SFI1_HUMAN
ID SFI1_HUMAN Reviewed; 1242 AA.
AC A8K8P3; A1L373; A1L387; A2A2L2; B1AKL9; B5MDB7; B7Z1V6; B7Z8G3; B7ZBE2;
AC B7ZBE3; O60289; Q2TAN8; Q5W1B5; Q86TK0; Q8N4U8; Q8N8C1; Q8WU14;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein SFI1 homolog;
DE Short=hSFI1;
GN Name=SFI1; Synonyms=KIAA0542;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS HIS-322
RP AND PRO-1087.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 9 AND 10), AND VARIANTS
RP HIS-322; GLN-549 AND PRO-1087.
RC TISSUE=Cerebellum, Testis, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5), AND VARIANTS
RP HIS-322; GLN-549 AND PRO-1087.
RC TISSUE=Brain, Lung, PNS, 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 [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CETN2.
RX PubMed=14504268; DOI=10.1083/jcb.200307064;
RA Kilmartin J.V.;
RT "Sfi1p has conserved centrin-binding sites and an essential function in
RT budding yeast spindle pole body duplication.";
RL J. Cell Biol. 162:1211-1221(2003).
RN [7]
RP FUNCTION, INTERACTION WITH CETN2, AND SUBCELLULAR LOCATION.
RX PubMed=16956364; DOI=10.1111/j.1742-4658.2006.05456.x;
RA Martinez-Sanz J., Yang A., Blouquit Y., Duchambon P., Assairi L.,
RA Craescu C.T.;
RT "Binding of human centrin 2 to the centrosomal protein hSfi1.";
RL FEBS J. 273:4504-4515(2006).
CC -!- FUNCTION: Plays a role in the dynamic structure of centrosome-
CC associated contractile fibers via its interaction with CETN2.
CC {ECO:0000269|PubMed:16956364}.
CC -!- SUBUNIT: Interacts with CETN2 (via C-terminus).
CC {ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:16956364}.
CC -!- INTERACTION:
CC A8K8P3; P41208: CETN2; NbExp=4; IntAct=EBI-743371, EBI-1789926;
CC A8K8P3; P62136: PPP1CA; NbExp=2; IntAct=EBI-743371, EBI-357253;
CC A8K8P3-4; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-10321817, EBI-77889;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:14504268,
CC ECO:0000269|PubMed:16956364}. Note=Localized close to the centriole.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=A8K8P3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8K8P3-2; Sequence=VSP_033702;
CC Name=3;
CC IsoId=A8K8P3-3; Sequence=VSP_033699;
CC Name=4;
CC IsoId=A8K8P3-4; Sequence=VSP_033699, VSP_033701, VSP_033708;
CC Name=5;
CC IsoId=A8K8P3-5; Sequence=VSP_033700, VSP_033703;
CC Name=9;
CC IsoId=A8K8P3-9; Sequence=VSP_033700, VSP_033702;
CC Name=10;
CC IsoId=A8K8P3-10; Sequence=VSP_033699, VSP_038325;
CC -!- DOMAIN: CETN2-binding regions contains a conserved Trp residue in their
CC C-terminal ends, which seems critical for interaction with CETN2.
CC -!- SIMILARITY: Belongs to the SFI1 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-24 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10815.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI29927.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA25468.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB011114; BAA25468.2; ALT_INIT; mRNA.
DR EMBL; AK292408; BAF85097.1; -; mRNA.
DR EMBL; AK293987; BAH11642.1; -; mRNA.
DR EMBL; AK303362; BAH13949.1; -; mRNA.
DR EMBL; AL096701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021576; AAH21576.1; -; mRNA.
DR EMBL; BC110814; AAI10815.1; ALT_INIT; mRNA.
DR EMBL; BC129926; AAI29927.1; ALT_INIT; mRNA.
DR EMBL; BC129945; AAI29946.1; -; mRNA.
DR CCDS; CCDS43004.1; -. [A8K8P3-1]
DR CCDS; CCDS43005.1; -. [A8K8P3-2]
DR CCDS; CCDS58803.1; -. [A8K8P3-9]
DR CCDS; CCDS58804.1; -. [A8K8P3-3]
DR PIR; T00322; T00322.
DR RefSeq; NP_001007468.1; NM_001007467.2. [A8K8P3-1]
DR RefSeq; NP_001245254.1; NM_001258325.1. [A8K8P3-9]
DR RefSeq; NP_001245255.1; NM_001258326.1. [A8K8P3-3]
DR RefSeq; NP_001245256.1; NM_001258327.1. [A8K8P3-10]
DR RefSeq; NP_055590.2; NM_014775.3. [A8K8P3-2]
DR RefSeq; XP_006724453.1; XM_006724390.2. [A8K8P3-3]
DR RefSeq; XP_016884640.1; XM_017029151.1. [A8K8P3-2]
DR RefSeq; XP_016884643.1; XM_017029154.1. [A8K8P3-9]
DR PDB; 2K2I; NMR; -; B=641-660.
DR PDBsum; 2K2I; -.
DR AlphaFoldDB; A8K8P3; -.
DR BMRB; A8K8P3; -.
DR SMR; A8K8P3; -.
DR BioGRID; 115153; 29.
DR CORUM; A8K8P3; -.
DR IntAct; A8K8P3; 17.
DR MINT; A8K8P3; -.
DR STRING; 9606.ENSP00000383145; -.
DR iPTMnet; A8K8P3; -.
DR PhosphoSitePlus; A8K8P3; -.
DR BioMuta; SFI1; -.
DR EPD; A8K8P3; -.
DR MassIVE; A8K8P3; -.
DR MaxQB; A8K8P3; -.
DR PaxDb; A8K8P3; -.
DR PeptideAtlas; A8K8P3; -.
DR PRIDE; A8K8P3; -.
DR ProteomicsDB; 1880; -. [A8K8P3-1]
DR ProteomicsDB; 1881; -. [A8K8P3-10]
DR ProteomicsDB; 1882; -. [A8K8P3-2]
DR ProteomicsDB; 1883; -. [A8K8P3-3]
DR ProteomicsDB; 1884; -. [A8K8P3-4]
DR ProteomicsDB; 1885; -. [A8K8P3-5]
DR ProteomicsDB; 1886; -. [A8K8P3-9]
DR Antibodypedia; 45464; 56 antibodies from 17 providers.
DR DNASU; 9814; -.
DR Ensembl; ENST00000400288.7; ENSP00000383145.2; ENSG00000198089.16. [A8K8P3-1]
DR Ensembl; ENST00000400289.5; ENSP00000383146.1; ENSG00000198089.16. [A8K8P3-3]
DR Ensembl; ENST00000432498.5; ENSP00000402679.1; ENSG00000198089.16. [A8K8P3-2]
DR Ensembl; ENST00000540643.5; ENSP00000443025.1; ENSG00000198089.16. [A8K8P3-9]
DR GeneID; 9814; -.
DR KEGG; hsa:9814; -.
DR MANE-Select; ENST00000400288.7; ENSP00000383145.2; NM_001007467.3; NP_001007468.1.
DR UCSC; uc003ale.5; human. [A8K8P3-1]
DR CTD; 9814; -.
DR DisGeNET; 9814; -.
DR GeneCards; SFI1; -.
DR HGNC; HGNC:29064; SFI1.
DR HPA; ENSG00000198089; Low tissue specificity.
DR MIM; 612765; gene.
DR neXtProt; NX_A8K8P3; -.
DR OpenTargets; ENSG00000198089; -.
DR PharmGKB; PA142670930; -.
DR VEuPathDB; HostDB:ENSG00000198089; -.
DR eggNOG; KOG4775; Eukaryota.
DR GeneTree; ENSGT00940000154110; -.
DR HOGENOM; CLU_007965_0_0_1; -.
DR InParanoid; A8K8P3; -.
DR OMA; QTHFCDW; -.
DR OrthoDB; 941268at2759; -.
DR PhylomeDB; A8K8P3; -.
DR TreeFam; TF328940; -.
DR PathwayCommons; A8K8P3; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; A8K8P3; -.
DR BioGRID-ORCS; 9814; 9 hits in 1083 CRISPR screens.
DR ChiTaRS; SFI1; human.
DR EvolutionaryTrace; A8K8P3; -.
DR GenomeRNAi; 9814; -.
DR Pharos; A8K8P3; Tdark.
DR PRO; PR:A8K8P3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; A8K8P3; protein.
DR Bgee; ENSG00000198089; Expressed in right hemisphere of cerebellum and 155 other tissues.
DR ExpressionAtlas; A8K8P3; baseline and differential.
DR Genevisible; A8K8P3; HS.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR InterPro; IPR030516; SFI1.
DR PANTHER; PTHR22028:SF4; PTHR22028:SF4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..1242
FT /note="Protein SFI1 homolog"
FT /id="PRO_0000334621"
FT REPEAT 138..170
FT /note="HAT 1"
FT REPEAT 172..201
FT /note="HAT 2"
FT REPEAT 270..302
FT /note="HAT 3"
FT REPEAT 334..368
FT /note="HAT 4"
FT REPEAT 399..431
FT /note="HAT 5"
FT REPEAT 1148..1180
FT /note="HAT 6"
FT REGION 111..130
FT /note="Interaction with CETN2"
FT REGION 475..494
FT /note="Interaction with CETN2"
FT REGION 641..660
FT /note="Interaction with CETN2"
FT REGION 1017..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 31..112
FT /note="Missing (in isoform 3, isoform 4 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033699"
FT VAR_SEQ 89..112
FT /note="Missing (in isoform 5 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033700"
FT VAR_SEQ 150..220
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033701"
FT VAR_SEQ 386..416
FT /note="Missing (in isoform 2 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9628581"
FT /id="VSP_033702"
FT VAR_SEQ 678..904
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033703"
FT VAR_SEQ 708..719
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038325"
FT VAR_SEQ 1145..1242
FT /note="GSLDLEAELEEIQQQLLHYQTTKQNLWSCRRQASSLRRWLELNREEPGPEDQ
FT EVEQQVQKELEQVEMQIQLLAEELQAQRQPIGACVARIQALRQALC -> AWTLRLNLR
FT RSSSNYCTTRPPSRTSGPVGGKRAACAGGWS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033708"
FT VARIANT 13
FT /note="H -> L (in dbSNP:rs5749290)"
FT /id="VAR_043439"
FT VARIANT 72
FT /note="R -> H (in dbSNP:rs16989698)"
FT /id="VAR_043440"
FT VARIANT 167
FT /note="Q -> H (in dbSNP:rs7511430)"
FT /id="VAR_043441"
FT VARIANT 322
FT /note="Y -> H (in dbSNP:rs5753700)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9628581"
FT /id="VAR_043442"
FT VARIANT 330
FT /note="W -> R (in dbSNP:rs16989291)"
FT /id="VAR_043443"
FT VARIANT 549
FT /note="R -> Q (in dbSNP:rs2006771)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_043444"
FT VARIANT 760
FT /note="R -> H (in dbSNP:rs9621295)"
FT /id="VAR_062234"
FT VARIANT 1087
FT /note="L -> P (in dbSNP:rs12171042)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9628581"
FT /id="VAR_043445"
FT CONFLICT 353
FT /note="R -> W (in Ref. 5; AAI10815)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="W -> R (in Ref. 5; AAI29927)"
FT /evidence="ECO:0000305"
FT HELIX 651..659
FT /evidence="ECO:0007829|PDB:2K2I"
SQ SEQUENCE 1242 AA; 147664 MW; 7BE570BDD7F72B6E CRC64;
MKNLLTEKCI SSHNFHQKVI KQRMEKKVDS RYFKDGAVKK PYSAKTLSNK KSSASFGIRR
ELPSTSHLVQ YRGTHTCTRQ GRLRELRIRC VARKFLYLWI RMTFGRVFPS KARFYYEQRL
LRKVFEEWKE EWWVFQHEWK LCVRADCHYR YYLYNLMFQT WKTYVRQQQE MRNKYIRAEV
HDAKQKMRQA WKSWLIYVVV RRTKLQMQTT ALEFRQRIIL RVWWSTWRQR LGQVRVSRAL
HASALKHRAL SLQVQAWSQW REQLLYVQKE KQKVVSAVKH HQHWQKRRFL KAWLEYLQVR
RVKRQQNEMA ERFHHVTVLQ IYFCDWQQAW ERRESLYAHH AQVEKLARKM ALRRAFTHWK
HYMLLCAEEA AQFEMAEEHH RHSQLYFCFR ALKDNVTHAH LQQIRRNLAH QQHGVTLLHR
FWNLWRSQIE QKKERELLPL LHAAWDHYRI ALLCKCIELW LQYTQKRRYK QLLQARADGH
FQQRALPAAF HTWNRLWRWR HQENVLSARA TRFHRETLEK QVFSLWRQKM FQHRENRLAE
RMAILHAERQ LLYRSWFMWH QQAAARHQEQ EWQTVACAHH RHGRLKKAFC LWRESAQGLR
TERTGRVRAA EFHMAQLLRW AWSQWRECLA LRGAERQKLM RADLHHQHSV LHRALQAWVT
YQGRVRSILR EVAARESQHN RQLLRGALRR WKENTMARVD EAKKTFQAST HYRRTICSKV
LVQWREAVSV QMYYRQQEDC AIWEAQKVLD RGCLRTWFQR WWDCSRRSAQ QRLQLERAVQ
HHHRQLLLEG LARWKTHHLQ CVRKRLLHRQ STQLLAQRLS RTCFRQWRQQ LAARRQEQRA
TVRALWFWAF SLQAKVWATW LAFVLERRRK KARLQWALQA YQGQLLQEGA TRLLRFAASM
KASRQQLQAQ QQVQAAHSLH RAVRRCATLW KQKVLGRGGK PQPLAAIAPS RKVTFEGPLL
NRIAAGAGDG TLETKRPQAS RPLGALGRLA AEEPHALELN TAHSARKQPR RPHFLLEPAQ
SQRPQKPQEH GLGMAQPAAP SLTRPFLAEA PTALVPHSPL PGALSSAPGP KQPPTASTGP
ELLLLPLSSF MPCGAAAPAR VSAQRATPRD KPPVPSSLAS VPDPHLLLPG DFSATRAGPG
LSTAGSLDLE AELEEIQQQL LHYQTTKQNL WSCRRQASSL RRWLELNREE PGPEDQEVEQ
QVQKELEQVE MQIQLLAEEL QAQRQPIGAC VARIQALRQA LC
