KIF9_HUMAN
ID KIF9_HUMAN Reviewed; 790 AA.
AC Q9HAQ2; Q86Z28; Q9H8A4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Kinesin-like protein KIF9;
GN Name=KIF9;
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] (ISOFORM 2).
RC TISSUE=Testis;
RA Li J.M., Sha J.H., Zhou Z.M.;
RT "Human kinesin protein 9, highly similar to Mus musculus mRNA for kinesin
RT like protein 9.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TRP-638.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-641 (ISOFORM 1), AND VARIANT
RP TRP-638.
RC TISSUE=Thyroid;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-530 AND SER-546, 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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-340 IN COMPLEX WITH ADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the human KIF9 motor domain in complex with ADP.";
RL Submitted (NOV-2006) to the PDB data bank.
CC -!- FUNCTION: Essential for normal male fertility and for progressive
CC motility of spermatozoa. {ECO:0000250|UniProtKB:Q9WV04}.
CC -!- SUBUNIT: Interacts with HYDIN. {ECO:0000250|UniProtKB:Q9WV04}.
CC -!- INTERACTION:
CC Q9HAQ2; K7EM05: ACBD4; NbExp=3; IntAct=EBI-8472129, EBI-16431307;
CC Q9HAQ2; P13196: ALAS1; NbExp=3; IntAct=EBI-8472129, EBI-3905054;
CC Q9HAQ2; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-8472129, EBI-746752;
CC Q9HAQ2; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-8472129, EBI-718459;
CC Q9HAQ2; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-8472129, EBI-2548012;
CC Q9HAQ2; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-8472129, EBI-11977221;
CC Q9HAQ2; O60759: CYTIP; NbExp=3; IntAct=EBI-8472129, EBI-997814;
CC Q9HAQ2; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-8472129, EBI-11988027;
CC Q9HAQ2; P50402: EMD; NbExp=3; IntAct=EBI-8472129, EBI-489887;
CC Q9HAQ2; P51114-2: FXR1; NbExp=3; IntAct=EBI-8472129, EBI-11022345;
CC Q9HAQ2; Q9NYA3: GOLGA6A; NbExp=5; IntAct=EBI-8472129, EBI-11163335;
CC Q9HAQ2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-8472129, EBI-2549423;
CC Q9HAQ2; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-8472129, EBI-10961706;
CC Q9HAQ2; O75031: HSF2BP; NbExp=3; IntAct=EBI-8472129, EBI-7116203;
CC Q9HAQ2; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-8472129, EBI-8638439;
CC Q9HAQ2; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-8472129, EBI-747204;
CC Q9HAQ2; Q96EL1: INKA1; NbExp=3; IntAct=EBI-8472129, EBI-10285157;
CC Q9HAQ2; Q15051-2: IQCB1; NbExp=3; IntAct=EBI-8472129, EBI-11944935;
CC Q9HAQ2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-8472129, EBI-2556193;
CC Q9HAQ2; Q7L273: KCTD9; NbExp=3; IntAct=EBI-8472129, EBI-4397613;
CC Q9HAQ2; O95678: KRT75; NbExp=3; IntAct=EBI-8472129, EBI-2949715;
CC Q9HAQ2; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-8472129, EBI-12012928;
CC Q9HAQ2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-8472129, EBI-1216080;
CC Q9HAQ2; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-8472129, EBI-742610;
CC Q9HAQ2; O15344: MID1; NbExp=3; IntAct=EBI-8472129, EBI-2340316;
CC Q9HAQ2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-8472129, EBI-10172526;
CC Q9HAQ2; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-8472129, EBI-2548751;
CC Q9HAQ2; Q15742: NAB2; NbExp=3; IntAct=EBI-8472129, EBI-8641936;
CC Q9HAQ2; O43482: OIP5; NbExp=3; IntAct=EBI-8472129, EBI-536879;
CC Q9HAQ2; A6NGQ2: OOEP; NbExp=3; IntAct=EBI-8472129, EBI-18583589;
CC Q9HAQ2; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-8472129, EBI-14066006;
CC Q9HAQ2; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-8472129, EBI-10171633;
CC Q9HAQ2; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-8472129, EBI-1105153;
CC Q9HAQ2; Q96MT3: PRICKLE1; NbExp=3; IntAct=EBI-8472129, EBI-2348662;
CC Q9HAQ2; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-8472129, EBI-912440;
CC Q9HAQ2; Q5RL73: RBM48; NbExp=3; IntAct=EBI-8472129, EBI-473821;
CC Q9HAQ2; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-8472129, EBI-12037847;
CC Q9HAQ2; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-8472129, EBI-10269374;
CC Q9HAQ2; Q9H5V9: STEEP1; NbExp=3; IntAct=EBI-8472129, EBI-1053419;
CC Q9HAQ2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-8472129, EBI-1105213;
CC Q9HAQ2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-8472129, EBI-2130429;
CC Q9HAQ2; P08670: VIM; NbExp=3; IntAct=EBI-8472129, EBI-353844;
CC Q9HAQ2; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-8472129, EBI-2799833;
CC Q9HAQ2; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-8472129, EBI-742740;
CC Q9HAQ2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-8472129, EBI-14104088;
CC Q9HAQ2; Q8N3Z6: ZCCHC7; NbExp=3; IntAct=EBI-8472129, EBI-7265024;
CC Q9HAQ2; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-8472129, EBI-740727;
CC Q9HAQ2; Q9C0F3: ZNF436; NbExp=3; IntAct=EBI-8472129, EBI-8489702;
CC Q9HAQ2; Q969W8: ZNF566; NbExp=3; IntAct=EBI-8472129, EBI-2555762;
CC Q9HAQ2; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-8472129, EBI-10172590;
CC Q9HAQ2; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-8472129, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9WV04}.
CC Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000250|UniProtKB:Q9WV04}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9HAQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAQ2-2; Sequence=VSP_002868;
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14713.1; Type=Miscellaneous discrepancy; Note=Dubious isoform. Probable cloning artifact lacking polyadenylation evidence.; Evidence={ECO:0000305};
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DR EMBL; AF311212; AAG33849.1; -; mRNA.
DR EMBL; AC104447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030657; AAH30657.1; -; mRNA.
DR EMBL; AK023894; BAB14713.1; ALT_SEQ; mRNA.
DR CCDS; CCDS2751.1; -. [Q9HAQ2-2]
DR CCDS; CCDS2752.1; -. [Q9HAQ2-1]
DR RefSeq; NP_001128350.1; NM_001134878.1. [Q9HAQ2-1]
DR RefSeq; NP_071737.1; NM_022342.4. [Q9HAQ2-2]
DR RefSeq; NP_878905.2; NM_182902.3. [Q9HAQ2-1]
DR RefSeq; XP_011532306.1; XM_011534004.2. [Q9HAQ2-1]
DR RefSeq; XP_016862518.1; XM_017007029.1. [Q9HAQ2-1]
DR PDB; 3NWN; X-ray; 2.00 A; A=1-340.
DR PDBsum; 3NWN; -.
DR AlphaFoldDB; Q9HAQ2; -.
DR SMR; Q9HAQ2; -.
DR BioGRID; 122086; 71.
DR IntAct; Q9HAQ2; 55.
DR MINT; Q9HAQ2; -.
DR STRING; 9606.ENSP00000333942; -.
DR ChEMBL; CHEMBL2321637; -.
DR iPTMnet; Q9HAQ2; -.
DR PhosphoSitePlus; Q9HAQ2; -.
DR BioMuta; KIF9; -.
DR DMDM; 308153656; -.
DR jPOST; Q9HAQ2; -.
DR MassIVE; Q9HAQ2; -.
DR MaxQB; Q9HAQ2; -.
DR PaxDb; Q9HAQ2; -.
DR PeptideAtlas; Q9HAQ2; -.
DR PRIDE; Q9HAQ2; -.
DR ProteomicsDB; 81418; -. [Q9HAQ2-1]
DR ProteomicsDB; 81419; -. [Q9HAQ2-2]
DR Antibodypedia; 12887; 123 antibodies from 21 providers.
DR DNASU; 64147; -.
DR Ensembl; ENST00000265529.7; ENSP00000265529.3; ENSG00000088727.14. [Q9HAQ2-1]
DR Ensembl; ENST00000444589.6; ENSP00000414987.2; ENSG00000088727.14. [Q9HAQ2-2]
DR Ensembl; ENST00000452770.6; ENSP00000391100.2; ENSG00000088727.14. [Q9HAQ2-1]
DR Ensembl; ENST00000684063.1; ENSP00000507186.1; ENSG00000088727.14. [Q9HAQ2-1]
DR GeneID; 64147; -.
DR KEGG; hsa:64147; -.
DR MANE-Select; ENST00000684063.1; ENSP00000507186.1; NM_182902.4; NP_878905.2.
DR UCSC; uc003cqx.3; human. [Q9HAQ2-1]
DR CTD; 64147; -.
DR DisGeNET; 64147; -.
DR GeneCards; KIF9; -.
DR HGNC; HGNC:16666; KIF9.
DR HPA; ENSG00000088727; Tissue enhanced (testis).
DR MIM; 607910; gene.
DR neXtProt; NX_Q9HAQ2; -.
DR OpenTargets; ENSG00000088727; -.
DR PharmGKB; PA30110; -.
DR VEuPathDB; HostDB:ENSG00000088727; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000158533; -.
DR HOGENOM; CLU_001485_16_2_1; -.
DR InParanoid; Q9HAQ2; -.
DR OMA; AFFQAQK; -.
DR OrthoDB; 424630at2759; -.
DR PhylomeDB; Q9HAQ2; -.
DR TreeFam; TF105229; -.
DR PathwayCommons; Q9HAQ2; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9HAQ2; -.
DR BioGRID-ORCS; 64147; 17 hits in 1084 CRISPR screens.
DR ChiTaRS; KIF9; human.
DR EvolutionaryTrace; Q9HAQ2; -.
DR GenomeRNAi; 64147; -.
DR Pharos; Q9HAQ2; Tbio.
DR PRO; PR:Q9HAQ2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9HAQ2; protein.
DR Bgee; ENSG00000088727; Expressed in bronchial epithelial cell and 180 other tissues.
DR ExpressionAtlas; Q9HAQ2; baseline and differential.
DR Genevisible; Q9HAQ2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0002102; C:podosome; IDA:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1903008; P:organelle disassembly; IMP:UniProtKB.
DR GO; GO:1901317; P:regulation of flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0071801; P:regulation of podosome assembly; IMP:UniProtKB.
DR Gene3D; 3.40.850.10; -; 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; PTHR24115; PTHR24115; 1.
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 3D-structure; Alternative splicing; ATP-binding; Cell projection; Cilium;
KW Coiled coil; Cytoplasm; Cytoskeleton; Flagellum; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..790
FT /note="Kinesin-like protein KIF9"
FT /id="PRO_0000125442"
FT DOMAIN 6..340
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 477..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 342..380
FT /evidence="ECO:0000255"
FT COILED 658..690
FT /evidence="ECO:0000255"
FT COMPBIAS 520..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 530
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 505..569
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_002868"
FT VARIANT 78
FT /note="V -> I (in dbSNP:rs2270569)"
FT /id="VAR_022139"
FT VARIANT 96
FT /note="G -> A (in dbSNP:rs3733092)"
FT /id="VAR_020443"
FT VARIANT 638
FT /note="R -> W (in dbSNP:rs2276853)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_024513"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:3NWN"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 133..145
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3NWN"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 188..209
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 217..227
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:3NWN"
FT STRAND 306..317
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:3NWN"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:3NWN"
SQ SEQUENCE 790 AA; 89986 MW; AD5CCEDFA64FA971 CRC64;
MGTRKKVHAF VRVKPTDDFA HEMIRYGDDK RSIDIHLKKD IRRGVVNNQQ TDWSFKLDGV
LHDASQDLVY ETVAKDVVSQ ALDGYNGTIM CYGQTGAGKT YTMMGATENY KHRGILPRAL
QQVFRMIEER PTHAITVRVS YLEIYNESLF DLLSTLPYVG PSVTPMTIVE NPQGVFIKGL
SVHLTSQEED AFSLLFEGET NRIIASHTMN KNSSRSHCIF TIYLEAHSRT LSEEKYITSK
INLVDLAGSE RLGKSGSEGQ VLKEATYINK SLSFLEQAII ALGDQKRDHI PFRQCKLTHA
LKDSLGGNCN MVLVTNIYGE AAQLEETLSS LRFASRMKLV TTEPAINEKY DAERMVKNLE
KELALLKQEL AIHDSLTNRT FVTYDPMDEI QIAEINSQVR RYLEGTLDEI DIISLRQIKE
VFNQFRVVLS QQEQEVESTL RRKYTLIDRN DFAAISAIQK AGLVDVDGHL VGEPEGQNFG
LGVAPFSTKP GKKAKSKKTF KEPLSSLARK EGASSPVNGK DLDYVSTSKT QLVPSSKDGD
VKDMLSRDRE TSSIEPLPSD SPKEELRPIR PDTPPSKPVA FEEFKNEQGS EINRIFKENK
SILNERRKRA SETTQHINAI KREIDVTKEA LNFQKSLREK QGKYENKGLM IIDEEEFLLI
LKLKDLKKQY RSEYQDLRDL RAEIQYCQHL VDQCRHRLLM EFDIWYNESF VIPEDMQMAL
KPGGSIRPGM VPVNRIVSLG EDDQDKFSQL QQRVLPEGPD SISFYNAKVK IEQKHNYLKT
MMGLQQAHRK
