ID   KIFC1_HUMAN             Reviewed;         673 AA.
AC   Q9BW19; O60887; Q14834; Q4KMP0; Q5SU09; Q6GMS7; Q6P4A5; Q9UQP7;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Kinesin-like protein KIFC1;
DE   AltName: Full=Kinesin-like protein 2;
DE   AltName: Full=Kinesin-related protein HSET;
GN   Name=KIFC1; Synonyms=HSET, KNSL2;
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], AND VARIANT GLN-219.
RX   PubMed=10369922; DOI=10.1007/s002510050660;
RA   Janitz K., Wild A., Beck S., Savasta S., Beluffi G., Ziegler A., Volz A.;
RT   "Genomic organization of the HSET locus and the possible association of
RT   HLA-linked genes with immotile cilia syndrome (ICS).";
RL   Immunogenetics 49:644-652(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Kidney, Muscle, and Uterus;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 155-673.
RC   TISSUE=Testis;
RX   PubMed=8276466; DOI=10.1007/bf00241260;
RA   Ando A., Yara-Kikuti Y., Kawata H., Okamoto N., Imai T., Eki T.,
RA   Yokoyama K., Soeda E., Ikemura T., Abe K., Inoko H.;
RT   "Cloning of a new kinesin-related gene located at the centromeric end of
RT   the human MHC region.";
RL   Immunogenetics 39:194-200(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=15843429; DOI=10.1091/mbc.e05-02-0167;
RA   Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B.,
RA   Abraham R.T., Jiang W.;
RT   "Functional analysis of human microtubule-based motor proteins, the
RT   kinesins and dyneins, in mitosis/cytokinesis using RNA interference.";
RL   Mol. Biol. Cell 16:3187-3199(2005).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-26; SER-33 AND
RP   THR-359, AND 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).
CC   -!- FUNCTION: Minus end-directed microtubule-dependent motor required for
CC       bipolar spindle formation (PubMed:15843429). May contribute to movement
CC       of early endocytic vesicles (By similarity). Regulates cilium formation
CC       and structure (By similarity). {ECO:0000250|UniProtKB:Q9QWT9,
CC       ECO:0000269|PubMed:15843429}.
CC   -!- SUBUNIT: Binds NUBP1 and NUBP2. Interacts with PPP1R42 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QWT9}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q9QWT9}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:Q9QWT9}. Early endosome
CC       {ECO:0000250|UniProtKB:Q9QWT9}. Note=Associated with nucleus during
CC       interphase, centrosomes in early and spindle in later mitosis.
CC       {ECO:0000250|UniProtKB:Q9QWT9}.
CC   -!- MISCELLANEOUS: HeLa cells lacking KIFC1 show multipolar mitotic
CC       spindles and a defect in chromosome congression and chromosome
CC       alignment during mitosis.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH00712.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH63567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH73878.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH98438.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA03509.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ010479; CAA09217.1; -; mRNA.
DR   EMBL; AL021366; CAA16157.1; -; Genomic_DNA.
DR   EMBL; AL050332; CAB63782.1; -; Genomic_DNA.
DR   EMBL; AL662799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX088650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX248088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000712; AAH00712.2; ALT_INIT; mRNA.
DR   EMBL; BC063567; AAH63567.1; ALT_INIT; mRNA.
DR   EMBL; BC073878; AAH73878.1; ALT_INIT; mRNA.
DR   EMBL; BC098438; AAH98438.1; ALT_INIT; mRNA.
DR   EMBL; BC121041; AAI21042.1; -; mRNA.
DR   EMBL; BC121042; AAI21043.1; -; mRNA.
DR   EMBL; D14678; BAA03509.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS34430.1; -.
DR   PIR; I54523; I54523.
DR   RefSeq; NP_002254.2; NM_002263.3.
DR   PDB; 5WDH; X-ray; 2.25 A; A=307-663.
DR   PDBsum; 5WDH; -.
DR   AlphaFoldDB; Q9BW19; -.
DR   SMR; Q9BW19; -.
DR   BioGRID; 110031; 86.
DR   IntAct; Q9BW19; 30.
DR   MINT; Q9BW19; -.
DR   STRING; 9606.ENSP00000393963; -.
DR   BindingDB; Q9BW19; -.
DR   ChEMBL; CHEMBL3351200; -.
DR   GlyGen; Q9BW19; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BW19; -.
DR   PhosphoSitePlus; Q9BW19; -.
DR   SwissPalm; Q9BW19; -.
DR   BioMuta; KIFC1; -.
DR   DMDM; 20138710; -.
DR   EPD; Q9BW19; -.
DR   jPOST; Q9BW19; -.
DR   MassIVE; Q9BW19; -.
DR   MaxQB; Q9BW19; -.
DR   PaxDb; 9606-ENSP00000393963; -.
DR   PeptideAtlas; Q9BW19; -.
DR   ProteomicsDB; 79250; -.
DR   Pumba; Q9BW19; -.
DR   Antibodypedia; 29133; 198 antibodies from 30 providers.
DR   DNASU; 3833; -.
DR   Ensembl; ENST00000374523.8; ENSP00000363647.4; ENSG00000204197.9.
DR   Ensembl; ENST00000428849.7; ENSP00000393963.2; ENSG00000237649.8.
DR   Ensembl; ENST00000448818.6; ENSP00000407885.2; ENSG00000233450.7.
DR   GeneID; 3833; -.
DR   KEGG; hsa:3833; -.
DR   MANE-Select; ENST00000428849.7; ENSP00000393963.2; NM_002263.4; NP_002254.2.
DR   UCSC; uc003oef.5; human.
DR   AGR; HGNC:6389; -.
DR   CTD; 3833; -.
DR   DisGeNET; 3833; -.
DR   GeneCards; KIFC1; -.
DR   HGNC; HGNC:6389; KIFC1.
DR   HPA; ENSG00000237649; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 603763; gene.
DR   neXtProt; NX_Q9BW19; -.
DR   OpenTargets; ENSG00000237649; -.
DR   PharmGKB; PA30178; -.
DR   VEuPathDB; HostDB:ENSG00000237649; -.
DR   eggNOG; KOG0239; Eukaryota.
DR   GeneTree; ENSGT00940000161735; -.
DR   HOGENOM; CLU_001485_12_4_1; -.
DR   InParanoid; Q9BW19; -.
DR   OMA; WTYHDEA; -.
DR   OrthoDB; 453489at2759; -.
DR   PhylomeDB; Q9BW19; -.
DR   TreeFam; TF105237; -.
DR   PathwayCommons; Q9BW19; -.
DR   Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-HSA-983189; Kinesins.
DR   SignaLink; Q9BW19; -.
DR   SIGNOR; Q9BW19; -.
DR   BioGRID-ORCS; 3833; 41 hits in 1153 CRISPR screens.
DR   ChiTaRS; KIFC1; human.
DR   EvolutionaryTrace; Q9BW19; -.
DR   GeneWiki; KIFC1; -.
DR   GenomeRNAi; 3833; -.
DR   Pharos; Q9BW19; Tchem.
DR   PRO; PR:Q9BW19; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9BW19; Protein.
DR   Bgee; ENSG00000237649; Expressed in ventricular zone and 103 other cell types or tissues.
DR   ExpressionAtlas; Q9BW19; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; IMP:UniProtKB.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; NAS:UniProtKB.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR   CDD; cd01366; KISc_C_terminal; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
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   PANTHER; PTHR47972:SF45; KINESIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   Genevisible; Q9BW19; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Endosome; Microtubule; Mitosis; Motor protein;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..673
FT                   /note="Kinesin-like protein KIFC1"
FT                   /id="PRO_0000125428"
FT   DOMAIN          310..663
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          23..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          142..306
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        36..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..342
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         410..417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         359
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         219
FT                   /note="R -> Q (in dbSNP:rs61736175)"
FT                   /evidence="ECO:0000269|PubMed:10369922"
FT                   /id="VAR_012650"
FT   CONFLICT        368
FT                   /note="T -> P (in Ref. 3; AAH00712)"
FT                   /evidence="ECO:0000305"
FT   STRAND          311..317
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          331..333
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          347..350
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          371..373
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          375..378
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           384..389
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           392..396
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           397..400
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          404..411
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           416..420
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           428..430
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           433..449
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   TURN            450..452
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          453..465
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          468..471
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          487..489
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          497..499
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           510..526
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           535..537
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          538..554
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          556..565
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           596..607
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           615..617
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           619..624
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           625..627
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   STRAND          633..640
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           644..646
FT                   /evidence="ECO:0007829|PDB:5WDH"
FT   HELIX           647..662
FT                   /evidence="ECO:0007829|PDB:5WDH"
SQ   SEQUENCE   673 AA;  73748 MW;  9E99737665BF1E92 CRC64;
     MDPQRSPLLE VKGNIELKRP LIKAPSQLPL SGSRLKRRPD QMEDGLEPEK KRTRGLGATT
     KITTSHPRVP SLTTVPQTQG QTTAQKVSKK TGPRCSTAIA TGLKNQKPVP AVPVQKSGTS
     GVPPMAGGKK PSKRPAWDLK GQLCDLNAEL KRCRERTQTL DQENQQLQDQ LRDAQQQVKA
     LGTERTTLEG HLAKVQAQAE QGQQELKNLR ACVLELEERL STQEGLVQEL QKKQVELQEE
     RRGLMSQLEE KERRLQTSEA ALSSSQAEVA SLRQETVAQA ALLTEREERL HGLEMERRRL
     HNQLQELKGN IRVFCRVRPV LPGEPTPPPG LLLFPSGPGG PSDPPTRLSL SRSDERRGTL
     SGAPAPPTRH DFSFDRVFPP GSGQDEVFEE IAMLVQSALD GYPVCIFAYG QTGSGKTFTM
     EGGPGGDPQL EGLIPRALRH LFSVAQELSG QGWTYSFVAS YVEIYNETVR DLLATGTRKG
     QGGECEIRRA GPGSEELTVT NARYVPVSCE KEVDALLHLA RQNRAVARTA QNERSSRSHS
     VFQLQISGEH SSRGLQCGAP LSLVDLAGSE RLDPGLALGP GERERLRETQ AINSSLSTLG
     LVIMALSNKE SHVPYRNSKL TYLLQNSLGG SAKMLMFVNI SPLEENVSES LNSLRFASKV
     NQCVIGTAQA NRK
//