SDK2_HUMAN
ID SDK2_HUMAN Reviewed; 2172 AA.
AC Q58EX2; A6NMR8; C9JA57; Q86VY3; Q9NTD2; Q9NVB3; Q9P214;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein sidekick-2 {ECO:0000250|UniProtKB:Q6V4S5};
DE Flags: Precursor;
GN Name=SDK2 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:19308};
GN Synonyms=KIAA1514 {ECO:0000303|PubMed:10819331};
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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 324-1921 (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-2172 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 825-2172 (ISOFORM 3).
RC TISSUE=Eye;
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 1032-2172 (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1520-2172 (ISOFORM 1).
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 [6]
RP IDENTIFICATION BY MASS 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 STRUCTURE BY NMR OF 589-687; 885-990 AND 1281-1397.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first, fourth and eighth FN3 domain of sidekick-
RT 2 protein.";
RL Submitted (JUN-2005) to the PDB data bank.
RN [8]
RP VARIANT SER-376.
RX PubMed=28397838; DOI=10.1038/mp.2017.60;
RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA Vincent J.B.;
RT "Mapping autosomal recessive intellectual disability: combined microarray
RT and exome sequencing identifies 26 novel candidate genes in 192
RT consanguineous families.";
RL Mol. Psychiatry 23:973-984(2018).
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. Acts by promoting
CC formation of synapses between two specific retinal cell types: the
CC retinal ganglion cells W3B-RGCs and the excitatory amacrine cells VG3-
CC ACs. Formation of synapses between these two cells plays a key role in
CC detection of motion. Promotes synaptic connectivity via homophilic
CC interactions. {ECO:0000250|UniProtKB:Q6V4S5}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion. Interacts (via PDZ-binding motif) with MAGI1, MAGI2, DLG2,
CC DLG3 and DLG4. {ECO:0000250|UniProtKB:Q6V4S5}.
CC -!- INTERACTION:
CC Q58EX2; Q2NL98: VMAC; NbExp=3; IntAct=EBI-2801316, EBI-2803134;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8AV57};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV57}.
CC Synapse {ECO:0000250|UniProtKB:Q6V4S5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q58EX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58EX2-2; Sequence=VSP_017523, VSP_017524;
CC Name=3;
CC IsoId=Q58EX2-3; Sequence=VSP_017522;
CC Name=4;
CC IsoId=Q58EX2-4; Sequence=VSP_017525;
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 -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91841.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AC032019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB040947; BAA96038.1; -; mRNA.
DR EMBL; BC045763; AAH45763.1; -; mRNA.
DR EMBL; BC066363; AAH66363.1; -; mRNA.
DR EMBL; AL137357; CAB70709.1; -; mRNA.
DR EMBL; AK001694; BAA91841.1; ALT_INIT; mRNA.
DR CCDS; CCDS45769.1; -. [Q58EX2-1]
DR PIR; T46428; T46428.
DR RefSeq; NP_001138424.1; NM_001144952.1. [Q58EX2-1]
DR RefSeq; XP_011523216.1; XM_011524914.2. [Q58EX2-3]
DR PDB; 1WF5; NMR; -; A=580-687.
DR PDB; 1WFN; NMR; -; A=885-990.
DR PDB; 1WFO; NMR; -; A=1281-1397.
DR PDB; 1WIS; NMR; -; A=983-1093.
DR PDBsum; 1WF5; -.
DR PDBsum; 1WFN; -.
DR PDBsum; 1WFO; -.
DR PDBsum; 1WIS; -.
DR AlphaFoldDB; Q58EX2; -.
DR SMR; Q58EX2; -.
DR BioGRID; 120034; 45.
DR IntAct; Q58EX2; 18.
DR STRING; 9606.ENSP00000376421; -.
DR GlyGen; Q58EX2; 7 sites.
DR iPTMnet; Q58EX2; -.
DR PhosphoSitePlus; Q58EX2; -.
DR BioMuta; SDK2; -.
DR DMDM; 296452966; -.
DR EPD; Q58EX2; -.
DR jPOST; Q58EX2; -.
DR MassIVE; Q58EX2; -.
DR MaxQB; Q58EX2; -.
DR PaxDb; Q58EX2; -.
DR PeptideAtlas; Q58EX2; -.
DR PRIDE; Q58EX2; -.
DR ProteomicsDB; 62611; -. [Q58EX2-1]
DR ProteomicsDB; 62612; -. [Q58EX2-2]
DR ProteomicsDB; 62613; -. [Q58EX2-3]
DR ProteomicsDB; 62614; -. [Q58EX2-4]
DR Antibodypedia; 2228; 18 antibodies from 5 providers.
DR DNASU; 54549; -.
DR Ensembl; ENST00000392650.8; ENSP00000376421.3; ENSG00000069188.17. [Q58EX2-1]
DR GeneID; 54549; -.
DR KEGG; hsa:54549; -.
DR MANE-Select; ENST00000392650.8; ENSP00000376421.3; NM_001144952.2; NP_001138424.1.
DR UCSC; uc010dfm.4; human. [Q58EX2-1]
DR CTD; 54549; -.
DR DisGeNET; 54549; -.
DR GeneCards; SDK2; -.
DR HGNC; HGNC:19308; SDK2.
DR HPA; ENSG00000069188; Tissue enhanced (brain, cervix, testis).
DR MIM; 607217; gene.
DR neXtProt; NX_Q58EX2; -.
DR OpenTargets; ENSG00000069188; -.
DR PharmGKB; PA134981456; -.
DR VEuPathDB; HostDB:ENSG00000069188; -.
DR eggNOG; KOG3510; Eukaryota.
DR eggNOG; KOG4221; Eukaryota.
DR GeneTree; ENSGT00940000155761; -.
DR HOGENOM; CLU_001875_1_0_1; -.
DR InParanoid; Q58EX2; -.
DR OMA; CIRANEA; -.
DR OrthoDB; 134749at2759; -.
DR PhylomeDB; Q58EX2; -.
DR TreeFam; TF316846; -.
DR PathwayCommons; Q58EX2; -.
DR Reactome; R-HSA-373756; SDK interactions.
DR SignaLink; Q58EX2; -.
DR BioGRID-ORCS; 54549; 16 hits in 1062 CRISPR screens.
DR ChiTaRS; SDK2; human.
DR EvolutionaryTrace; Q58EX2; -.
DR GeneWiki; SDK2; -.
DR GenomeRNAi; 54549; -.
DR Pharos; Q58EX2; Tdark.
DR PRO; PR:Q58EX2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q58EX2; protein.
DR Bgee; ENSG00000069188; Expressed in cartilage tissue and 176 other tissues.
DR ExpressionAtlas; Q58EX2; baseline and differential.
DR Genevisible; Q58EX2; HS.
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; TAS:Reactome.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
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; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..2172
FT /note="Protein sidekick-2"
FT /id="PRO_0000226978"
FT TOPO_DOM 21..1932
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1933..1953
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1954..2172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..108
FT /note="Ig-like C2-type 1"
FT DOMAIN 113..200
FT /note="Ig-like C2-type 2"
FT DOMAIN 215..294
FT /note="Ig-like C2-type 3"
FT DOMAIN 308..396
FT /note="Ig-like C2-type 4"
FT DOMAIN 402..491
FT /note="Ig-like C2-type 5"
FT DOMAIN 496..585
FT /note="Ig-like C2-type 6"
FT DOMAIN 592..688
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 693..789
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 794..893
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 897..991
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 995..1094
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1099..1197
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1202..1299
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1303..1397
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1402..1499
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1504..1621
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1626..1722
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1726..1821
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1824..1923
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1707..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2039..2067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2098..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2166..2172
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6V4S5"
FT COMPBIAS 1709..1729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2039..2059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2098..2133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2134..2148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 237..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 330..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 423..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 517..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1569..1588
FT /note="SMYSMRNLSRPSLTQYELDN -> Y (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017522"
FT VAR_SEQ 1865..1921
FT /note="DEGLWDILIKDIPKEVSSYTFSMDILKPGVSYDFRVIAVNDYGFGTPSSPSQ
FT SVPAQ -> GAPRPAGLRPHSSLSPFFLGPSTWGTCLCPPPEKALVLLQVKSPGPVEEW
FT ETGLGGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_017523"
FT VAR_SEQ 1922..2172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_017524"
FT VAR_SEQ 2156..2172
FT /note="SLAPGSRAPIAGFSSFV -> KAGVQKEGENRERMCVASSSSALRWWGSLLP
FT WELHGAGEVAVSLLWTRSGPGIWRERGSGG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017525"
FT VARIANT 376
FT /note="G -> S (found in a consanguineous family with
FT intellectual disability; unknown pathological significance;
FT dbSNP:rs372925045)"
FT /evidence="ECO:0000269|PubMed:28397838"
FT /id="VAR_080771"
FT CONFLICT 1218
FT /note="V -> G (in Ref. 4; CAB70709)"
FT /evidence="ECO:0000305"
FT CONFLICT 1382
FT /note="G -> V (in Ref. 4; CAB70709)"
FT /evidence="ECO:0000305"
FT CONFLICT 1553
FT /note="T -> M (in Ref. 3; AAH45763/AAH66363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1680
FT /note="L -> P (in Ref. 5; BAA91841)"
FT /evidence="ECO:0000305"
FT CONFLICT 2092
FT /note="K -> R (in Ref. 5; BAA91841)"
FT /evidence="ECO:0000305"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:1WF5"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:1WF5"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:1WF5"
FT STRAND 622..630
FT /evidence="ECO:0007829|PDB:1WF5"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:1WF5"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:1WF5"
FT STRAND 660..671
FT /evidence="ECO:0007829|PDB:1WF5"
FT STRAND 673..676
FT /evidence="ECO:0007829|PDB:1WF5"
FT STRAND 902..905
FT /evidence="ECO:0007829|PDB:1WFN"
FT STRAND 908..914
FT /evidence="ECO:0007829|PDB:1WFN"
FT STRAND 927..936
FT /evidence="ECO:0007829|PDB:1WFN"
FT HELIX 938..940
FT /evidence="ECO:0007829|PDB:1WFN"
FT STRAND 944..946
FT /evidence="ECO:0007829|PDB:1WFN"
FT STRAND 952..957
FT /evidence="ECO:0007829|PDB:1WFN"
FT STRAND 963..971
FT /evidence="ECO:0007829|PDB:1WFN"
FT STRAND 976..985
FT /evidence="ECO:0007829|PDB:1WFN"
FT STRAND 997..1003
FT /evidence="ECO:0007829|PDB:1WIS"
FT STRAND 1009..1014
FT /evidence="ECO:0007829|PDB:1WIS"
FT STRAND 1024..1030
FT /evidence="ECO:0007829|PDB:1WIS"
FT STRAND 1042..1049
FT /evidence="ECO:0007829|PDB:1WIS"
FT STRAND 1054..1058
FT /evidence="ECO:0007829|PDB:1WIS"
FT STRAND 1065..1067
FT /evidence="ECO:0007829|PDB:1WIS"
FT STRAND 1072..1074
FT /evidence="ECO:0007829|PDB:1WIS"
FT STRAND 1308..1312
FT /evidence="ECO:0007829|PDB:1WFO"
FT STRAND 1314..1320
FT /evidence="ECO:0007829|PDB:1WFO"
FT STRAND 1333..1342
FT /evidence="ECO:0007829|PDB:1WFO"
FT STRAND 1350..1353
FT /evidence="ECO:0007829|PDB:1WFO"
FT STRAND 1359..1364
FT /evidence="ECO:0007829|PDB:1WFO"
FT STRAND 1367..1378
FT /evidence="ECO:0007829|PDB:1WFO"
FT STRAND 1383..1392
FT /evidence="ECO:0007829|PDB:1WFO"
SQ SEQUENCE 2172 AA; 239396 MW; 3CAF9FE659C72A03 CRC64;
MWGLLIWTLL ALHQIRAARA QDDVSPYFKT EPVRTQVHLE GNRLVLTCMA EGSWPLEFKW
LHNNRELTKF SLEYRYMITS LDRTHAGFYR CIVRNRMGAL LQRQTEVQVA YMGSFEEGEK
HQSVSHGEAA VIRAPRIASF PQPQVTWFRD GRKIPPSSRI AITLENTLVI LSTVAPDAGR
YYVQAVNDKN GDNKTSQPIT LTVENVGGPA DPIAPTIIIP PKNTSVVAGT SEVTLECVAN
ARPLIKLHII WKKDGVLLSG GISDHNRRLT IPNPTGSDAG YYECEAVLRS SSVPSVVRGA
YLSVLEPPQF VKEPERHITA EMEKVVDIPC QAKGVPPPSI TWYKDAAVVE VEKLTRFRQR
NDGGLQISGL VPDDTGMFQC FARNAAGEVQ TSTYLAVTSI APNITRGPLD STVIDGMSVV
LACETSGAPR PAITWQKGER ILASGSVQLP RFTPLESGSL LISPTHISDA GTYTCLATNS
RGVDEASADL VVWARTRITK PPQDQSVIKG TQASMVCGVT HDPRVTIRYI WEKDGATLGT
ESHPRIRLDR NGSLHISQTW SGDIGTYTCR VISAGGNDSR SAHLRVRQLP HAPEHPVATL
STVERRAINL TWTKPFDGNS PLIRYILEMS ENNAPWTVLL ASVDPKATSV TVKGLVPARS
YQFRLCAVND VGKGQFSKDT ERVSLPEEPP TAPPQNVIAS GRTNQSIMIQ WQPPPESHQN
GILKGYIIRY CLAGLPVGYQ FKNITDADVN NLLLEDLIIW TNYEIEVAAY NSAGLGVYSS
KVTEWTLQGV PTVPPGNVHA EATNSTTIRF TWNAPSPQFI NGINQGYKLI AWEPEQEEEV
TMVTARPNFQ DSIHVGFVSG LKKFTEYFTS VLCFTTPGDG PRSTPQLVRT HEDVPGPVGH
LSFSEILDTS LKVSWQEPGE KNGILTGYRI SWEEYNRTNT RVTHYLPNVT LEYRVTGLTA
LTTYTIEVAA MTSKGQGQVS ASTISSGVPP ELPGPPTNLG ISNIGPRSVT LQFRPGYDGK
TSISRWLVEA QVGVVGEGEE WLLIHQLSNE PDARSMEVPD LNPFTCYSFR MRQVNIVGTS
PPSQPSRKIQ TLQAPPDMAP ANVSLRTASE TSLWLRWMPL PEMEYNGNPE SVGYKIKYSR
SDGHGKTLSH VVQDRVERDY TIEDLEEWTE YRVQVQAFNA IGSGPWSQTV VGRTRESVPS
SGPTNVSALA TTSSSMLVRW SEVPEADRNG LVLGYKVMYK EKDSDTQPRF WLVEGNSSRS
AQLTGLGKYV LYEVQVLAFT RIGDGSPSHP PILERTLDDV PGPPMGILFP EVRTTSVRLI
WQPPAAPNGI ILAYQITHRL NTTTANTATV EVLAPSARQY TATGLKPESV YLFRITAQTR
KGWGEAAEAL VVTTEKRDRP QPPSRPMVQQ EDVRARSVLL SWEPGSDGLS PVRYYTIQTR
ELPSGRWALH SASVSHNASS FIVDRLKPFT SYKFRVKATN DIGDSEFSEE SESLTTLQAA
PDEAPTILSV TPHTTTSVLI RWQPPAEDKI NGILLGFRIR YRELLYEGLR GFTLRGINNP
GATWAELTSM YSMRNLSRPS LTQYELDNLN KHRRYEIRMS VYNAVGEGPS SPPQEVFVGE
AVPTAAPRNV VVHGATATQL DVTWEPPPLD SQNGDIQGYK IYFWEAQRGN LTERVKTLFL
AENSVKLKNL TGYTAYMVSV AAFNAAGDGP RSTPTQGQTQ QAAPSAPSSV KFSELTTTSV
NVSWEAPQFP NGILEGYRLV YEPCSPVDGV SKIVTVDVKG NSPLWLKVKD LAEGVTYRFR
IRAKTFTYGP EIEANVTTGP GEGAPGPPGV PIIVRYSSAI AIHWSSGDPG KGPITRYVIE
ARPSDEGLWD ILIKDIPKEV SSYTFSMDIL KPGVSYDFRV IAVNDYGFGT PSSPSQSVPA
QKANPFYEEW WFLVVIALVG LIFILLLVFV LIIRGQSKKY AKKTDSGNSA KSGALGHSEM
MSLDESSFPA LELNNRRLSV KNSFCRKNGL YTRSPPRPSP GSLHYSDEDV TKYNDLIPAE
SSSLTEKPSE ISDSQGSDSE YEVDSNHQKA HSFVNHYISD PTYYNSWRRQ QKGISRAQAY
SYTESDSGEP DHTTVTNSTS TQQGSLFRPK ASRTPTPQNP PNPPSQQSTL YRPPSSLAPG
SRAPIAGFSS FV
