR PeptideAtlas; Q8TCX1; -.
DR PRIDE; 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 Antibodypedia; 47397; 96 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 CTD; 51626; -.
DR DisGeNET; 51626; -.
DR GeneCards; 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; IRKHTCR; -.
DR OrthoDB; 910690at2759; -.
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 1072 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 202 other tissues.
DR ExpressionAtlas; Q8TCX1; baseline and differential.
DR Genevisible; Q8TCX1; HS.
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; PTHR13236; 1.
DR Pfam; PF05783; DLIC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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
