SDK2_MOUSE
ID SDK2_MOUSE Reviewed; 2176 AA.
AC Q6V4S5; Q3TTK1; Q5U5W7; Q6ZPP2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein sidekick-2 {ECO:0000303|PubMed:15213259};
DE Flags: Precursor;
GN Name=Sdk2 {ECO:0000303|PubMed:15213259, ECO:0000312|MGI:MGI:2443847};
GN Synonyms=Kiaa1514 {ECO:0000303|PubMed:14621295};
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=FVB/N;
RX PubMed=15213259; DOI=10.1097/01.asn.0000128975.28958.c2;
RA Kaufman L., Hayashi K., Ross M.J., Ross M.D., Klotman P.E.;
RT "Sidekick-1 is upregulated in glomeruli in HIV-associated nephropathy.";
RL J. Am. Soc. Nephrol. 15:1721-1730(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 183-2176 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP SUBUNIT.
RX PubMed=15703275; DOI=10.1096/fj.04-2947fje;
RA Hayashi K., Kaufman L., Ross M.D., Klotman P.E.;
RT "Definition of the critical domains required for homophilic targeting of
RT mouse sidekick molecules.";
RL FASEB J. 19:614-616(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION, PDZ-BINDING MOTIF, DOMAIN, INTERACTION WITH MAGI1;
RP MAGI2; DLG2; DLG3 AND DLG4, AND MUTAGENESIS OF 2174-SER--VAL-2176.
RX PubMed=20219992; DOI=10.1523/jneurosci.6319-09.2010;
RA Yamagata M., Sanes J.R.;
RT "Synaptic localization and function of Sidekick recognition molecules
RT require MAGI scaffolding proteins.";
RL J. Neurosci. 30:3579-3588(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26287463; DOI=10.1038/nature14682;
RA Krishnaswamy A., Yamagata M., Duan X., Hong Y.K., Sanes J.R.;
RT "Sidekick 2 directs formation of a retinal circuit that detects
RT differential motion.";
RL Nature 524:466-470(2015).
CC -!- FUNCTION: Adhesion molecule that promotes lamina-specific synaptic
CC connections in the retina and is specifically required for the
CC formation of neuronal circuits that detect motion (PubMed:26287463).
CC Acts by promoting formation of synapses between two specific retinal
CC cell types: the retinal ganglion cells W3B-RGCs and the excitatory
CC amacrine cells VG3-ACs. Formation of synapses between these two cells
CC plays a key role in detection of motion (PubMed:26287463). Promotes
CC synaptic connectivity via homophilic interactions (PubMed:26287463).
CC {ECO:0000269|PubMed:26287463}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion (PubMed:15703275, PubMed:26287463). Interacts (via PDZ-binding
CC motif) with MAGI1, MAGI2, DLG2, DLG3 and DLG4 (PubMed:20219992).
CC {ECO:0000269|PubMed:15703275, ECO:0000269|PubMed:20219992,
CC ECO:0000269|PubMed:26287463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8AV57};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV57}.
CC Synapse {ECO:0000269|PubMed:20219992, ECO:0000305|PubMed:26287463}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6V4S5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6V4S5-2; Sequence=VSP_017526;
CC Name=3;
CC IsoId=Q6V4S5-3; Sequence=VSP_017527, VSP_017528;
CC -!- TISSUE SPECIFICITY: Expressed in retinal ganglion cells (RGCs) that
CC form synapses in distinct inner plexiform layer (IPL) sublaminae.
CC Specifically expressed in specific subsets of retinal ganglion cells
CC (RGCs), named W3B-RGCs, that specifically respond when the timing of
CC the movement of a small object differs from that of the background, but
CC not when they coincide (at protein level). Also present in excitatory
CC amacrine cell type called VG3-ACs, that provide strong and selective
CC input W3B-RGCs (at protein level) (PubMed:26287463). Expressed at low
CC levels in the glomeruli (PubMed:15213259).
CC {ECO:0000269|PubMed:15213259, ECO:0000269|PubMed:26287463}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in many fetal tissues, inlcuding
CC kidney but shows markedly lower expression in adult organs. Expression
CC in kidney is high throughout development with maximal expression
CC occurring near birth. {ECO:0000269|PubMed:15213259}.
CC -!- DOMAIN: the PDZ-binding motif mediates interaction with PDZ domain-
CC containing proteins MAGI1, MAGI2, DLG2, DLG3 and DLG4 and is required
CC for is required for synaptic localization in photoreceptors.
CC {ECO:0000269|PubMed:20219992}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile but show decreased
CC synaptic connectivity between the retinal ganglion cells W3B-RGCs and
CC the excitatory amacrine cells VG3-ACs. {ECO:0000269|PubMed:26287463}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Discerning change - Issue
CC 176 of February 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/176/";
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DR EMBL; AY351699; AAQ57661.1; -; mRNA.
DR EMBL; AK161326; BAE36324.1; -; mRNA.
DR EMBL; BC038036; AAH38036.1; -; mRNA.
DR EMBL; AK129379; BAC98189.1; -; mRNA.
DR CCDS; CCDS25605.1; -. [Q6V4S5-1]
DR RefSeq; NP_766388.2; NM_172800.2. [Q6V4S5-1]
DR PDB; 5K6X; X-ray; 2.70 A; A/B=22-403.
DR PDB; 5K6Y; X-ray; 3.20 A; A/B=22-403.
DR PDB; 5K6Z; X-ray; 2.70 A; A/B=22-211.
DR PDB; 5K70; X-ray; 2.70 A; A/B/C/D=22-403.
DR PDB; 5XX0; X-ray; 2.40 A; A/B=1-403.
DR PDBsum; 5K6X; -.
DR PDBsum; 5K6Y; -.
DR PDBsum; 5K6Z; -.
DR PDBsum; 5K70; -.
DR PDBsum; 5XX0; -.
DR AlphaFoldDB; Q6V4S5; -.
DR SMR; Q6V4S5; -.
DR BioGRID; 231935; 3.
DR STRING; 10090.ENSMUSP00000038972; -.
DR GlyConnect; 2645; 4 N-Linked glycans (10 sites).
DR GlyGen; Q6V4S5; 14 sites, 4 N-linked glycans (10 sites).
DR iPTMnet; Q6V4S5; -.
DR PhosphoSitePlus; Q6V4S5; -.
DR MaxQB; Q6V4S5; -.
DR PaxDb; Q6V4S5; -.
DR PeptideAtlas; Q6V4S5; -.
DR PRIDE; Q6V4S5; -.
DR ProteomicsDB; 257113; -. [Q6V4S5-1]
DR ProteomicsDB; 257114; -. [Q6V4S5-2]
DR ProteomicsDB; 257115; -. [Q6V4S5-3]
DR Antibodypedia; 2228; 18 antibodies from 5 providers.
DR DNASU; 237979; -.
DR Ensembl; ENSMUST00000041627; ENSMUSP00000038972; ENSMUSG00000041592. [Q6V4S5-1]
DR GeneID; 237979; -.
DR KEGG; mmu:237979; -.
DR UCSC; uc007mfd.1; mouse. [Q6V4S5-2]
DR UCSC; uc007mfe.1; mouse. [Q6V4S5-1]
DR UCSC; uc007mfg.1; mouse. [Q6V4S5-3]
DR CTD; 54549; -.
DR MGI; MGI:2443847; Sdk2.
DR VEuPathDB; HostDB:ENSMUSG00000041592; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155761; -.
DR HOGENOM; CLU_001875_1_0_1; -.
DR InParanoid; Q6V4S5; -.
DR OMA; CIRANEA; -.
DR OrthoDB; 134749at2759; -.
DR PhylomeDB; Q6V4S5; -.
DR TreeFam; TF316846; -.
DR Reactome; R-MMU-373756; SDK interactions.
DR BioGRID-ORCS; 237979; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Sdk2; mouse.
DR PRO; PR:Q6V4S5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6V4S5; protein.
DR Bgee; ENSMUSG00000041592; Expressed in vault of skull and 186 other tissues.
DR ExpressionAtlas; Q6V4S5; baseline and differential.
DR Genevisible; Q6V4S5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR GO; GO:0010842; P:retina layer formation; IMP:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IMP:UniProtKB.
DR CDD; cd00063; FN3; 13.
DR Gene3D; 2.60.40.10; -; 19.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 13.
DR Pfam; PF07679; I-set; 4.
DR SMART; SM00060; FN3; 13.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 7.
DR PROSITE; PS50853; FN3; 13.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..2176
FT /note="Protein sidekick-2"
FT /id="PRO_0000226979"
FT TOPO_DOM 25..1936
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1937..1957
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1958..2176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..112
FT /note="Ig-like C2-type 1"
FT DOMAIN 117..204
FT /note="Ig-like C2-type 2"
FT DOMAIN 219..298
FT /note="Ig-like C2-type 3"
FT DOMAIN 312..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 406..495
FT /note="Ig-like C2-type 5"
FT DOMAIN 500..589
FT /note="Ig-like C2-type 6"
FT DOMAIN 596..692
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 697..793
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 798..897
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 901..995
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 999..1098
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1103..1201
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1206..1303
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1307..1401
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1406..1503
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1508..1625
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1630..1726
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1730..1825
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1828..1930
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1712..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2013..2032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2043..2070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2102..2176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2170..2176
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:20219992"
FT COMPBIAS 1715..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2102..2137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 241..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 334..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 427..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 521..573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..1602
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017526"
FT VAR_SEQ 534..542
FT /note="VWEKDGATL -> SMQSGKGRL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017527"
FT VAR_SEQ 543..2176
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017528"
FT MUTAGEN 2174..2176
FT /note="Missing: Abolishes localization to synapses and
FT induces diffuse expression in photoreceptor cells."
FT /evidence="ECO:0000269|PubMed:20219992"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5K6X"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:5XX0"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5XX0"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:5XX0"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 228..240
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:5XX0"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:5K6Y"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:5XX0"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:5XX0"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5K6X"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 300..316
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:5XX0"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:5K6Y"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5XX0"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 380..388
FT /evidence="ECO:0007829|PDB:5XX0"
FT STRAND 391..402
FT /evidence="ECO:0007829|PDB:5XX0"
SQ SEQUENCE 2176 AA; 239902 MW; CAF12063E0A6EAD3 CRC64;
MFSSMWRLPL WTLLALHRIH SAGAQDDVPP YFKTEPVRTQ VHLEGNRLVL TCMAEGSWPL
EFKWLHNNRE LTRFSLEYRY MITSLDRTHA GFYRCIVRNR MGALLQRQTE VQVAYMGSFE
EGEKRQSVNH GEAAVIRAPR ISSFPRPQVT WFRDGRKIPP SSRIAITLEN TLVILSTVAP
DAGRYYVQAV NDKNGDNKTS QPITLAVENV GGPADPIAPT IIIPPKNTSV VAGTSEVTME
CVANARPLIK LHIVWKKDGA PLSSGISDYN RRLTIANPTV SDAGYYECEA MLRSSSVAPV
TRGAYLSVLE PPQFVREPER HITAEMEKVV DIPCRAKGVP PPSITWYKDA ALVEVGKLTR
FKQRSDGGLQ ISGLLPDDTG MLQCFAHNAA GEAQTSTYLA VTSIAPNITR GPLDSTVIDG
MSVVLACETS GAPRPAITWQ KGERILASGS VQLPRFTLLE SGSLLISPTH ISDAGTYTCL
ATNSRGVDEA SADLVVWART RITKPPQDQS VIKGTQASMV CGVTHDPRVT VRYVWEKDGA
TLAVETNPRI RLDRNGSLHI SQTWSGDIGT YTCRVLSAGG NDSRNAHLRV RQLPHAPEHP
VATLSTVERR AINLTWAKPF DGNSPLMRYV LEMSENNAPW TILLASVDPE ATSVMVKGLV
PARSYQFRLC AVNDVGKGQF SKDTERVSLP EEPPTAPPQN VIASGRTNQS IMIQWQPPPE
SHQNGILKGY IIRYCLAGLP VGYQFKNITD ADVNNLLLED LIIWTNYEIE VAAYNSAGLG
VYSSKVTEWT LQGVPTVPPG NVHAEATNST TIRFTWNAPS PQFINGINQG YKLIAWEPAQ
EEEVTMVTAR PNFQDSIHVG FVSGLKKFTE YFTSVLCFTT PGDGPRSSPQ LVRTHEDVPG
PVGHLSFNDI LDTSLKVSWQ EPGEKNGILT GYRISWEEYN RTNTRVTHYL PNVTLEYRVT
GLTALTTYTI EVAAMTSKGQ GQVSASTISS GVPPELPGAP TNLGISNIGP RSVTLQFRPG
YDGKTSISRW VVEAQVGVIG EGEEWLLIYQ LGNEPDARSM EVPDLNPFTY YSFRMRQVNI
VGTSPPSQPS RKIQTLQAPP DIAPANVTLR TASETSLWLR WMPLPEMEYN GNPESVGYKI
KYGRSDGHGK TLSHTVQDRV EREYTIEDLE EWTEYRVQVQ AFNAIGSGPW SQAVVGRTRE
SVPSSGPTNV SALATTSSSM LVRWSEIPEA DRNGLVLGYK VRYKEKDSDS QPRFWLVEGN
SSRSAQLTGL GKYVLYEVQV LAFTRIGDGS PSHPPILERT LDDVPGPPMG ILFPEVRTTS
VRLIWQPPAA PNGIILAYQI THRLNATTAN TATVEVLAPS ARQYMATGLK PESVYLFRIT
AQTRKGWGEA AEALVVTTEK RDRPQPPSKP VVQQEDVKAR SVLLSWEPGS DGLSPVRYYT
IQTRELPSGR WALHSASVSH NASAFTVDRL KPFTSYKFRV KATNDIGDSE FSEESESLTT
LQAAPDEAPT ILSVTPHTTT SVLIRWQPPS EDKINGILLG FRIRYRELLY DGLRGFTLRG
INNPGAKWAE LTSLYSMRNL TRPSLTQYEL DNLSKHRRYE IRMSIYNAVG EGPLSPPQEV
FVGEAVPTAA PQNVAIHSAT ATQLDVTWEP PPLDNQNGDI QGYKIYFWEV QRRNLTERVK
TLFLAENSVK LKNLTGYTAY MVSVAAFNAA GDGPRSTPTR GQTQQAAPSA PGSVKFSELT
TTSVNVSWDA PQFPNGPLEG YRLVYEPCTP VDGVSKIVTV DVKGNSPLWL KVKDLAEGMT
YRFRIKAKTF TYGPEIEANI TTGPGEGAPG PPGVPIIVRY SSAIAIHWSS GDPGKGPITR
YVIEARPSDE GLWDILIKDI PKEVTSYTFS MDILKPGVSY DFRVIAVNDY GFGTPSSPSQ
SVPAQKASPF YEEWWFLVVI ALVGLIFILL LVFVLIIRGQ SKKYSKKTDS GGNTKSGALG
HGEMLSLDES SFPALELNNR RLSVKNSFCR KNGLYTRSPP RPSPGSLHYS DEDVTKYNDL
IPAESSSLTE KPSEISDSQG SDSEYEVDTN TQKAHSFVNH YISDPTYYNS WRRQQKGISR
AQAYSYTESD SGEPDHVTVP NSNSTQQGSL FRPKASRTPT PQNPPNPQSQ QSTLYRPPSS
LAPGSRAPIA GFSSFV
