SDK1_MOUSE
ID SDK1_MOUSE Reviewed; 2193 AA.
AC Q3UH53; Q3UFD1; Q6PAL2; Q6V3A4; Q8BMC2; Q8BZI1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein sidekick-1 {ECO:0000303|PubMed:15213259};
DE Flags: Precursor;
GN Name=Sdk1 {ECO:0000303|PubMed:15213259, ECO:0000312|MGI:MGI:2444413};
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] (ISOFORMS 1 AND 2), AND 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 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Sympathetic ganglion, Urinary bladder, and Wolffian duct;
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] OF 35-2193 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 SUBUNIT (ISOFORM 1 AND ISOFORM 2), DOMAIN, AND MUTAGENESIS OF
RP 227-GLN--ALA-232.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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 [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MAGI1; MAGI2; DLG2; DLG3 AND
RP DLG4.
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 [7]
RP TISSUE SPECIFICITY.
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. Expressed in specific subsets of
CC interneurons and retinal ganglion cells (RGCs) and promotes synaptic
CC connectivity via homophilic interactions.
CC {ECO:0000250|UniProtKB:Q8AV58}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion (PubMed:15703275). Interacts (via PDZ-binding motif) with
CC MAGI1, MAGI2, DLG2, DLG3 and DLG4 (PubMed:20219992).
CC {ECO:0000269|PubMed:15703275, ECO:0000269|PubMed:20219992}.
CC -!- SUBUNIT: [Isoform 2]: Does not mediate homophilic interactions
CC (PubMed:15703275). {ECO:0000269|PubMed:15703275}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8AV58};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV58}.
CC Synapse {ECO:0000269|PubMed:20219992}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UH53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UH53-2; Sequence=VSP_017520, VSP_017521;
CC -!- TISSUE SPECIFICITY: Expressed by non-overlapping subsets of retinal
CC neurons. Sdk1 and Sdk2 are expressed in non-overlapping subsets of
CC interneurons and retinal ganglion cells (RGCs) that form synapses in
CC distinct inner plexiform layer (IPL) sublaminae (at protein level).
CC {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:0000250|UniProtKB:Q6V4S5}.
CC -!- DOMAIN: Ig-like C2-type domains 1 and 2 mediate homophilic
CC interactions. {ECO:0000269|PubMed:15703275}.
CC -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC28986.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY353236; AAQ57662.1; -; mRNA.
DR EMBL; AK032883; BAC28069.1; ALT_INIT; mRNA.
DR EMBL; AK035225; BAC28986.1; ALT_INIT; mRNA.
DR EMBL; AK147578; BAE28004.1; -; mRNA.
DR EMBL; AK148648; BAE28630.1; -; mRNA.
DR EMBL; BC060237; AAH60237.1; -; mRNA.
DR CCDS; CCDS39360.2; -. [Q3UH53-1]
DR RefSeq; NP_808547.3; NM_177879.5. [Q3UH53-1]
DR PDB; 5K6U; X-ray; 2.20 A; A=78-459.
DR PDB; 5K6V; X-ray; 3.21 A; A=78-459.
DR PDB; 5K6W; X-ray; 3.50 A; A/B=78-556.
DR PDB; 5K6Z; X-ray; 2.70 A; A/B=268-459.
DR PDB; 5XWX; X-ray; 1.55 A; A/B=1-458.
DR PDBsum; 5K6U; -.
DR PDBsum; 5K6V; -.
DR PDBsum; 5K6W; -.
DR PDBsum; 5K6Z; -.
DR PDBsum; 5XWX; -.
DR AlphaFoldDB; Q3UH53; -.
DR SMR; Q3UH53; -.
DR BioGRID; 236924; 1.
DR STRING; 10090.ENSMUSP00000082928; -.
DR GlyConnect; 2644; 1 N-Linked glycan (2 sites).
DR GlyGen; Q3UH53; 17 sites, 1 N-linked glycan (2 sites).
DR iPTMnet; Q3UH53; -.
DR PhosphoSitePlus; Q3UH53; -.
DR jPOST; Q3UH53; -.
DR PaxDb; Q3UH53; -.
DR PeptideAtlas; Q3UH53; -.
DR PRIDE; Q3UH53; -.
DR ProteomicsDB; 257111; -. [Q3UH53-1]
DR ProteomicsDB; 257112; -. [Q3UH53-2]
DR Antibodypedia; 2506; 32 antibodies from 16 providers.
DR DNASU; 330222; -.
DR Ensembl; ENSMUST00000074546; ENSMUSP00000074133; ENSMUSG00000039683. [Q3UH53-2]
DR Ensembl; ENSMUST00000085774; ENSMUSP00000082928; ENSMUSG00000039683. [Q3UH53-1]
DR GeneID; 330222; -.
DR KEGG; mmu:330222; -.
DR UCSC; uc009ail.2; mouse. [Q3UH53-1]
DR UCSC; uc009ain.2; mouse. [Q3UH53-2]
DR CTD; 221935; -.
DR MGI; MGI:2444413; Sdk1.
DR VEuPathDB; HostDB:ENSMUSG00000039683; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000157747; -.
DR HOGENOM; CLU_001875_1_0_1; -.
DR InParanoid; Q3UH53; -.
DR OMA; NWKRNGV; -.
DR OrthoDB; 134749at2759; -.
DR PhylomeDB; Q3UH53; -.
DR TreeFam; TF316846; -.
DR Reactome; R-MMU-373756; SDK interactions.
DR BioGRID-ORCS; 330222; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Sdk1; mouse.
DR PRO; PR:Q3UH53; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3UH53; protein.
DR Bgee; ENSMUSG00000039683; Expressed in otolith organ and 113 other tissues.
DR Genevisible; Q3UH53; 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; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0048148; P:behavioral response to cocaine; IDA:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; IDA:MGI.
DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISS: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; 3.
DR SMART; SM00060; FN3; 13.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 7.
DR PROSITE; PS50853; FN3; 13.
DR PROSITE; PS50835; IG_LIKE; 5.
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..?
FT /evidence="ECO:0000255"
FT CHAIN ?..2193
FT /note="Protein sidekick-1"
FT /id="PRO_0000226976"
FT TOPO_DOM ?..1991
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1992..2012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2013..2193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 86..168
FT /note="Ig-like C2-type 1"
FT DOMAIN 173..259
FT /note="Ig-like C2-type 2"
FT DOMAIN 275..363
FT /note="Ig-like C2-type 3"
FT DOMAIN 368..458
FT /note="Ig-like C2-type 4"
FT DOMAIN 462..551
FT /note="Ig-like C2-type 5"
FT DOMAIN 556..645
FT /note="Ig-like C2-type 6"
FT DOMAIN 652..748
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 753..849
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 854..952
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 956..1050
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1054..1153
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1158..1256
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1261..1358
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1362..1456
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1461..1558
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1563..1681
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1686..1782
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1786..1881
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1884..1982
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2057..2080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2187..2193
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6V4S5"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 997
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 297..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 390..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 483..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 577..629
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..260
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15213259"
FT /id="VSP_017520"
FT VAR_SEQ 261..265
FT /note="LSVAR -> MDRSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15213259"
FT /id="VSP_017521"
FT MUTAGEN 227..232
FT /note="Missing: Abolishes homophilic interactions."
FT /evidence="ECO:0000269|PubMed:15703275"
FT CONFLICT 1009
FT /note="M -> T (in Ref. 1; AAQ57662)"
FT /evidence="ECO:0000305"
FT CONFLICT 1888
FT /note="P -> L (in Ref. 2; BAE28630)"
FT /evidence="ECO:0000305"
FT CONFLICT 1957
FT /note="E -> G (in Ref. 2; BAC28986)"
FT /evidence="ECO:0000305"
FT CONFLICT 2038
FT /note="L -> Q (in Ref. 2; BAE28630)"
FT /evidence="ECO:0000305"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5K6U"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5K6V"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:5XWX"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5XWX"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:5XWX"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5K6U"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:5XWX"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:5XWX"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:5XWX"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 356..372
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:5XWX"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:5XWX"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 436..444
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 447..458
FT /evidence="ECO:0007829|PDB:5XWX"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 484..489
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:5K6W"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:5K6W"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 531..538
FT /evidence="ECO:0007829|PDB:5K6W"
FT STRAND 543..553
FT /evidence="ECO:0007829|PDB:5K6W"
SQ SEQUENCE 2193 AA; 240306 MW; C22752D48DC4B137 CRC64;
MARARPSVAG GGVAAPPERA GPGRPRRSRT GHHCDPECPG LRAAPRTPGP GAGRRAAKLR
PGRGWWALLL LQLHLLRALA QDDVAPYFKT EPGLPQIHLE GNRLVLTCLA EGSWPLEFKW
IRNDSELTTY SSEYKYIIPS LQKLDAGFYR CVVRNRMGAL LQRKSEIQVA YMGNFMDTDQ
RKTVSQGHAA LLNLLPIVSC PQPQVTWFRE GHKIIPSSRI AITLENQLVI LATTASDAGA
YYVQAVNEKN GENKTSPFIH LSVARDTGTH EAMAPIIVVA PGNRSVVAGS SETTLECIAN
ARPVEELSVH WKRNGVRLTS GLHSYGRRLT ITNPTSADTG MYVCEATLRG STFEPARARA
FLSIIEPPYF TAEPESRILG EVEETMDIPC RAMGVPLPTL QWYKDAVPLS KLQNPRYKVL
PSGGLHIQKL SPEDSGIFQC FASNEGGEVQ THTYLDVTNI APAFTQRPVD TTVTDGMTAV
LRCEVSGAPK PAITWKRGNH ILASGSVRIP RFMLLESGGL RIAPVFIQDA GNYTCYAANT
EASVNASAML TVWNRTSIVH PPEDRVVIKG TTATLCCGAT HDPRTSLRYV WKKDNVVITA
SSSSRIVVEK DGSLVISQTW SGDIGDYTCE IISEGGSDSR TARLEVIELP HPPQNLLASL
SPARSHSVTL SWVRPFDGNS PVLYYIVQVS ENNSPWKVHL SNVGPEMTGV TVSGLTPART
YQFRVCAVNQ VGKGQYSTET SRLMLPEEPP SAPPKNIVAS GRTNQSIMVQ WQPPPETEHN
GVLRGYILRY RLAGLPGEHQ QRNISSPEVN YCLVTDLIIW TQYEIQVAAY NGAGLGVFSR
AVTEYTLQGV PTAPPQNVQA EAVNSTTVHF LWNPPPQQFI NGINQGYKLL AWPADAPETV
TVVTIAPDFH GIHHGYITNL KKFTAYFTSV LCFTTPGDGP PSSPQLVWTH EDKPGAVGHL
SFTEILDTSL KVSWQEPLER NGIIMGYQIS WEVYGRNDSR LTHTLNSTMH EYKIQGLSSL
TTYTIDVAAL TAAGVGVTTS STISSGVPPD LPGAPSNLVI SNISPRSATL QFRPGYDGKT
AICRWIVEGQ VGAIGDEEEW VTLYEEENEP DAQMLEIPNL TPYTHYRFRM RQVNIVGPSP
FSQSSRVIQT LQAPPDVAPT SLTVRTASET SLRLRWVPLP DSQYNGNPES VGYRVKYWRS
DQPSSALAQV VSDRLERELT IEELEEWTEY ELRMQAFNAI GAGPWSELVR GRTRESVPSA
APENVSAEAV SSTQILLTWA SVPEQDQNGL ILGYKVLYCA KDLDPEPRSH VVRGNHTQSA
LLAGLRKFVV YELQVLAFTR IGNGVPSSPL ILERTKDDTP GPPVRLVFPE VRLTAVRIVW
QPPEEPNGVI LGYQIAYRLA SGSPHTFTTV EVGATVRQFT ATELAPESAY IFRLSAKTRQ
GWGEPLEATV ITTEKRERPA PPRELLVPQA EVTARSLRLQ WVPGSDGASP IRYFTVQVRE
LPGGEWQTYS SSISHEATAC AVERLRPFTS YKLRLKATND IGDSDFSAET EAVTTLQDVP
GEPPGSVSAT PHTTSSVLIQ WQPPRDESLN GLLQGYRIYY RELESETGMS PEPKTLKSPS
ALRAELTAQS SFKTVNSSSS LTTYELTHLK KYRRYEVIMT AYNIIGESPA SVPVEVFVGE
AAPAMAPQNV QVTPLTASQL EVTWDPPPPE SQNGNIQGYK VYYWEADSRN ETEKMKVLFL
PEPVVKIKDL TSHTKYLISI SAFNAAGDGP KSDPCQGRTH QAAPGPPSFL AFSEITSTTL
NVSWGEPSAA NGILQGYRVV YEPLAPVQGV SKVVTVDVKG NWQRWLKVRD LTKGVTYFFR
VQARTIAYGP ELQANVTAGP AEGSPGSPRN VLVTKSASEL TLQWTEGNAG TTPTTGYVIE
ARPSDEGLWD MFAKDIPRSA TSYTVDLDKL RQGVTYEFRV VAVNKAGFGE PSRPSIAVSA
QAEAPFYEEW WFLLVMALSS LLLILLVVFV LVLHGQSKKY KSCSTGKGIS NMEETVTLDN
GGFAALELNS RHLNVKSTFS KKNGTRSPPR PSPGGLHYSD EDICNKYNGA VLTESVNLKE
KSVDGSESEA SDSDYEEALP KHSFVNHYMS DPTYYNSWKR RPPAAAPHRY EAVAGAEAGP
HLHTVITTQS AGGVYTPAGP GARAPLTGFS SFV
