ID KLC2_HUMAN Reviewed; 622 AA. AC Q9H0B6; A8MXL7; B2RDY4; Q9H9C8; Q9HA20; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 23-MAY-2018, entry version 171. DE RecName: Full=Kinesin light chain 2; DE Short=KLC 2; GN Name=KLC2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Mammary gland, 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-582 AND RP SER-589, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [8] RP IDENTIFICATION BY 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-445; SER-581; RP SER-582 AND SER-589, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] 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., RA Buerckstuemmer T., 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582 AND SER-610, 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-521; SER-581; RP SER-582; SER-589; SER-608; SER-610 AND SER-615, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [13] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP INVOLVEMENT IN SPOAN. RX PubMed=26385635; DOI=10.1093/hmg/ddv388; RA Melo U.S., Macedo-Souza L.I., Figueiredo T., Muotri A.R., RA Gleeson J.G., Coux G., Armas P., Calcaterra N.B., Kitajima J.P., RA Amorim S., Olavio T.R., Griesi-Oliveira K., Coatti G.C., Rocha C.R., RA Martins-Pinheiro M., Menck C.F., Zaki M.S., Kok F., Zatz M., RA Santos S.; RT "Overexpression of KLC2 due to a homozygous deletion in the non-coding RT region causes SPOAN syndrome."; RL Hum. Mol. Genet. 24:6877-6885(2015). CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing CC protein that may play a role in organelle transport. The light CC chain may function in coupling of cargo to the heavy chain or in CC the modulation of its ATPase activity (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two CC light chains. {ECO:0000250}. CC -!- INTERACTION: CC Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-726994, EBI-2869338; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H0B6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H0B6-2; Sequence=VSP_043486; CC Note=No experimental confirmation available.; CC -!- DISEASE: Spastic paraplegia, optic atrophy, and neuropathy (SPOAN) CC [MIM:609541]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness CC and spasticity of the lower limbs. Rate of progression and the CC severity of symptoms are quite variable. Initial symptoms may CC include difficulty with balance, weakness and stiffness in the CC legs, muscle spasms, and dragging the toes when walking. In some CC forms of the disorder, bladder symptoms (such as incontinence) may CC appear, or the weakness and stiffness may spread to other parts of CC the body. SPOAN is characterized by spastic paraplegia with CC progressive joint contractures and spine deformities, loss of CC independent ambulation by age 10 years, sub-normal vision CC secondary to congenital optic atrophy, and neuropathy. Inheritance CC is autosomal recessive. {ECO:0000269|PubMed:26385635}. Note=The CC gene represented in this entry is involved in disease CC pathogenesis. The disease is caused by a homozygous deletion in CC the non-coding region of the KLC2 gene. CC {ECO:0000269|PubMed:26385635}. CC -!- SIMILARITY: Belongs to the kinesin light chain family. CC {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; AL136864; CAB66798.1; -; mRNA. DR EMBL; AK022449; BAB14039.1; -; mRNA. DR EMBL; AK022907; BAB14302.1; -; mRNA. DR EMBL; AK094593; BAG52895.1; -; mRNA. DR EMBL; AK315725; BAG38081.1; -; mRNA. DR EMBL; AP000759; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001107; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034373; AAH34373.1; -; mRNA. DR CCDS; CCDS44653.1; -. [Q9H0B6-2] DR CCDS; CCDS8130.1; -. [Q9H0B6-1] DR RefSeq; NP_001128246.1; NM_001134774.1. [Q9H0B6-2] DR RefSeq; NP_001128247.1; NM_001134775.1. [Q9H0B6-1] DR RefSeq; NP_001128248.1; NM_001134776.1. [Q9H0B6-1] DR RefSeq; NP_001305663.1; NM_001318734.1. [Q9H0B6-1] DR RefSeq; NP_073733.1; NM_022822.2. [Q9H0B6-1] DR RefSeq; XP_005274240.1; XM_005274183.1. [Q9H0B6-1] DR UniGene; Hs.280792; -. DR PDB; 3CEQ; X-ray; 2.75 A; A/B=217-480. DR PDB; 3EDT; X-ray; 2.70 A; B/D/F/H=217-480. DR PDBsum; 3CEQ; -. DR PDBsum; 3EDT; -. DR ProteinModelPortal; Q9H0B6; -. DR SMR; Q9H0B6; -. DR BioGrid; 122313; 78. DR DIP; DIP-40381N; -. DR ELM; Q9H0B6; -. DR IntAct; Q9H0B6; 42. DR MINT; Q9H0B6; -. DR STRING; 9606.ENSP00000314837; -. DR iPTMnet; Q9H0B6; -. DR PhosphoSitePlus; Q9H0B6; -. DR BioMuta; KLC2; -. DR DMDM; 13878553; -. DR EPD; Q9H0B6; -. DR MaxQB; Q9H0B6; -. DR PaxDb; Q9H0B6; -. DR PeptideAtlas; Q9H0B6; -. DR PRIDE; Q9H0B6; -. DR DNASU; 64837; -. DR Ensembl; ENST00000316924; ENSP00000314837; ENSG00000174996. [Q9H0B6-1] DR Ensembl; ENST00000394066; ENSP00000377630; ENSG00000174996. [Q9H0B6-2] DR Ensembl; ENST00000394067; ENSP00000377631; ENSG00000174996. [Q9H0B6-1] DR Ensembl; ENST00000417856; ENSP00000399403; ENSG00000174996. [Q9H0B6-1] DR Ensembl; ENST00000421552; ENSP00000408484; ENSG00000174996. [Q9H0B6-2] DR GeneID; 64837; -. DR KEGG; hsa:64837; -. DR UCSC; uc001ohb.3; human. [Q9H0B6-1] DR CTD; 64837; -. DR DisGeNET; 64837; -. DR EuPathDB; HostDB:ENSG00000174996.11; -. DR GeneCards; KLC2; -. DR HGNC; HGNC:20716; KLC2. DR HPA; HPA040416; -. DR HPA; HPA040434; -. DR MalaCards; KLC2; -. DR MIM; 609541; phenotype. DR MIM; 611729; gene. DR neXtProt; NX_Q9H0B6; -. DR OpenTargets; ENSG00000174996; -. DR PharmGKB; PA142671587; -. DR eggNOG; KOG1840; Eukaryota. DR eggNOG; COG0457; LUCA. DR GeneTree; ENSGT00390000006393; -. DR HOGENOM; HOG000261663; -. DR HOVERGEN; HBG006217; -. DR InParanoid; Q9H0B6; -. DR KO; K10407; -. DR OMA; GPQEPRN; -. DR OrthoDB; EOG091G05DM; -. DR PhylomeDB; Q9H0B6; -. DR TreeFam; TF314010; -. 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 SIGNOR; Q9H0B6; -. DR ChiTaRS; KLC2; human. DR EvolutionaryTrace; Q9H0B6; -. DR GeneWiki; KLC2; -. DR GenomeRNAi; 64837; -. DR PRO; PR:Q9H0B6; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000174996; -. DR CleanEx; HS_KLC2; -. DR ExpressionAtlas; Q9H0B6; baseline and differential. DR Genevisible; Q9H0B6; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005871; C:kinesin complex; ISS:HGNC. DR GO; GO:0016938; C:kinesin I complex; NAS:BHF-UCL. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0019894; F:kinesin binding; ISS:BHF-UCL. DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0007018; P:microtubule-based movement; TAS:Reactome. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR002151; Kinesin_light. DR InterPro; IPR015792; Kinesin_light_repeat. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PRINTS; PR00381; KINESINLIGHT. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF48452; SSF48452; 3. DR PROSITE; PS01160; KINESIN_LIGHT; 2. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome; KW Cytoplasm; Cytoskeleton; Hereditary spastic paraplegia; Microtubule; KW Motor protein; Neurodegeneration; Neuropathy; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; TPR repeat. FT CHAIN 1 622 Kinesin light chain 2. FT /FTId=PRO_0000215095. FT REPEAT 198 231 TPR 1. FT REPEAT 240 273 TPR 2. FT REPEAT 282 315 TPR 3. FT REPEAT 324 357 TPR 4. FT REPEAT 366 399 TPR 5. FT REPEAT 449 482 TPR 6. FT COILED 78 143 {ECO:0000255}. FT MOD_RES 151 151 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 175 175 Phosphoserine. FT {ECO:0000250|UniProtKB:O88448}. FT MOD_RES 179 179 Phosphoserine. FT {ECO:0000250|UniProtKB:O88448}. FT MOD_RES 445 445 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 508 508 Phosphoserine. FT {ECO:0000250|UniProtKB:O88448}. FT MOD_RES 521 521 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 556 556 Phosphoserine. FT {ECO:0000250|UniProtKB:Q5PQM2}. FT MOD_RES 557 557 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9NSK0}. FT MOD_RES 581 581 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 582 582 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 589 589 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 608 608 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 610 610 Phosphoserine. FT {ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 615 615 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT VAR_SEQ 77 153 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043486. FT VARIANT 517 517 P -> S (in dbSNP:rs2276036). FT /FTId=VAR_020379. FT CONFLICT 6 6 F -> Y (in Ref. 2; BAB14302). FT {ECO:0000305}. FT CONFLICT 306 306 K -> R (in Ref. 2; BAB14039). FT {ECO:0000305}. FT HELIX 217 232 {ECO:0000244|PDB:3EDT}. FT STRAND 234 236 {ECO:0000244|PDB:3EDT}. FT HELIX 237 252 {ECO:0000244|PDB:3EDT}. FT HELIX 256 273 {ECO:0000244|PDB:3EDT}. FT HELIX 279 293 {ECO:0000244|PDB:3EDT}. FT TURN 294 296 {ECO:0000244|PDB:3EDT}. FT HELIX 298 316 {ECO:0000244|PDB:3EDT}. FT HELIX 321 335 {ECO:0000244|PDB:3EDT}. FT TURN 336 338 {ECO:0000244|PDB:3EDT}. FT HELIX 340 357 {ECO:0000244|PDB:3EDT}. FT HELIX 363 379 {ECO:0000244|PDB:3EDT}. FT HELIX 382 400 {ECO:0000244|PDB:3EDT}. FT STRAND 401 403 {ECO:0000244|PDB:3EDT}. FT HELIX 411 420 {ECO:0000244|PDB:3EDT}. FT STRAND 427 429 {ECO:0000244|PDB:3CEQ}. FT STRAND 431 433 {ECO:0000244|PDB:3CEQ}. FT HELIX 446 461 {ECO:0000244|PDB:3EDT}. FT HELIX 465 476 {ECO:0000244|PDB:3EDT}. SQ SEQUENCE 622 AA; 68935 MW; 5B57ABE4DF6E396E CRC64; MAMMVFPREE KLSQDEIVLG TKAVIQGLET LRGEHRALLA PLVAPEAGEA EPGSQERCIL LRRSLEAIEL GLGEAQVILA LSSHLGAVES EKQKLRAQVR RLVQENQWLR EELAGTQQKL QRSEQAVAQL EEEKQHLLFM SQIRKLDEDA SPNEEKGDVP KDTLDDLFPN EDEQSPAPSP GGGDVSGQHG GYEIPARLRT LHNLVIQYAS QGRYEVAVPL CKQALEDLEK TSGHDHPDVA TMLNILALVY RDQNKYKEAA HLLNDALAIR EKTLGKDHPA VAATLNNLAV LYGKRGKYKE AEPLCKRALE IREKVLGKFH PDVAKQLSNL ALLCQNQGKA EEVEYYYRRA LEIYATRLGP DDPNVAKTKN NLASCYLKQG KYQDAETLYK EILTRAHEKE FGSVNGDNKP IWMHAEEREE SKDKRRDSAP YGEYGSWYKA CKVDSPTVNT TLRSLGALYR RQGKLEAAHT LEDCASRNRK QGLDPASQTK VVELLKDGSG RRGDRRSSRD MAGGAGPRSE SDLEDVGPTA EWNGDGSGSL RRSGSFGKLR DALRRSSEML VKKLQGGTPQ EPPNPRMKRA SSLNFLNKSV EEPTQPGGTG LSDSRTLSSS SMDLSRRSSL VG //