ID   Q9VSW5_DROME            Unreviewed;       814 AA.
AC   Q9VSW5;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 201.
DE   SubName: Full=Kinesin-like protein at 67A, isoform A {ECO:0000313|EMBL:AAF50296.1};
DE            EC=5.6.1.3 {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|EMBL:AHN58024.1};
DE   SubName: Full=Kinesin-like protein at 67A, isoform C {ECO:0000313|EMBL:AHN58024.1};
GN   Name=Klp67A {ECO:0000313|EMBL:AAF50296.1,
GN   ECO:0000313|FlyBase:FBgn0004379};
GN   Synonyms=0427/05 {ECO:0000313|EMBL:AAF50296.1}, anon-WO0140519.224
GN   {ECO:0000313|EMBL:AAF50296.1}, anon-WO0172774.120
GN   {ECO:0000313|EMBL:AAF50296.1}, Dmel\CG10923
GN   {ECO:0000313|EMBL:AAF50296.1}, DmKlp67A {ECO:0000313|EMBL:AAF50296.1},
GN   KIF 18A {ECO:0000313|EMBL:AAF50296.1}, KIF18A/B
GN   {ECO:0000313|EMBL:AAF50296.1}, Kin-8 {ECO:0000313|EMBL:AAF50296.1},
GN   KLP3 {ECO:0000313|EMBL:AAF50296.1}, Klp3
GN   {ECO:0000313|EMBL:AAF50296.1}, Klp67 {ECO:0000313|EMBL:AAF50296.1},
GN   klp67 {ECO:0000313|EMBL:AAF50296.1}, KLP67A
GN   {ECO:0000313|EMBL:AAF50296.1}, klp67A {ECO:0000313|EMBL:AAF50296.1},
GN   klp67a {ECO:0000313|EMBL:AAF50296.1}, KRP67A
GN   {ECO:0000313|EMBL:AAF50296.1}, l(3)S042705
GN   {ECO:0000313|EMBL:AAF50296.1};
GN   ORFNames=CG10923 {ECO:0000313|EMBL:AAF50296.1,
GN   ECO:0000313|FlyBase:FBgn0004379}, Dmel_CG10923
GN   {ECO:0000313|EMBL:AAF50296.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA   An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L.,
RA   Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C.,
RA   Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AAF50296.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA   Svirskas R., Rubin G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [9] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
RN   [10] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=26109357; DOI=.1534/g3.115.018929;
RG   FlyBase Consortium;
RA   Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA   Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA   Gelbart W.M., null;
RT   "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT   Throughput Data.";
RL   G3 (Bethesda) 5:1721-1736(2015).
RN   [11] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=26109356; DOI=.1534/g3.115.018937;
RG   FlyBase Consortium;
RA   Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA   Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA   null;
RT   "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL   G3 (Bethesda) 5:1737-1749(2015).
RN   [12] {ECO:0000313|EMBL:AAF50296.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=25589440;
RA   Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA   Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA   Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA   de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA   Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA   Karpen G.H., Celniker S.E.;
RT   "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL   Genome Res. 25:445-458(2015).
RN   [13] {ECO:0000313|EMBL:AAF50296.1}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (DEC-2023) to the EMBL/GenBank/DDBJ databases.
RN   [14] {ECO:0000313|EMBL:AAF50296.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Berkeley Drosophila Genome Project;
RA   Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA   Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA   Rubin G.;
RT   "Drosophila melanogaster release 4 sequence.";
RL   Submitted (AUG-2025) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-8 subfamily.
CC       {ECO:0000256|ARBA:ARBA00060769}.
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; AE014296; AAF50296.1; -; Genomic_DNA.
DR   EMBL; AE014296; AHN58024.1; -; Genomic_DNA.
DR   RefSeq; NP_001286999.1; NM_001300070.1.
DR   RefSeq; NP_523992.2; NM_079268.3.
DR   AlphaFoldDB; Q9VSW5; -.
DR   SMR; Q9VSW5; -.
DR   IntAct; Q9VSW5; 3.
DR   STRING; 7227.FBpp0312148; -.
DR   PaxDb; 7227-FBpp0312148; -.
DR   PeptideAtlas; Q9VSW5; -.
DR   DNASU; 39068; -.
DR   GeneID; 39068; -.
DR   UCSC; CG10923-RA; d. melanogaster.
DR   AGR; FB:FBgn0004379; -.
DR   CTD; 39068; -.
DR   FlyBase; FBgn0004379; Klp67A.
DR   VEuPathDB; VectorBase:FBgn0004379; -.
DR   eggNOG; KOG0242; Eukaryota.
DR   OMA; EQNQRCI; -.
DR   OrthoDB; 3176171at2759; -.
DR   BioGRID-ORCS; 39068; 1 hit in 3 CRISPR screens.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0004379; Expressed in egg cell and 38 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR   GO; GO:0005828; C:kinetochore microtubule; IDA:FlyBase.
DR   GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase.
DR   GO; GO:0072686; C:mitotic spindle; IDA:FlyBase.
DR   GO; GO:0061673; C:mitotic spindle astral microtubule; IBA:GO_Central.
DR   GO; GO:1990023; C:mitotic spindle midzone; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005876; C:spindle microtubule; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IDA:FlyBase.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR   GO; GO:0055047; P:generative cell mitosis; IMP:FlyBase.
DR   GO; GO:0007060; P:male meiosis chromosome segregation; IMP:FlyBase.
DR   GO; GO:0007141; P:male meiosis I; IMP:FlyBase.
DR   GO; GO:0016346; P:male meiotic chromosome movement towards spindle pole; IMP:FlyBase.
DR   GO; GO:0007110; P:meiosis I cytokinesis; IMP:FlyBase.
DR   GO; GO:0007019; P:microtubule depolymerization; IMP:FlyBase.
DR   GO; GO:0007100; P:mitotic centrosome separation; IMP:FlyBase.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR   GO; GO:0031134; P:sister chromatid biorientation; IMP:FlyBase.
DR   GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR   GO; GO:0007054; P:spindle assembly involved in male meiosis I; IMP:FlyBase.
DR   GO; GO:0051231; P:spindle elongation; IMP:FlyBase.
DR   CDD; cd01370; KISc_KIP3_like; 1.
DR   FunFam; 3.40.850.10:FF:000054; Kinesin-like protein; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF65; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 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; PS50067; KINESIN_MOTOR_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Isomerase {ECO:0000313|EMBL:AAF50296.1};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9VSW5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803}.
FT   DOMAIN          8..346
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          616..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          368..395
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        651..662
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..697
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         111..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   814 AA;  92350 MW;  6AD4CF16279C19A5 CRC64;
     MPSEQHTNIK VAVRVRPYNV RELEQKQRSI IKVMDRSALL FDPDEEDDEF FFQGAKQPYR
     DITKRMNKKL TMEFDRVFDI DNSNQDLFEE CTAPLVDAVL NGYNCSVFVY GATGAGKTFT
     MLGSEAHPGL TYLTMQDLFD KIQAQSDVRK FDVGVSYLEV YNEHVMNLLT KSGPLKLRED
     NNGVVVSGLC LTPIYSAEEL LRMLMLGNSH RTQHPTDANA ESSRSHAIFQ VHIRITERKT
     DTKRTVKLSM IDLAGSERAA STKGIGVRFK EGASINKSLL ALGNCINKLA DGLKHIPYRD
     SNLTRILKDS LGGNCRTLMV ANVSMSSLTY EDTYNTLKYA SRAKKIRTTL KQNVLKSKMP
     TEFYVKKIDE VVAENERLKE RNKALEAKAT QLERAGNSGF DPLELKTWYS KIDAVYAAAR
     QLQEHVLGMR SKIKNINYRQ TLKKELEEFR KLMCVDQRVC QEDFRRFANY MSTLTSQMEK
     YKEELPSWLS KMEIAYQDLE SLKREVNKSK AYQILIVYVK YKDLELQLTK QNIFNNHVNA
     INQELVENLD LMRKSFRTAC EVLNQTYDRL EDGQKLTPEI EAVFERLLRK MRFADSEANT
     KMAEMNPLAV PVALRSSAQE EEEPTCSLTA SAKKRQRQAA QSDDDLHLSM EDFDSQDTES
     DSEELHRTFK RPRNLNETQV LGPCSSSSSS STSSSSSARK ALTATVTKPR TVQQRLVSDL
     ISDQNVRGGN EKIKKALLKS NHFTAQGLQR TLAAASLAKE NVKYNANYVR KSPRALMAKA
     LAGTSTLARK PLGSASKEPP LVKFNRAASF RLKK
//