KIF1C_HUMAN
ID KIF1C_HUMAN Reviewed; 1103 AA.
AC O43896; D3DTL6; O75186; Q5U618;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Kinesin-like protein KIF1C;
GN Name=KIF1C; Synonyms=KIAA0706;
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], FUNCTION, PHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=9685376; DOI=10.1074/jbc.273.32.20267;
RA Dorner C., Ciossek T., Mueller S., Moeller N.P.H., Ullrich A., Lammers R.;
RT "Characterization of KIF1C, a new kinesin-like protein involved in vesicle
RT transport from the Golgi apparatus to the endoplasmic reticulum.";
RL J. Biol. Chem. 273:20267-20275(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, AND IDENTIFICATION BY
RP 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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1083 AND SER-1092, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-676, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-494 AND SER-915, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, AND IDENTIFICATION BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1041, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [15]
RP INTERACTION WITH BICD2, AND INVOLVEMENT IN SPAX2.
RX PubMed=24482476; DOI=10.1126/science.1247363;
RA Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
RA Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A.,
RA Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M.,
RA Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G.,
RA Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S.,
RA Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M.,
RA Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J.,
RA Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A.,
RA Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T.,
RA Gleeson J.G.;
RT "Exome sequencing links corticospinal motor neuron disease to common
RT neurodegenerative disorders.";
RL Science 343:506-511(2014).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 498-599.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the FHA domain of human kinesin family member C.";
RL Submitted (FEB-2006) to the PDB data bank.
RN [17]
RP VARIANT SPAX2 TRP-169.
RX PubMed=24319291; DOI=10.1136/jmedgenet-2013-102012;
RA Dor T., Cinnamon Y., Raymond L., Shaag A., Bouslam N., Bouhouche A.,
RA Gaussen M., Meyer V., Durr A., Brice A., Benomar A., Stevanin G.,
RA Schuelke M., Edvardson S.;
RT "KIF1C mutations in two families with hereditary spastic paraparesis and
RT cerebellar dysfunction.";
RL J. Med. Genet. 51:137-142(2014).
CC -!- FUNCTION: Motor required for the retrograde transport of Golgi vesicles
CC to the endoplasmic reticulum. Has a microtubule plus end-directed
CC motility. {ECO:0000269|PubMed:9685376}.
CC -!- SUBUNIT: Monomer. Interacts with BICD2. {ECO:0000269|PubMed:24482476,
CC ECO:0000305}.
CC -!- INTERACTION:
CC O43896; A0JNT9: Bicdl1; Xeno; NbExp=3; IntAct=EBI-1644048, EBI-7893170;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, with most
CC abundant expression in heart and skeletal muscle.
CC {ECO:0000269|PubMed:9685376}.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:9685376}.
CC -!- DISEASE: Spastic ataxia 2, autosomal recessive (SPAX2) [MIM:611302]: A
CC neurologic disorder characterized by cerebellar ataxia, dysarthria, and
CC variable spasticity of the lower limbs. Cognition is not affected.
CC {ECO:0000269|PubMed:24319291, ECO:0000269|PubMed:24482476}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31681.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U91329; AAC52117.1; -; mRNA.
DR EMBL; AB014606; BAA31681.2; ALT_INIT; mRNA.
DR EMBL; CH471108; EAW90366.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90367.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90368.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90369.1; -; Genomic_DNA.
DR EMBL; BC034993; AAH34993.1; -; mRNA.
DR CCDS; CCDS11065.1; -.
DR RefSeq; NP_006603.2; NM_006612.5.
DR RefSeq; XP_005256481.1; XM_005256424.2.
DR PDB; 2G1L; X-ray; 2.60 A; A=498-599.
DR PDBsum; 2G1L; -.
DR AlphaFoldDB; O43896; -.
DR SMR; O43896; -.
DR BioGRID; 115972; 136.
DR DIP; DIP-40376N; -.
DR IntAct; O43896; 42.
DR MINT; O43896; -.
DR STRING; 9606.ENSP00000320821; -.
DR iPTMnet; O43896; -.
DR MetOSite; O43896; -.
DR PhosphoSitePlus; O43896; -.
DR BioMuta; KIF1C; -.
DR EPD; O43896; -.
DR jPOST; O43896; -.
DR MassIVE; O43896; -.
DR MaxQB; O43896; -.
DR PaxDb; O43896; -.
DR PeptideAtlas; O43896; -.
DR PRIDE; O43896; -.
DR ProteomicsDB; 49220; -.
DR Antibodypedia; 11469; 156 antibodies from 29 providers.
DR DNASU; 10749; -.
DR Ensembl; ENST00000320785.10; ENSP00000320821.5; ENSG00000129250.12.
DR GeneID; 10749; -.
DR KEGG; hsa:10749; -.
DR MANE-Select; ENST00000320785.10; ENSP00000320821.5; NM_006612.6; NP_006603.2.
DR UCSC; uc002gan.3; human.
DR CTD; 10749; -.
DR DisGeNET; 10749; -.
DR GeneCards; KIF1C; -.
DR HGNC; HGNC:6317; KIF1C.
DR HPA; ENSG00000129250; Group enriched (brain, choroid plexus, heart muscle, skeletal muscle, tongue).
DR MalaCards; KIF1C; -.
DR MIM; 603060; gene.
DR MIM; 611302; phenotype.
DR neXtProt; NX_O43896; -.
DR OpenTargets; ENSG00000129250; -.
DR Orphanet; 397946; Autosomal spastic paraplegia type 58.
DR PharmGKB; PA30100; -.
DR VEuPathDB; HostDB:ENSG00000129250; -.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000159295; -.
DR HOGENOM; CLU_009645_0_0_1; -.
DR InParanoid; O43896; -.
DR OMA; GGFHYNQ; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; O43896; -.
DR TreeFam; TF105221; -.
DR PathwayCommons; O43896; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; O43896; -.
DR SIGNOR; O43896; -.
DR BioGRID-ORCS; 10749; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; KIF1C; human.
DR EvolutionaryTrace; O43896; -.
DR GeneWiki; KIF1C; -.
DR GenomeRNAi; 10749; -.
DR Pharos; O43896; Tbio.
DR PRO; PR:O43896; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43896; protein.
DR Bgee; ENSG00000129250; Expressed in C1 segment of cervical spinal cord and 203 other tissues.
DR ExpressionAtlas; O43896; baseline and differential.
DR Genevisible; O43896; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:ProtInc.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISS:ARUK-UCL.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISS:ARUK-UCL.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Methylation; Microtubule; Motor protein;
KW Neurodegeneration; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1103
FT /note="Kinesin-like protein KIF1C"
FT /id="PRO_0000125410"
FT DOMAIN 5..348
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 523..590
FT /note="FHA"
FT REGION 400..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..388
FT /evidence="ECO:0000255"
FT COILED 438..479
FT /evidence="ECO:0000255"
FT COILED 633..674
FT /evidence="ECO:0000255"
FT COILED 828..872
FT /evidence="ECO:0000255"
FT COMPBIAS 415..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1020
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1083
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1041
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1083
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VARIANT 169
FT /note="R -> W (in SPAX2; dbSNP:rs587777198)"
FT /evidence="ECO:0000269|PubMed:24319291"
FT /id="VAR_070937"
FT CONFLICT 669
FT /note="R -> Q (in Ref. 1; AAC52117)"
FT /evidence="ECO:0000305"
FT CONFLICT 955..962
FT /note="SGGRGGGL -> LWGPGRGV (in Ref. 1; AAC52117)"
FT /evidence="ECO:0000305"
FT CONFLICT 976..977
FT /note="KL -> NV (in Ref. 1; AAC52117)"
FT /evidence="ECO:0000305"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 520..529
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 541..550
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 556..562
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:2G1L"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:2G1L"
FT STRAND 593..598
FT /evidence="ECO:0007829|PDB:2G1L"
SQ SEQUENCE 1103 AA; 122947 MW; 5FDEEB8C91B3C46B CRC64;
MAGASVKVAV RVRPFNARET SQDAKCVVSM QGNTTSIINP KQSKDAPKSF TFDYSYWSHT
STEDPQFASQ QQVYRDIGEE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGR QEPGQQGIVP
QLCEDLFSRV SENQSAQLSY SVEVSYMEIY CERVRDLLNP KSRGSLRVRE HPILGPYVQD
LSKLAVTSYA DIADLMDCGN KARTVAATNM NETSSRSHAV FTIVFTQRCH DQLTGLDSEK
VSKISLVDLA GSERADSSGA RGMRLKEGAN INKSLTTLGK VISALADMQS KKRKSDFIPY
RDSVLTWLLK ENLGGNSRTA MIAALSPADI NYEETLSTLR YADRTKQIRC NAIINEDPNA
RLIRELQEEV ARLRELLMAQ GLSASALEGL KTEEGSVRGA LPAVSSPPAP VSPSSPTTHN
GELEPSFSPN TESQIGPEEA MERLQETEKI IAELNETWEE KLRKTEALRM EREALLAEMG
VAVREDGGTV GVFSPKKTPH LVNLNEDPLM SECLLYHIKD GVTRVGQVDM DIKLTGQFIR
EQHCLFRSIP QPDGEVVVTL EPCEGAETYV NGKLVTEPLV LKSGNRIVMG KNHVFRFNHP
EQARLERERG VPPPPGPPSE PVDWNFAQKE LLEQQGIDIK LEMEKRLQDL ENQYRKEKEE
ADLLLEQQRL YADSDSGDDS DKRSCEESWR LISSLREQLP PTTVQTIVKR CGLPSSGKRR
APRRVYQIPQ RRRLQGKDPR WATMADLKMQ AVKEICYEVA LADFRHGRAE IEALAALKMR
ELCRTYGKPD GPGDAWRAVA RDVWDTVGEE EGGGAGSGGG SEEGARGAEV EDLRAHIDKL
TGILQEVKLQ NSSKDRELQA LRDRMLRMER VIPLAQDHED ENEEGGEVPW APPEGSEAAE
EAAPSDRMPS ARPPSPPLSS WERVSRLMEE DPAFRRGRLR WLKQEQLRLQ GLQGSGGRGG
GLRRPPARFV PPHDCKLRFP FKSNPQHRES WPGMGSGEAP TPLQPPEEVT PHPATPARRP
PSPRRSHHPR RNSLDGGGRS RGAGSAQPEP QHFQPKKHNS YPQPPQPYPA QRPPGPRYPP
YTTPPRMRRQ RSAPDLKESG AAV
