KIFC1_MOUSE
ID KIFC1_MOUSE Reviewed; 674 AA.
AC Q9QWT9; O08671; O35230; Q497Y3; Q4A1N2; Q6PG90; Q8BV06; Q99L84; Q9JKZ0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Kinesin-like protein KIFC1;
GN Name=Kifc1 {ECO:0000312|MGI:MGI:109596};
GN Synonyms=Kifc4 {ECO:0000303|PubMed:9339368},
GN Kifc5a {ECO:0000303|PubMed:10775188}, Kifc5b {ECO:0000303|PubMed:10775188};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA19676.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC STRAIN=ICR {ECO:0000312|EMBL:BAA19676.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAA19676.1};
RX PubMed=9115736; DOI=10.1016/s0896-6273(00)81243-x;
RA Saito N., Okada Y., Noda Y., Kinoshita Y., Kondo S., Hirokawa N.;
RT "KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor
RT for dendritic transport of multivesicular body-like organelles.";
RL Neuron 18:425-438(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF34646.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10775188; DOI=10.1095/biolreprod62.5.1360;
RA Navolanic P.M., Sperry A.O.;
RT "Identification of isoforms of a mitotic motor in mammalian
RT spermatogenesis.";
RL Biol. Reprod. 62:1360-1369(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAJ19646.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH NUBP1 AND NUBP2,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6 X SJL {ECO:0000312|EMBL:CAJ19646.1};
RC TISSUE=Hippocampus {ECO:0000312|EMBL:CAJ19646.1};
RX PubMed=16638812; DOI=10.1242/jcs.02922;
RA Christodoulou A., Lederer C.W., Surrey T., Vernos I., Santama N.;
RT "Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in
RT the regulation of centrosome duplication.";
RL J. Cell Sci. 119:2035-2047(2006).
RN [4] {ECO:0000312|EMBL:AAC97970.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129 {ECO:0000312|EMBL:AAC97970.1};
RA Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M.,
RA Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.;
RT "Sequence of the mouse major histocompatibility complex class II region.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH57162.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH03753.1}, and
RC NMRI {ECO:0000312|EMBL:AAH57162.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH57162.1}, and
RC Thyroid {ECO:0000312|EMBL:AAI00329.1};
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 [6] {ECO:0000312|EMBL:AAC97970.1}
RP PROTEIN SEQUENCE OF 97-131, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7] {ECO:0000305, ECO:0000312|EMBL:BAC38230.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 387-674.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38230.1};
RC TISSUE=Head {ECO:0000312|EMBL:BAC38230.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAC39966.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 416-570.
RX PubMed=9339368; DOI=10.1006/geno.1997.4901;
RA Yang Z., Hanlon D.W., Marszalek J.R., Goldstein L.S.;
RT "Identification, partial characterization, and genetic mapping of kinesin-
RT like protein genes in mouse.";
RL Genomics 45:123-131(1997).
RN [9] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17360972; DOI=10.1091/mbc.e06-06-0524;
RA Nath S., Bananis E., Sarkar S., Stockert R.J., Sperry A.O., Murray J.W.,
RA Wolkoff A.W.;
RT "Kif5B and Kifc1 interact and are required for motility and fission of
RT early endocytic vesicles in mouse liver.";
RL Mol. Biol. Cell 18:1839-1849(2007).
RN [10]
RP INTERACTION WITH PPP1R42.
RX PubMed=18237440; DOI=10.1186/1471-2121-9-9;
RA Wang R., Sperry A.O.;
RT "Identification of a novel Leucine-rich repeat protein and candidate PP1
RT regulatory subunit expressed in developing spermatids.";
RL BMC Cell Biol. 9:9-9(2008).
RN [11]
RP FUNCTION.
RX PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
RA Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
RA Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
RA Santama N.;
RT "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of
RT ciliogenesis.";
RL Cell. Mol. Life Sci. 71:517-538(2014).
CC -!- FUNCTION: Minus end-directed microtubule-dependent motor required for
CC bipolar spindle formation (PubMed:16638812). May contribute to movement
CC of early endocytic vesicles (PubMed:17360972). Regulates cilium
CC formation and structure (PubMed:23807208).
CC {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972,
CC ECO:0000269|PubMed:23807208}.
CC -!- SUBUNIT: Binds NUBP1 and NUBP2 (PubMed:16638812). Interacts with
CC PPP1R42 (PubMed:18237440). {ECO:0000269|PubMed:16638812,
CC ECO:0000269|PubMed:18237440}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16638812,
CC ECO:0000269|PubMed:17360972, ECO:0000269|PubMed:23807208}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:16638812,
CC ECO:0000269|PubMed:17360972}. Early endosome
CC {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}.
CC Note=Associated with nucleus during interphase, centrosomes in early
CC and spindle in later mitosis. {ECO:0000269|PubMed:16638812,
CC ECO:0000269|PubMed:17360972}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:10775188};
CC IsoId=Q9QWT9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16638812};
CC IsoId=Q9QWT9-2; Sequence=VSP_052526;
CC Name=3 {ECO:0000269|PubMed:9115736};
CC IsoId=Q9QWT9-3; Sequence=VSP_052526, VSP_052527;
CC -!- TISSUE SPECIFICITY: Highly expressed in 14 dpc embryos, spleen and
CC NIH3T3 cells. Also expressed in testis, brain, lung, kidney and
CC cultured astrocytes. Very low levels in skeletal muscle and heart.
CC {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:9115736}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in hippocampus of 13 dpc embryos
CC declining to low levels by 18 dpc and to undetectable levels in
CC juvenile and adult hippocampus. {ECO:0000269|PubMed:16638812}.
CC -!- DISRUPTION PHENOTYPE: Centrosome amplification as well as multipolar
CC spindles. Cells overexpressing Kifc1 show a single microtubule aster
CC and growth arrest in prometaphase. {ECO:0000269|PubMed:16638812}.
CC -!- MISCELLANEOUS: Purified early endocytic vesicles bind minus end-
CC directed Kifc1 as well as plus end-directed Kif5b. Addition of anti-
CC Kifc1 antibodies leads to a decrease in minus end-directed vesicle
CC motility in vitro. {ECO:0000269|PubMed:17360972}.
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=BAA19676.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D49544; BAA19676.1; ALT_FRAME; mRNA.
DR EMBL; AF221102; AAF34646.1; -; mRNA.
DR EMBL; AM051187; CAJ19646.1; -; mRNA.
DR EMBL; AF110520; AAC97970.1; -; Genomic_DNA.
DR EMBL; BC003753; AAH03753.1; -; mRNA.
DR EMBL; BC057162; AAH57162.1; -; mRNA.
DR EMBL; BC100328; AAI00329.1; -; mRNA.
DR EMBL; AK081484; BAC38230.1; -; mRNA.
DR EMBL; AF013117; AAC39966.1; -; mRNA.
DR CCDS; CCDS57065.1; -. [Q9QWT9-1]
DR RefSeq; NP_001182227.1; NM_001195298.1. [Q9QWT9-1]
DR RefSeq; NP_444403.2; NM_053173.2.
DR AlphaFoldDB; Q9QWT9; -.
DR SMR; Q9QWT9; -.
DR BioGRID; 200952; 10.
DR BioGRID; 224976; 50.
DR IntAct; Q9QWT9; 9.
DR STRING; 10090.ENSMUSP00000134572; -.
DR iPTMnet; Q9QWT9; -.
DR PhosphoSitePlus; Q9QWT9; -.
DR EPD; Q9QWT9; -.
DR jPOST; Q9QWT9; -.
DR MaxQB; Q9QWT9; -.
DR PaxDb; Q9QWT9; -.
DR PeptideAtlas; Q9QWT9; -.
DR PRIDE; Q9QWT9; -.
DR ProteomicsDB; 263541; -. [Q9QWT9-1]
DR ProteomicsDB; 263542; -. [Q9QWT9-2]
DR ProteomicsDB; 263543; -. [Q9QWT9-3]
DR DNASU; 16580; -.
DR Ensembl; ENSMUST00000114361; ENSMUSP00000110001; ENSMUSG00000079553. [Q9QWT9-3]
DR Ensembl; ENSMUST00000173492; ENSMUSP00000134572; ENSMUSG00000079553. [Q9QWT9-1]
DR GeneID; 100502766; -.
DR GeneID; 16580; -.
DR KEGG; mmu:100502766; -.
DR KEGG; mmu:16580; -.
DR UCSC; uc008bzw.2; mouse. [Q9QWT9-1]
DR CTD; 16580; -.
DR CTD; 3833; -.
DR MGI; MGI:109596; Kifc1.
DR VEuPathDB; HostDB:ENSMUSG00000079553; -.
DR eggNOG; KOG0239; Eukaryota.
DR GeneTree; ENSGT00940000161735; -.
DR HOGENOM; CLU_001485_12_4_1; -.
DR InParanoid; Q9QWT9; -.
DR OMA; TWTYHDE; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; Q9QWT9; -.
DR TreeFam; TF105237; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 100502766; 4 hits in 73 CRISPR screens.
DR BioGRID-ORCS; 16580; 3 hits in 53 CRISPR screens.
DR ChiTaRS; Kifc1; mouse.
DR PRO; PR:Q9QWT9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QWT9; protein.
DR Bgee; ENSMUSG00000079553; Expressed in bone marrow and 122 other tissues.
DR ExpressionAtlas; Q9QWT9; baseline and differential.
DR Genevisible; Q9QWT9; MM.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR GO; GO:0005871; C:kinesin complex; ISS:MGI.
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; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; ISS:MGI.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0072382; P:minus-end-directed vesicle transport along microtubule; IMP:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:MGI.
DR GO; GO:0047496; P:vesicle transport along microtubule; IGI:MGI.
DR Gene3D; 3.40.850.10; -; 1.
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 Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 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 Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Endosome; Microtubule;
KW Mitosis; Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..674
FT /note="Kinesin-like protein KIFC1"
FT /id="PRO_0000302089"
FT DOMAIN 311..664
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 66..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 146..315
FT /evidence="ECO:0000255"
FT COMPBIAS 69..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 411..418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW19"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW19"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW19"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW19"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16638812,
FT ECO:0000303|PubMed:9115736"
FT /id="VSP_052526"
FT VAR_SEQ 203..222
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9115736"
FT /id="VSP_052527"
FT CONFLICT 101
FT /note="I -> V (in Ref. 1; BAA19676, 2; AAF34646, 3;
FT CAJ19646 and 5; AAH03753/AAH57162/AAI00329)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="V -> A (in Ref. 1; BAA19676, 2; AAF34646, 3;
FT CAJ19646 and 5; AAH03753/AAH57162/AAI00329)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="T -> M (in Ref. 1; BAA19676, 2; AAF34646 and 3;
FT CAJ19646)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="E -> K (in Ref. 1; BAA19676, 2; AAF34646, 3;
FT CAJ19646 and 5; AAH03753)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="V -> L (in Ref. 5; AAH57162)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="F -> L (in Ref. 3; CAJ19646)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="E -> A (in Ref. 1; BAA19676, 2; AAF34646, 3;
FT CAJ19646 and 5; AAH03753/AAI00329)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="P -> L (in Ref. 5; AAI00329)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="E -> A (in Ref. 7; BAC38230)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="P -> L (in Ref. 1; BAA19676)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="A -> V (in Ref. 1; BAA19676)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="D -> G (in Ref. 2; AAF34646)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="H -> P (in Ref. 7; BAC38230)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="S -> R (in Ref. 1; BAA19676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 674 AA; 74153 MW; A99B6FB6F9BC1B03 CRC64;
MDVQAQRPPL LEVKRNVELK AALVKSSSRV PLSASRLKRG PDQMEDALEP AKKRTRVMGA
VTKVDTSRPR GPLLSTVSQT QGHTAAQKGP KKTGPRGCSA IGTVLRSQKP VPAAPAQKPG
TSTAPVVVGK RAGKRPAWDL KGQLCDLNEE LKRYREKTQT LELENRGLRE QLREVQEQAT
TLGTERNTLE GELASVRSRA EQDQQRLETL SARVLELEEC LGTRERLLQE LQGERLQLQE
ERSTLSTQLE EQERRFQATE AALSSSQEEV VCLRQKTEAQ VTLLAEQGDR LYGLEMERRR
LHNQLQELKG NIRVFCRVRP VLEGESTPSP GFLVFPPGPA GPSDPPTGLS LSRSDDRRST
LTGAPAPTVR HDFSFDRVFP PGSKQEEVFE EIAMLVQSAL DGYPVCIFAY GQTGSGKTFT
MEGGPRGDPQ LEGLIPRAMR HLFSVAQEMS GQGWTYSFVA SYVEIYNETV RDLLATGPRK
GQGGECEIRR ASPGSEELTV TNARYVPVSC EKEVEALLHL AHQNRAVAHT AQNKRSSRSH
SVFQLQISGE HAARGLQCGA PLNLVDLAGS ERLDPGLHLG PGERDRLRET QAINSSLSTL
GLVIMALSNK ESHVPYRNSK LTYLLQNSLG GSAKMLMFVN ISPLEENVSE SLNSLRFASK
VNQCVIGTAQ ANKK
