SLIK1_HUMAN
ID SLIK1_HUMAN Reviewed; 696 AA.
AC Q96PX8; Q5U5I6; Q96SF9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=SLIT and NTRK-like protein 1;
DE AltName: Full=Leucine-rich repeat-containing protein 12;
DE Flags: Precursor;
GN Name=SLITRK1; Synonyms=KIAA1910, LRRC12; ORFNames=UNQ233/PRO266;
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 {ECO:0000312|EMBL:BAB67803.1};
RN [1] {ECO:0000312|EMBL:BAB67803.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAB67803.1};
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-418.
RC TISSUE=Hippocampus;
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 [5] {ECO:0000305}
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:14557068}, and
RC Brain tumor {ECO:0000269|PubMed:14557068};
RX PubMed=14557068; DOI=10.1016/s0378-1119(03)00715-7;
RA Aruga J., Yokota N., Mikoshiba K.;
RT "Human SLITRK family genes: genomic organization and expression profiling
RT in normal brain and brain tumor tissue.";
RL Gene 315:87-94(2003).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INVOLVEMENT IN TTM.
RX PubMed=16224024; DOI=10.1126/science.1116502;
RA Abelson J.F., Kwan K.Y., O'Roak B.J., Baek D.Y., Stillman A.A.,
RA Morgan T.M., Mathews C.A., Pauls D.L., Rasin M.-R., Gunel M., Davis N.R.,
RA Ercan-Sencicek A.G., Guez D.H., Spertus J.A., Leckman J.F., Dure L.S. IV,
RA Kurlan R., Singer H.S., Gilbert D.L., Farhi A., Louvi A., Lifton R.P.,
RA Sestan N., State M.W.;
RT "Sequence variants in SLITRK1 are associated with Tourette's syndrome.";
RL Science 310:317-320(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, INTERACTION WITH
RP YWHAB; YWHAE; YWHAG; YWHAH; SFN; YWHAQ AND YWHAZ, PHOSPHORYLATION AT
RP SER-695, AND MUTAGENESIS OF SER-695.
RX PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
RA Kajiwara Y., Buxbaum J.D., Grice D.E.;
RT "SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a phosphorylation-
RT dependent manner.";
RL Biol. Psychiatry 66:918-925(2009).
RN [8]
RP FUNCTION, MUTAGENESIS OF VAL-85, CHARACTERIZATION OF VARIANTS ILE-400 AND
RP SER-418, AND CHARACTERIZATION OF VARIANTS TTM LYS-584 AND GLY-593.
RX PubMed=27812321; DOI=10.3389/fnmol.2016.00104;
RA Kang H., Han K.A., Won S.Y., Kim H.M., Lee Y.H., Ko J., Um J.W.;
RT "Slitrk missense mutations associated with neuropsychiatric disorders
RT distinctively impair Slitrk trafficking and synapse formation.";
RL Front. Mol. Neurosci. 9:104-104(2016).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=27273464; DOI=10.1038/srep27343;
RA Beaubien F., Raja R., Kennedy T.E., Fournier A.E., Cloutier J.F.;
RT "Slitrk1 is localized to excitatory synapses and promotes their
RT development.";
RL Sci. Rep. 6:27343-27343(2016).
RN [10]
RP VARIANTS TTM LYS-584 AND GLY-593.
RX PubMed=17003809; DOI=10.1038/sj.mp.4001898;
RA Zuchner S., Cuccaro M.L., Tran-Viet K.N., Cope H., Krishnan R.R.,
RA Pericak-Vance M.A., Wright H.H., Ashley-Koch A.;
RT "SLITRK1 mutations in trichotillomania.";
RL Mol. Psychiatry 11:887-889(2006).
RN [11]
RP VARIANTS ILE-400 AND SER-418.
RX PubMed=23990902; DOI=10.1371/journal.pone.0070376;
RA Ozomaro U., Cai G., Kajiwara Y., Yoon S., Makarov V., Delorme R.,
RA Betancur C., Ruhrmann S., Falkai P., Grabe H.J., Maier W., Wagner M.,
RA Lennertz L., Moessner R., Murphy D.L., Buxbaum J.D., Zuechner S.,
RA Grice D.E.;
RT "Characterization of SLITRK1 variation in obsessive-compulsive disorder.";
RL PLoS ONE 8:E70376-E70376(2013).
CC -!- FUNCTION: It is involved in synaptogenesis and promotes excitatory
CC synapse differentiation (PubMed:27273464, PubMed:27812321). Enhances
CC neuronal dendrite outgrowth (PubMed:16224024, PubMed:19640509).
CC {ECO:0000269|PubMed:16224024, ECO:0000269|PubMed:19640509,
CC ECO:0000269|PubMed:27273464, ECO:0000269|PubMed:27812321}.
CC -!- SUBUNIT: Can form homodimers; homodimerization requires repeat LRR 2
CC (PubMed:27273464). Interacts with YWHAB, YWHAE, YWHAG, YWHAH, SFN,
CC YWHAQ and YWHAZ (PubMed:19640509). {ECO:0000269|PubMed:19640509,
CC ECO:0000269|PubMed:27273464}.
CC -!- INTERACTION:
CC Q96PX8; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-7137880, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:19640509}.
CC Synapse {ECO:0000250|UniProtKB:Q810C1}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the frontal lobe of the
CC cerebral cortex of the brain. Also expressed in some astrocytic brain
CC tumors such as astrocytomas, oligodendrogliomas, glioblastomas,
CC gangliogliomas and primitive neuroectodermal tumors.
CC {ECO:0000269|PubMed:14557068}.
CC -!- DEVELOPMENTAL STAGE: At 20 weeks of gestation, expressed in multiple
CC brain regions, including the developing neo-cortical plate, subplate
CC zone, striatum, globus pallidus, thalamus and subthalamus.
CC {ECO:0000269|PubMed:16224024}.
CC -!- PTM: Undergoes proteolytic cleavage that results in shedding of the
CC ectodomain and cleavage of the C-terminal cytoplasmic tail.
CC Glycosylated. Phosphorylation at Ser-695 is necessary for proper
CC function in promoting neurite outgrowth. {ECO:0000269|PubMed:19640509}.
CC -!- DISEASE: Trichotillomania (TTM) [MIM:613229]: A neuropsychiatric
CC disorder characterized by chronic, repetitive, or compulsive hair
CC pulling resulting in noticeable hair loss. Affected individuals may
CC develop physical complications and often have overlapping psychological
CC disorders, such as Gilles de la Tourette syndrome or obsessive-
CC compulsive disorder. {ECO:0000269|PubMed:16224024,
CC ECO:0000269|PubMed:17003809, ECO:0000269|PubMed:27812321}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the SLITRK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB67803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Out of the ordinary - Issue
CC 187 of January 2017;
CC URL="https://web.expasy.org/spotlight/back_issues/187/";
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DR EMBL; AB067497; BAB67803.1; ALT_INIT; mRNA.
DR EMBL; AY358289; AAQ88656.1; -; mRNA.
DR EMBL; AL355481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051738; AAH51738.1; -; mRNA.
DR CCDS; CCDS9464.1; -.
DR RefSeq; NP_001268432.1; NM_001281503.1.
DR RefSeq; NP_443142.1; NM_052910.2.
DR PDB; 4RCA; X-ray; 2.99 A; B=20-264.
DR PDB; 4RCW; X-ray; 3.19 A; A/B=341-580.
DR PDBsum; 4RCA; -.
DR PDBsum; 4RCW; -.
DR AlphaFoldDB; Q96PX8; -.
DR SMR; Q96PX8; -.
DR BioGRID; 125359; 5.
DR IntAct; Q96PX8; 2.
DR MINT; Q96PX8; -.
DR STRING; 9606.ENSP00000366288; -.
DR iPTMnet; Q96PX8; -.
DR PhosphoSitePlus; Q96PX8; -.
DR BioMuta; SLITRK1; -.
DR DMDM; 46396997; -.
DR jPOST; Q96PX8; -.
DR MassIVE; Q96PX8; -.
DR PaxDb; Q96PX8; -.
DR PeptideAtlas; Q96PX8; -.
DR PRIDE; Q96PX8; -.
DR ProteomicsDB; 77783; -.
DR Antibodypedia; 2648; 268 antibodies from 31 providers.
DR DNASU; 114798; -.
DR Ensembl; ENST00000377084.3; ENSP00000366288.2; ENSG00000178235.8.
DR Ensembl; ENST00000674365.1; ENSP00000501349.1; ENSG00000178235.8.
DR GeneID; 114798; -.
DR KEGG; hsa:114798; -.
DR MANE-Select; ENST00000674365.1; ENSP00000501349.1; NM_001281503.2; NP_001268432.1.
DR UCSC; uc001vlk.4; human.
DR CTD; 114798; -.
DR DisGeNET; 114798; -.
DR GeneCards; SLITRK1; -.
DR HGNC; HGNC:20297; SLITRK1.
DR HPA; ENSG00000178235; Tissue enhanced (brain, retina).
DR MalaCards; SLITRK1; -.
DR MIM; 609678; gene.
DR MIM; 613229; phenotype.
DR neXtProt; NX_Q96PX8; -.
DR OpenTargets; ENSG00000178235; -.
DR Orphanet; 856; NON RARE IN EUROPE: Tourette syndrome.
DR PharmGKB; PA134944423; -.
DR VEuPathDB; HostDB:ENSG00000178235; -.
DR eggNOG; ENOG502QTHH; Eukaryota.
DR GeneTree; ENSGT00940000159810; -.
DR HOGENOM; CLU_012706_2_0_1; -.
DR InParanoid; Q96PX8; -.
DR OMA; ETCDPGP; -.
DR OrthoDB; 217854at2759; -.
DR PhylomeDB; Q96PX8; -.
DR TreeFam; TF351826; -.
DR PathwayCommons; Q96PX8; -.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; Q96PX8; -.
DR BioGRID-ORCS; 114798; 9 hits in 1057 CRISPR screens.
DR GeneWiki; SLITRK1_(gene); -.
DR GenomeRNAi; 114798; -.
DR Pharos; Q96PX8; Tbio.
DR PRO; PR:Q96PX8; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q96PX8; protein.
DR Bgee; ENSG00000178235; Expressed in Brodmann (1909) area 46 and 61 other tissues.
DR Genevisible; Q96PX8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0042592; P:homeostatic process; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IBA:GO_Central.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0007416; P:synapse assembly; IMP:UniProtKB.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR043326; Slitrk.
DR PANTHER; PTHR45773; PTHR45773; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00082; LRRCT; 2.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..696
FT /note="SLIT and NTRK-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000032673"
FT TOPO_DOM 18..622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..57
FT /note="LRRNT 1"
FT REPEAT 59..80
FT /note="LRR 1"
FT REPEAT 83..104
FT /note="LRR 2"
FT REPEAT 106..128
FT /note="LRR 3"
FT REPEAT 131..152
FT /note="LRR 4"
FT REPEAT 155..176
FT /note="LRR 5"
FT REPEAT 178..199
FT /note="LRR 6"
FT DOMAIN 212..263
FT /note="LRRCT 1"
FT DOMAIN 332..373
FT /note="LRRNT 2"
FT REPEAT 376..397
FT /note="LRR 7"
FT REPEAT 400..421
FT /note="LRR 8"
FT REPEAT 424..445
FT /note="LRR 9"
FT REPEAT 448..469
FT /note="LRR 10"
FT REPEAT 472..493
FT /note="LRR 11"
FT REPEAT 495..516
FT /note="LRR 12"
FT DOMAIN 529..580
FT /note="LRRCT 2"
FT REGION 265..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 695
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19640509"
FT VARIANT 400
FT /note="N -> I (probable disease-associated variant found in
FT a patient with obsessive-compulsive disorder; decreased
FT levels of mature protein; decreased localization to the
FT cell membrane surface expression; decreased function in
FT synaptogenesis)"
FT /evidence="ECO:0000269|PubMed:23990902,
FT ECO:0000269|PubMed:27812321"
FT /id="VAR_077626"
FT VARIANT 418
FT /note="T -> S (probable disease-associated variant found in
FT a patient with obsessive-compulsive disorder; decreased
FT levels of mature protein; decreased localization to the
FT cell membrane surface expression; decreased function in
FT synaptogenesis; dbSNP:rs150504822)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:23990902, ECO:0000269|PubMed:27812321"
FT /id="VAR_077627"
FT VARIANT 552
FT /note="L -> M (in dbSNP:rs7491932)"
FT /id="VAR_027755"
FT VARIANT 584
FT /note="R -> K (in TTM; unknown pathological significance;
FT does not affect synaptogenesis; dbSNP:rs1035448844)"
FT /evidence="ECO:0000269|PubMed:17003809,
FT ECO:0000269|PubMed:27812321"
FT /id="VAR_077628"
FT VARIANT 593
FT /note="S -> G (in TTM; unknown pathological significance;
FT does not affect synaptogenesis; dbSNP:rs1368546312)"
FT /evidence="ECO:0000269|PubMed:17003809,
FT ECO:0000269|PubMed:27812321"
FT /id="VAR_077629"
FT MUTAGEN 85
FT /note="V->M: Does not affect surface expression."
FT /evidence="ECO:0000269|PubMed:27812321"
FT MUTAGEN 695
FT /note="S->A: Loss of phosphorylation. Not able to promote
FT neurite outgrowth."
FT /evidence="ECO:0000269|PubMed:19640509"
FT MUTAGEN 695
FT /note="S->E: Able to promote neurite outgrowth as the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:19640509"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4RCA"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4RCA"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4RCA"
FT TURN 99..104
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4RCA"
FT TURN 123..128
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4RCA"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4RCA"
FT TURN 171..176
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4RCA"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4RCA"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4RCA"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:4RCA"
FT TURN 245..249
FT /evidence="ECO:0007829|PDB:4RCA"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4RCA"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:4RCW"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:4RCW"
FT TURN 416..421
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:4RCW"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:4RCW"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:4RCW"
FT HELIX 511..515
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4RCW"
FT TURN 535..537
FT /evidence="ECO:0007829|PDB:4RCW"
FT HELIX 538..545
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:4RCW"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:4RCW"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:4RCW"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:4RCW"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:4RCW"
SQ SEQUENCE 696 AA; 77735 MW; E0E9ACEDE0F0ACEC CRC64;
MLLWILLLET SLCFAAGNVT GDVCKEKICS CNEIEGDLHV DCEKKGFTSL QRFTAPTSQF
YHLFLHGNSL TRLFPNEFAN FYNAVSLHME NNGLHEIVPG AFLGLQLVKR LHINNNKIKS
FRKQTFLGLD DLEYLQADFN LLRDIDPGAF QDLNKLEVLI LNDNLISTLP ANVFQYVPIT
HLDLRGNRLK TLPYEEVLEQ IPGIAEILLE DNPWDCTCDL LSLKEWLENI PKNALIGRVV
CEAPTRLQGK DLNETTEQDL CPLKNRVDSS LPAPPAQEET FAPGPLPTPF KTNGQEDHAT
PGSAPNGGTK IPGNWQIKIR PTAAIATGSS RNKPLANSLP CPGGCSCDHI PGSGLKMNCN
NRNVSSLADL KPKLSNVQEL FLRDNKIHSI RKSHFVDYKN LILLDLGNNN IATVENNTFK
NLLDLRWLYM DSNYLDTLSR EKFAGLQNLE YLNVEYNAIQ LILPGTFNAM PKLRILILNN
NLLRSLPVDV FAGVSLSKLS LHNNYFMYLP VAGVLDQLTS IIQIDLHGNP WECSCTIVPF
KQWAERLGSE VLMSDLKCET PVNFFRKDFM LLSNDEICPQ LYARISPTLT SHSKNSTGLA
ETGTHSNSYL DTSRVSISVL VPGLLLVFVT SAFTVVGMLV FILRNRKRSK RRDANSSASE
INSLQTVCDS SYWHNGPYNA DGAHRVYDCG SHSLSD
