ID   KLC3_HUMAN              Reviewed;         504 AA.
AC   Q6P597; A0AVM3; A2RUT6; Q6GMU2; Q8NAL1; Q8WWJ9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Kinesin light chain 3;
DE   AltName: Full=KLC2-like;
DE   AltName: Full=kinesin light chain 2;
GN   Name=KLC3; Synonyms=KLC2, KLC2L;
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 [GENOMIC DNA].
RC   TISSUE=Fibroblast;
RX   PubMed=8786141; DOI=10.1006/geno.1996.0303;
RA   Lamerdin J.E., Stilwagen S.A., Ramirez M.H., Stubbs L., Carrano A.V.;
RT   "Sequence analysis of the ERCC2 gene regions in human, mouse, and hamster
RT   reveals three linked genes.";
RL   Genomics 34:399-409(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Placenta;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Colon;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466 AND SER-502, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-498 AND SER-502, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466 AND SER-502, AND
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).
CC   -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC       that may play a role in organelle transport. Plays a role during
CC       spermiogenesis in the development of the sperm tail midpiece and in the
CC       normal function of spermatozoa (By similarity). May play a role in the
CC       formation of the mitochondrial sheath formation in the developing
CC       spermatid midpiece (By similarity). {ECO:0000250|UniProtKB:Q91W40}.
CC   -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC       Associates with microtubulin in an ATP-dependent manner. Interacts with
CC       KIF5C. Interacts with ODF1 (By similarity). Interacts with LRGUK (By
CC       similarity). Interacts with VDAC2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q91W40}.
CC   -!- INTERACTION:
CC       Q6P597; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-1643885, EBI-742038;
CC       Q6P597; Q92870-2: APBB2; NbExp=3; IntAct=EBI-1643885, EBI-21535880;
CC       Q6P597; Q8N3I7: BBS5; NbExp=3; IntAct=EBI-1643885, EBI-2892592;
CC       Q6P597; A1A5D9: BICDL2; NbExp=4; IntAct=EBI-1643885, EBI-10171799;
CC       Q6P597; Q8NA61: CBY2; NbExp=3; IntAct=EBI-1643885, EBI-741724;
CC       Q6P597; P51946: CCNH; NbExp=4; IntAct=EBI-1643885, EBI-741406;
CC       Q6P597; Q6IPU0: CENPP; NbExp=3; IntAct=EBI-1643885, EBI-10250303;
CC       Q6P597; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-1643885, EBI-10181988;
CC       Q6P597; P28329-3: CHAT; NbExp=3; IntAct=EBI-1643885, EBI-25837549;
CC       Q6P597; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-1643885, EBI-12593112;
CC       Q6P597; Q86UW9: DTX2; NbExp=6; IntAct=EBI-1643885, EBI-740376;
CC       Q6P597; P22607: FGFR3; NbExp=3; IntAct=EBI-1643885, EBI-348399;
CC       Q6P597; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-1643885, EBI-10226858;
CC       Q6P597; P01112: HRAS; NbExp=3; IntAct=EBI-1643885, EBI-350145;
CC       Q6P597; P54652: HSPA2; NbExp=3; IntAct=EBI-1643885, EBI-356991;
CC       Q6P597; O43464: HTRA2; NbExp=3; IntAct=EBI-1643885, EBI-517086;
CC       Q6P597; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-1643885, EBI-8638439;
CC       Q6P597; Q9NV31: IMP3; NbExp=3; IntAct=EBI-1643885, EBI-747481;
CC       Q6P597; O14901: KLF11; NbExp=3; IntAct=EBI-1643885, EBI-948266;
CC       Q6P597; A1A4E9: KRT13; NbExp=3; IntAct=EBI-1643885, EBI-10171552;
CC       Q6P597; P19012: KRT15; NbExp=3; IntAct=EBI-1643885, EBI-739566;
CC       Q6P597; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-1643885, EBI-10182361;
CC       Q6P597; O14777: NDC80; NbExp=3; IntAct=EBI-1643885, EBI-715849;
CC       Q6P597; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-1643885, EBI-10172876;
CC       Q6P597; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-1643885, EBI-2811583;
CC       Q6P597; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-1643885, EBI-1105124;
CC       Q6P597; Q7Z412: PEX26; NbExp=3; IntAct=EBI-1643885, EBI-752057;
CC       Q6P597; P41219: PRPH; NbExp=3; IntAct=EBI-1643885, EBI-752074;
CC       Q6P597; P47897: QARS1; NbExp=3; IntAct=EBI-1643885, EBI-347462;
CC       Q6P597; P47897-2: QARS1; NbExp=3; IntAct=EBI-1643885, EBI-10209725;
CC       Q6P597; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-1643885, EBI-10244848;
CC       Q6P597; O75558: STX11; NbExp=3; IntAct=EBI-1643885, EBI-714135;
CC       Q6P597; P15884: TCF4; NbExp=3; IntAct=EBI-1643885, EBI-533224;
CC       Q6P597; Q99598: TSNAX; NbExp=5; IntAct=EBI-1643885, EBI-742638;
CC       Q6P597; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-1643885, EBI-2799833;
CC       Q6P597; Q9BTA9: WAC; NbExp=3; IntAct=EBI-1643885, EBI-749118;
CC       Q6P597; P62258: YWHAE; NbExp=2; IntAct=EBI-1643885, EBI-356498;
CC       Q6P597; P63104: YWHAZ; NbExp=2; IntAct=EBI-1643885, EBI-347088;
CC       Q6P597; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1643885, EBI-740727;
CC       Q6P597; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-1643885, EBI-10172590;
CC       Q6P597-2; P07196: NEFL; NbExp=3; IntAct=EBI-11033402, EBI-475646;
CC       Q6P597-3; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-12076930, EBI-12811889;
CC       Q6P597-3; A1A5D9: BICDL2; NbExp=3; IntAct=EBI-12076930, EBI-10171799;
CC       Q6P597-3; Q8WUE5: CT55; NbExp=3; IntAct=EBI-12076930, EBI-6873363;
CC       Q6P597-3; Q9UJP4: KLHL21; NbExp=3; IntAct=EBI-12076930, EBI-8837113;
CC       Q6P597-3; Q9H0N5: PCBD2; NbExp=3; IntAct=EBI-12076930, EBI-634289;
CC       Q6P597-3; Q99598: TSNAX; NbExp=7; IntAct=EBI-12076930, EBI-742638;
CC       Q6P597-3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12076930, EBI-739895;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q68G30, ECO:0000250|UniProtKB:Q91W40}.
CC       Mitochondrion {ECO:0000250|UniProtKB:Q91W40}. Note=In elongating
CC       spermatid tail midpiece, localized in outer dense fibers (ODFs) and
CC       associates with mitochondria. Also localizes to the manchette in
CC       elongating spermatids. {ECO:0000250|UniProtKB:Q68G30,
CC       ECO:0000250|UniProtKB:Q91W40}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6P597-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P597-2; Sequence=VSP_017832;
CC       Name=3;
CC         IsoId=Q6P597-3; Sequence=VSP_017831;
CC   -!- DOMAIN: The heptad repeat (HR) motif is sufficient for interaction with
CC       kinesin heavy (KHL) chains and ODF1. The TPR region is involved in
CC       mitochondrial binding (By similarity). {ECO:0000250|UniProtKB:Q68G30}.
CC   -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR   EMBL; L47234; AAL48324.1; -; Genomic_DNA.
DR   EMBL; AK092481; BAC03901.1; -; mRNA.
DR   EMBL; BC062998; AAH62998.2; -; mRNA.
DR   EMBL; BC073841; AAH73841.1; -; mRNA.
DR   EMBL; BC126418; AAI26419.1; -; mRNA.
DR   EMBL; BC133037; AAI33038.1; -; mRNA.
DR   CCDS; CCDS12660.2; -. [Q6P597-1]
DR   RefSeq; NP_803136.2; NM_177417.2. [Q6P597-1]
DR   AlphaFoldDB; Q6P597; -.
DR   SMR; Q6P597; -.
DR   BioGRID; 127078; 118.
DR   CORUM; Q6P597; -.
DR   ELM; Q6P597; -.
DR   IntAct; Q6P597; 96.
DR   MINT; Q6P597; -.
DR   STRING; 9606.ENSP00000375810; -.
DR   iPTMnet; Q6P597; -.
DR   PhosphoSitePlus; Q6P597; -.
DR   BioMuta; KLC3; -.
DR   DMDM; 91207086; -.
DR   EPD; Q6P597; -.
DR   jPOST; Q6P597; -.
DR   MassIVE; Q6P597; -.
DR   MaxQB; Q6P597; -.
DR   PaxDb; 9606-ENSP00000375810; -.
DR   PeptideAtlas; Q6P597; -.
DR   ProteomicsDB; 66995; -. [Q6P597-1]
DR   ProteomicsDB; 66996; -. [Q6P597-2]
DR   ProteomicsDB; 66997; -. [Q6P597-3]
DR   Pumba; Q6P597; -.
DR   TopDownProteomics; Q6P597-1; -. [Q6P597-1]
DR   TopDownProteomics; Q6P597-2; -. [Q6P597-2]
DR   Antibodypedia; 31299; 168 antibodies from 23 providers.
DR   DNASU; 147700; -.
DR   Ensembl; ENST00000391946.7; ENSP00000375810.2; ENSG00000104892.17. [Q6P597-1]
DR   Ensembl; ENST00000470402.1; ENSP00000436019.1; ENSG00000104892.17. [Q6P597-3]
DR   Ensembl; ENST00000585434.5; ENSP00000466067.1; ENSG00000104892.17. [Q6P597-2]
DR   GeneID; 147700; -.
DR   KEGG; hsa:147700; -.
DR   MANE-Select; ENST00000391946.7; ENSP00000375810.2; NM_177417.3; NP_803136.2.
DR   UCSC; uc002pbf.2; human. [Q6P597-1]
DR   AGR; HGNC:20717; -.
DR   CTD; 147700; -.
DR   DisGeNET; 147700; -.
DR   GeneCards; KLC3; -.
DR   HGNC; HGNC:20717; KLC3.
DR   HPA; ENSG00000104892; Tissue enhanced (esophagus, skin).
DR   MIM; 601334; gene.
DR   neXtProt; NX_Q6P597; -.
DR   OpenTargets; ENSG00000104892; -.
DR   PharmGKB; PA142671588; -.
DR   VEuPathDB; HostDB:ENSG00000104892; -.
DR   eggNOG; KOG1840; Eukaryota.
DR   GeneTree; ENSGT00940000162356; -.
DR   InParanoid; Q6P597; -.
DR   OrthoDB; 5392083at2759; -.
DR   PhylomeDB; Q6P597; -.
DR   TreeFam; TF314010; -.
DR   PathwayCommons; Q6P597; -.
DR   Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR   Reactome; R-HSA-5625970; RHO GTPases activate KTN1.
DR   Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-HSA-983189; Kinesins.
DR   SignaLink; Q6P597; -.
DR   BioGRID-ORCS; 147700; 18 hits in 1154 CRISPR screens.
DR   GeneWiki; KLC3; -.
DR   GenomeRNAi; 147700; -.
DR   Pharos; Q6P597; Tbio.
DR   PRO; PR:Q6P597; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q6P597; Protein.
DR   Bgee; ENSG00000104892; Expressed in upper arm skin and 154 other cell types or tissues.
DR   ExpressionAtlas; Q6P597; baseline and differential.
DR   GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0008088; P:axo-dendritic transport; IEA:Ensembl.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0120317; P:sperm mitochondrial sheath assembly; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45783; KINESIN LIGHT CHAIN; 1.
DR   PANTHER; PTHR45783:SF1; KINESIN LIGHT CHAIN 3; 1.
DR   Pfam; PF13424; TPR_12; 2.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
DR   Genevisible; Q6P597; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Differentiation; Microtubule; Mitochondrion; Motor protein; Phosphoprotein;
KW   Reference proteome; Repeat; Spermatogenesis; TPR repeat.
FT   CHAIN           1..504
FT                   /note="Kinesin light chain 3"
FT                   /id="PRO_0000230785"
FT   REPEAT          207..240
FT                   /note="TPR 1"
FT   REPEAT          249..282
FT                   /note="TPR 2"
FT   REPEAT          291..324
FT                   /note="TPR 3"
FT   REPEAT          333..366
FT                   /note="TPR 4"
FT   REPEAT          375..408
FT                   /note="TPR 5"
FT   REGION          153..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          90..150
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        157..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91W40"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         498
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         502
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1
FT                   /note="M -> MIPQTPHHCSPGAAM (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_017831"
FT   VAR_SEQ         163
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017832"
FT   CONFLICT        352
FT                   /note="V -> A (in Ref. 2; BAC03901)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   504 AA;  55364 MW;  3767D66C79EA3D49 CRC64;
     MSVQVAAPGS AGLGPERLSP EELVRQTRQV VQGLEALRAE HHGLAGHLAE ALAGQGPAAG
     LEMLEEKQQV VSHSLEAIEL GLGEAQVLLA LSAHVGALEA EKQRLRSQAR RLAQENVWLR
     EELEETQRRL RASEESVAQL EEEKRHLEFL GQLRQYDPPA ESQQSESPPR RDSLASLFPS
     EEEERKGPEA AGAAAAQQGG YEIPARLRTL HNLVIQYAGQ GRYEVAVPLC RQALEDLERS
     SGHCHPDVAT MLNILALVYR DQNKYKEATD LLHDALQIRE QTLGPEHPAV AATLNNLAVL
     YGKRGRYREA EPLCQRALEI REKVLGADHP DVAKQLNNLA LLCQNQGKFE DVERHYARAL
     SIYEALGGPH DPNVAKTKNN LASAYLKQNK YQQAEELYKE ILHKEDLPAP LGAPNTGTAG
     DAEQALRRSS SLSKIRESIR RGSEKLVSRL RGEAAAGAAG MKRAMSLNTL NVDAPRAPGT
     QFPSWHLDKA PRTLSASTQD LSPH
//