SLAI2_HUMAN
ID SLAI2_HUMAN Reviewed; 581 AA.
AC Q9P270; A8K4P1; Q8N5R3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=SLAIN motif-containing protein 2;
GN Name=SLAIN2; Synonyms=KIAA1458;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 180-581.
RC TISSUE=Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-48 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-48; SER-63; SER-147;
RP SER-179; SER-247; SER-250; SER-251; SER-254; SER-323; SER-377; SER-413;
RP SER-456; SER-462 AND SER-467, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-462 AND SER-467, AND
RP IDENTIFICATION BY 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-63; SER-134; SER-147;
RP SER-179; SER-247; SER-315; SER-323; SER-377; SER-391; SER-433; SER-456;
RP SER-462 AND SER-467, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-63 AND SER-391, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-551, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 574-581 IN COMPLEX WITH CLIP1,
RP FUNCTION, CIRCULAR DICHROISM, COILED-COIL DOMAIN, INTERACTION WITH CLIP1;
RP CLIP2; CLASP1; CKAP5; MAPRE1 AND MAPRE3, PHOSPHORYLATION, MUTAGENESIS OF
RP TYR-581, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M.,
RA Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O.,
RA Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC microtubule dynamics and microtubule organization. Promotes cytoplasmic
CC microtubule nucleation and elongation. Required for normal structure of
CC the microtubule cytoskeleton during interphase.
CC {ECO:0000269|PubMed:21646404}.
CC -!- SUBUNIT: Interacts with CLIP1, CLIP2, CKAP5, CLASP1, MAPRE1 and MAPRE3.
CC {ECO:0000269|PubMed:21646404}.
CC -!- INTERACTION:
CC Q9P270; Q14008: CKAP5; NbExp=4; IntAct=EBI-3959887, EBI-310585;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes with
CC microtubules. Detected at the plus end of growing microtubules.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in adult
CC liver, testis and ovary, and lowest levels in adult pancreas and spleen
CC and in fetal brain. {ECO:0000269|PubMed:10819331}.
CC -!- DOMAIN: The N-terminus forms a two-stranded coiled coil.
CC -!- PTM: Is highly phosphorylated during mitosis, but not during
CC interphase. The highly phosphorylated form does not localize at
CC microtubule plus ends and does not interact with MAPRE1 or CKAP5.
CC {ECO:0000269|PubMed:21646404}.
CC -!- SIMILARITY: Belongs to the SLAIN motif-containing family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31691.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA95982.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB040891; BAA95982.1; ALT_INIT; mRNA.
DR EMBL; AK291006; BAF83695.1; -; mRNA.
DR EMBL; BC031691; AAH31691.2; ALT_INIT; mRNA.
DR CCDS; CCDS47051.1; -.
DR RefSeq; NP_065897.1; NM_020846.1.
DR PDB; 3RDV; X-ray; 1.75 A; E/F/G/H=574-581.
DR PDBsum; 3RDV; -.
DR AlphaFoldDB; Q9P270; -.
DR SMR; Q9P270; -.
DR BioGRID; 121654; 114.
DR ELM; Q9P270; -.
DR IntAct; Q9P270; 62.
DR MINT; Q9P270; -.
DR STRING; 9606.ENSP00000264313; -.
DR GlyGen; Q9P270; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P270; -.
DR PhosphoSitePlus; Q9P270; -.
DR BioMuta; SLAIN2; -.
DR DMDM; 166977679; -.
DR EPD; Q9P270; -.
DR jPOST; Q9P270; -.
DR MassIVE; Q9P270; -.
DR MaxQB; Q9P270; -.
DR PaxDb; Q9P270; -.
DR PeptideAtlas; Q9P270; -.
DR PRIDE; Q9P270; -.
DR ProteomicsDB; 83740; -.
DR Antibodypedia; 23807; 110 antibodies from 26 providers.
DR DNASU; 57606; -.
DR Ensembl; ENST00000264313.11; ENSP00000264313.5; ENSG00000109171.15.
DR GeneID; 57606; -.
DR KEGG; hsa:57606; -.
DR MANE-Select; ENST00000264313.11; ENSP00000264313.5; NM_020846.2; NP_065897.1.
DR UCSC; uc003gya.5; human.
DR CTD; 57606; -.
DR DisGeNET; 57606; -.
DR GeneCards; SLAIN2; -.
DR HGNC; HGNC:29282; SLAIN2.
DR HPA; ENSG00000109171; Low tissue specificity.
DR MIM; 610492; gene.
DR neXtProt; NX_Q9P270; -.
DR OpenTargets; ENSG00000109171; -.
DR PharmGKB; PA162403457; -.
DR VEuPathDB; HostDB:ENSG00000109171; -.
DR eggNOG; ENOG502QSZP; Eukaryota.
DR GeneTree; ENSGT00390000017860; -.
DR HOGENOM; CLU_027278_2_0_1; -.
DR InParanoid; Q9P270; -.
DR OMA; PTDLQTN; -.
DR OrthoDB; 616171at2759; -.
DR PhylomeDB; Q9P270; -.
DR TreeFam; TF331616; -.
DR PathwayCommons; Q9P270; -.
DR SignaLink; Q9P270; -.
DR BioGRID-ORCS; 57606; 29 hits in 1075 CRISPR screens.
DR ChiTaRS; SLAIN2; human.
DR GenomeRNAi; 57606; -.
DR Pharos; Q9P270; Tbio.
DR PRO; PR:Q9P270; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9P270; protein.
DR Bgee; ENSG00000109171; Expressed in tibialis anterior and 190 other tissues.
DR ExpressionAtlas; Q9P270; baseline and differential.
DR Genevisible; Q9P270; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR InterPro; IPR026179; Slain.
DR PANTHER; PTHR22406; PTHR22406; 1.
DR Pfam; PF15301; SLAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..581
FT /note="SLAIN motif-containing protein 2"
FT /id="PRO_0000316965"
FT REGION 26..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..39
FT /evidence="ECO:0000269|PubMed:21646404"
FT COMPBIAS 108..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 581
FT /note="Important for interaction with CLIP1"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI08"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 538
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI08"
FT MOD_RES 551
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MUTAGEN 581
FT /note="Missing: Abolishes interaction with CLIP1."
FT /evidence="ECO:0000269|PubMed:21646404"
FT CONFLICT 233
FT /note="N -> D (in Ref. 2; BAF83695)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="V -> A (in Ref. 2; BAF83695)"
FT /evidence="ECO:0000305"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:3RDV"
SQ SEQUENCE 581 AA; 62543 MW; 44B10B1BBD555B26 CRC64;
MEDVNSNVNA DQEVRKLQEL VKKLEKQNEQ LRSRSGAVQG AGSLGPGSPV RAGASIPSSG
AASPRGFPLG LSAKSGGGPG SGPRRTSSEE LRDATSLLAA GEGGLLDEVE PLRPDELERL
SGWEEEEESW LYSSPKKKLT PMQKSVSPLV WCRQVLDYPS PDVECAKKSL IHKLDQTMSA
LKRQNLYNNP FNSMSYTSPY SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNLKSS
DRNPPLSPQS SIDSELSASE LDEDSIGSNY KLNDVTDVQI LARMQEESLR QEYAATTSRR
SSGSSCNSTR RGTFSDQELD AQSLDDEDDN MHHAVYPAVN RFSPSPRNSP RPSPKQSPRN
SPRSRSPARG IEYSRVSPQP MISRLQQPRL SLQGHPTDLQ TSNVKNEEKL RRSLPNLSRT
SNTQVDSVKS SRSDSNFQVP NGGIPRMQPQ ASAIPSPGKF RSPAAPSPLA LRQPVKAFSN
HGSGSPGSQE ITQLTQTTSS PGPPMVQSTV SANPPSNINS ATLTRPAGTT AMRSGLPRPS
APSAGGIPVP RSKLAQPVRR SLPAPKTYGS MKDDSWKDGC Y
