ID SDK1_HUMAN Reviewed; 2213 AA.
AC Q7Z5N4; Q8TEN9; Q8TEP5; Q96N44;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 27-MAR-2024, entry version 167.
DE RecName: Full=Protein sidekick-1 {ECO:0000303|PubMed:15213259};
DE Flags: Precursor;
GN Name=SDK1 {ECO:0000303|PubMed:15213259, ECO:0000312|HGNC:HGNC:19307};
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Bonner T.I.;
RT "Complete coding sequence of human sidekick homolog 1.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 723-2213 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1642-2213 (ISOFORM 1), AND VARIANTS ASN-1016
RP AND ARG-1641.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
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).
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. {ECO:0000250|UniProtKB:Q8AV58}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8AV58};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV58}.
CC Synapse {ECO:0000250|UniProtKB:Q8AV58}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z5N4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z5N4-2; Sequence=VSP_017517, VSP_017519;
CC Name=3;
CC IsoId=Q7Z5N4-3; Sequence=VSP_017518;
CC -!- TISSUE SPECIFICITY: Up-regulated in glomeruli in HIV-associated
CC nephropathy. In diseased glomeruli, significantly overexpressed and the
CC expression is no longer restricted to mesangial cells but includes
CC podocytes and parietal epithelial cells (PubMed:15213259).
CC {ECO:0000269|PubMed:15213259}.
CC -!- DOMAIN: Ig-like C2-type domains 1 and 2 mediate homophilic
CC interactions. {ECO:0000250|UniProtKB:Q3UH53}.
CC -!- MISCELLANEOUS: Dysregulation of this protein may play an important role
CC in podocyte dysfunction in HIV-associated nephropathy.
CC {ECO:0000269|PubMed:15213259}.
CC -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY310398; AAP75619.1; -; mRNA.
DR EMBL; AK055987; BAB71066.1; -; mRNA.
DR EMBL; AC004935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK074077; BAB84903.1; -; mRNA.
DR EMBL; AK074083; BAB84909.1; -; mRNA.
DR CCDS; CCDS34590.1; -. [Q7Z5N4-1]
DR RefSeq; NP_689957.3; NM_152744.3. [Q7Z5N4-1]
DR AlphaFoldDB; Q7Z5N4; -.
DR SMR; Q7Z5N4; -.
DR BioGRID; 128768; 21.
DR IntAct; Q7Z5N4; 6.
DR MINT; Q7Z5N4; -.
DR STRING; 9606.ENSP00000385899; -.
DR CarbonylDB; Q7Z5N4; -.
DR GlyCosmos; Q7Z5N4; 19 sites, No reported glycans.
DR GlyGen; Q7Z5N4; 19 sites.
DR iPTMnet; Q7Z5N4; -.
DR PhosphoSitePlus; Q7Z5N4; -.
DR BioMuta; SDK1; -.
DR DMDM; 296452965; -.
DR jPOST; Q7Z5N4; -.
DR MassIVE; Q7Z5N4; -.
DR PaxDb; 9606-ENSP00000385899; -.
DR PeptideAtlas; Q7Z5N4; -.
DR ProteomicsDB; 69335; -. [Q7Z5N4-1]
DR ProteomicsDB; 69336; -. [Q7Z5N4-2]
DR ProteomicsDB; 69337; -. [Q7Z5N4-3]
DR Pumba; Q7Z5N4; -.
DR Antibodypedia; 2506; 34 antibodies from 17 providers.
DR DNASU; 221935; -.
DR Ensembl; ENST00000404826.7; ENSP00000385899.2; ENSG00000146555.20. [Q7Z5N4-1]
DR GeneID; 221935; -.
DR KEGG; hsa:221935; -.
DR MANE-Select; ENST00000404826.7; ENSP00000385899.2; NM_152744.4; NP_689957.3.
DR UCSC; uc003smx.4; human. [Q7Z5N4-1]
DR AGR; HGNC:19307; -.
DR CTD; 221935; -.
DR DisGeNET; 221935; -.
DR GeneCards; SDK1; -.
DR HGNC; HGNC:19307; SDK1.
DR HPA; ENSG00000146555; Tissue enhanced (pancreas).
DR MIM; 607216; gene.
DR neXtProt; NX_Q7Z5N4; -.
DR OpenTargets; ENSG00000146555; -.
DR PharmGKB; PA134957188; -.
DR VEuPathDB; HostDB:ENSG00000146555; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000157747; -.
DR InParanoid; Q7Z5N4; -.
DR OMA; FMDADQR; -.
DR OrthoDB; 2874985at2759; -.
DR PhylomeDB; Q7Z5N4; -.
DR TreeFam; TF316846; -.
DR PathwayCommons; Q7Z5N4; -.
DR Reactome; R-HSA-373756; SDK interactions.
DR SignaLink; Q7Z5N4; -.
DR BioGRID-ORCS; 221935; 12 hits in 1142 CRISPR screens.
DR ChiTaRS; SDK1; human.
DR GenomeRNAi; 221935; -.
DR Pharos; Q7Z5N4; Tbio.
DR PRO; PR:Q7Z5N4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q7Z5N4; Protein.
DR Bgee; ENSG00000146555; Expressed in popliteal artery and 119 other cell types or tissues.
DR ExpressionAtlas; Q7Z5N4; baseline and differential.
DR Genevisible; Q7Z5N4; HS.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; IEA:Ensembl.
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; IEA:Ensembl.
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 CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR44170:SF30; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00041; fn3; 13.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13927; Ig_3; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00060; FN3; 13.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF49265; Fibronectin type III; 7.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 13.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..2213
FT /note="Protein sidekick-1"
FT /id="PRO_0000226975"
FT TOPO_DOM ?..2009
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2010..2030
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2031..2213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..186
FT /note="Ig-like C2-type 1"
FT DOMAIN 191..277
FT /note="Ig-like C2-type 2"
FT DOMAIN 293..378
FT /note="Ig-like C2-type 3"
FT DOMAIN 386..476
FT /note="Ig-like C2-type 4"
FT DOMAIN 480..569
FT /note="Ig-like C2-type 5"
FT DOMAIN 574..663
FT /note="Ig-like C2-type 6"
FT DOMAIN 670..766
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 771..867
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 872..970
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 974..1068
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1072..1171
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1176..1274
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1279..1376
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1380..1474
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1479..1576
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1581..1699
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1704..1800
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1804..1899
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1902..2000
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2075..2098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2207..2213
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6V4S5"
FT COMPBIAS 25..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 126..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 315..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 408..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 501..553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 595..647
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..1940
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017517"
FT VAR_SEQ 1643..1662
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_017518"
FT VAR_SEQ 1941..1942
FT /note="PS -> ME (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017519"
FT VARIANT 1016
FT /note="D -> N (in dbSNP:rs11978101)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025529"
FT VARIANT 1641
FT /note="H -> R (in dbSNP:rs671694)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025530"
FT CONFLICT 58
FT /note="S -> P (in Ref. 1; AAP75619 and 2; BAB71066)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="R -> H (in Ref. 1; AAP75619 and 2; BAB71066)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="N -> S (in Ref. 1; AAP75619 and 2; BAB71066)"
FT /evidence="ECO:0000305"
FT CONFLICT 1666
FT /note="H -> D (in Ref. 4; BAB84909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2213 AA; 242112 MW; 7475FB659695F2C5 CRC64;
MARGARPSAA GGGGGGAEPP ERAGPGRPRG SPPGRARPSL APRPGPEPSR PRAAPETSGG
DTAGAGRCGG RRAAKLGPGR RGWWALLALQ LHLLRALAQD DVAPYFKTEP GLPQIHLEGN
RLVLTCLAEG SWPLEFKWMR DDSELTTYSS EYKYIIPSLQ KLDAGFYRCV VRNRMGALLQ
RKSEVQVAYM GSFMDTDQRK TVSQGRAAIL NLLPITSYPR PQVTWFREGH KIIPSNRIAI
TLENQLVILA TTTSDAGAYY VQAVNEKNGE NKTSPFIHLS IARDVGTPET MAPTIVVPPG
NRSVVAGSSE TTLECIASAR PVEDLSVTWK RNGVRITSGL HSFGRRLTIS NPTSADTGPY
VCEAALPGSA FEPARATAFL FIIEPPYFTA EPESRISAEV EETVDIGCQA MGVPLPTLQW
YKDAISISRL QNPRYKVLAS GGLRIQKLRP EDSGIFQCFA SNEGGEIQTH TYLDVTNIAP
VFTQRPVDTT VTDGMTAILR CEVSGAPKPA ITWKRENHIL ASGSVRIPRF MLLESGGLQI
APVFIQDAGN YTCYAANTEG SLNASATLTV WNRTSIVHPP EDHVVIKGTT ATLHCGATHD
PRVSLRYVWK KDNVALTPSS TSRIVVEKDG SLLISQTWSG DIGDYSCEIV SEGGNDSRMA
RLEVIELPHS PQNLLVSPNS SHSHAVVLSW VRPFDGNSPI LYYIVELSEN NSPWKVHLSN
VGPEMTGVTV SGLTPARTYQ FRVCAVNEVG RGQYSAETSR LMLPEEPPSA PPKNIVASGR
TNQSIMVQWQ PPPETEHNGV LRGYILRYRL AGLPGEYQQR NITSPEVNYC LVTDLIIWTQ
YEIQVAAYNG AGLGVFSRAV TEYTLQGVPT APPQNVQTEA VNSTTIQFLW NPPPQQFING
INQGYKLLAW PADAPEAVTV VTIAPDFHGV HHGHITNLKK FTAYFTSVLC FTTPGDGPPS
TPQLVWTQED KPGAVGHLSF TEILDTSLKV SWQEPLEKNG IITGYQISWE VYGRNDSRLT
HTLNSTTHEY KIQGLSSLTT YTIDVAAVTA VGTGLVTSST ISSGVPPDLP GAPSNLVISN
ISPRSATLQF RPGYDGKTSI SRWIVEGQVG AIGDEEEWVT LYEEENEPDA QMLEIPNLTP
YTHYRFRMKQ VNIVGPSPYS PSSRVIQTLQ APPDVAPTSV TVRTASETSL RLRWVPLPDS
QYNGNPESVG YRIKYWRSDL QSSAVAQVVS DRLEREFTIE ELEEWMEYEL QMQAFNAVGA
GPWSEVVRGR TRESVPSAAP ENVSAEAVSS TQILLTWTSV PEQDQNGLIL GYKILFRAKD
LDPEPRSHIV RGNHTQSALL AGLRKFVLYE LQVLAFTRIG NGVPSTPLIL ERTKDDAPGP
PVRLVFPEVR LTSVRIVWQP PEEPNGIILG YQIAYRLASS SPHTFTTVEV GATVRQFTAT
DLAPESAYIF RLSAKTRQGW GEPLEATVIT TEKRERPAPP RELLVPQAEV TARSLRLQWV
PGSDGASPIR YFTMQVRELP RGEWQTYSSS ISHEATACVV DRLRPFTSYK LRLKATNDIG
DSDFSSETEA VTTLQDVPGE PPGSVSATPH TTSSVLIQWQ PPRDESLNGL LQGYRIYYRE
LEYEAGSGTE AKTLKNPIAL HAELTAQSSF KTVNSSSTST MCELTHLKKY RRYEVIMTAY
NIIGESPASA PVEVFVGEAA PAMAPQNVQV TPLTASQLEV TWDPPPPESQ NGNIQGYKIY
YWEADSQNET EKMKVLFLPE PVVRLKNLTS HTKYLVSISA FNAAGDGPKS DPQQGRTHQA
APGAPSFLAF SEITSTTLNV SWGEPAAANG ILQGYRVVYE PLAPVQGVSK VVTVEVRGNW
QRWLKVRDLT KGVTYFFRVQ ARTITYGPEL QANITAGPAE GSPGSPRDVL VTKSASELTL
QWTEGHSGDT PTTGYVIEAR PSDEGLWDMF VKDIPRSATS YTLSLDKLRQ GVTYEFRVVA
VNEAGYGEPS NPSTAVSAQV EAPFYEEWWF LLVMALSSLI VILLVVFALV LHGQNKKYKN
CSTGKGISTM EESVTLDNGG FAALELSSRH LNVKSTFSKK NGTRSPPRPS PGGLHYSDED
ICNKYNGAVL TESVSLKEKS ADASESEATD SDYEDALPKH SFVNHYMSDP TYYNSWKRRA
QGRAPAPHRY EAVAGSEAGA QLHPVITTQS AGGVYTPAGP GARTPLTGFS SFV
//
