SPRL1_HUMAN
ID SPRL1_HUMAN Reviewed; 664 AA.
AC Q14515; B4E2Z0; E7ESU2; Q14800;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=SPARC-like protein 1;
DE AltName: Full=High endothelial venule protein;
DE Short=Hevin;
DE AltName: Full=MAST 9;
DE Flags: Precursor;
GN Name=SPARCL1;
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), AND VARIANTS ASP-49 AND ASP-106.
RC TISSUE=Tonsil;
RX PubMed=7600298; DOI=10.1016/1074-7613(95)90083-7;
RA Girard J.-P., Springer T.A.;
RT "Cloning from purified high endothelial venule cells of hevin, a close
RT relative of the antiadhesive extracellular matrix protein SPARC.";
RL Immunity 2:113-123(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RA Schraml P., Shipman R., Ludwig C.U.;
RT "An alternative PCR-based method for the direct isolation of cDNA ends
RT (DICE).";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-412.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-398, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [7]
RP GLYCOSYLATION AT THR-31; THR-40; SER-44; THR-116 AND THR-398, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
CC -!- INTERACTION:
CC Q14515; Q99972: MYOC; NbExp=2; IntAct=EBI-2682673, EBI-11692272;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14515-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14515-2; Sequence=VSP_056678;
CC -!- TISSUE SPECIFICITY: Highly expressed in lymph node, brain, heart, lung,
CC skeletal muscle, ovary, small intestine, and colon, with lower levels
CC in placenta, pancreas, testis, spleen, and thymus, and no expression in
CC kidney, liver, and peripheral blood leukocytes.
CC -!- PTM: N- and O-glycosylated. O-glycosylated with a core 1 or possibly
CC core 8 glycan. {ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23234360}.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; X82157; CAA57650.1; -; mRNA.
DR EMBL; X86693; CAA60386.1; -; mRNA.
DR EMBL; AK304494; BAG65302.1; -; mRNA.
DR EMBL; AC093906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS3622.1; -. [Q14515-1]
DR CCDS; CCDS77939.1; -. [Q14515-2]
DR PIR; S60062; S60062.
DR RefSeq; NP_001121782.1; NM_001128310.2. [Q14515-1]
DR RefSeq; NP_001278905.1; NM_001291976.1. [Q14515-2]
DR RefSeq; NP_001278906.1; NM_001291977.1. [Q14515-2]
DR RefSeq; NP_004675.3; NM_004684.5. [Q14515-1]
DR PDB; 7KBU; X-ray; 2.27 A; A/B=431-663.
DR PDBsum; 7KBU; -.
DR AlphaFoldDB; Q14515; -.
DR SMR; Q14515; -.
DR BioGRID; 113992; 11.
DR IntAct; Q14515; 9.
DR MINT; Q14515; -.
DR STRING; 9606.ENSP00000414856; -.
DR TCDB; 8.A.74.1.5; the tm9 or phg1 targeting receptor (ppg1) family.
DR GlyConnect; 728; 1 N-Linked glycan (1 site), 3 O-Linked glycans (6 sites).
DR GlyGen; Q14515; 18 sites, 2 N-linked glycans (1 site), 6 O-linked glycans (11 sites).
DR iPTMnet; Q14515; -.
DR PhosphoSitePlus; Q14515; -.
DR BioMuta; SPARCL1; -.
DR DMDM; 259016170; -.
DR jPOST; Q14515; -.
DR MassIVE; Q14515; -.
DR PaxDb; Q14515; -.
DR PeptideAtlas; Q14515; -.
DR PRIDE; Q14515; -.
DR ProteomicsDB; 5865; -.
DR ProteomicsDB; 60018; -. [Q14515-1]
DR Antibodypedia; 25430; 283 antibodies from 32 providers.
DR DNASU; 8404; -.
DR Ensembl; ENST00000282470.11; ENSP00000282470.6; ENSG00000152583.13. [Q14515-1]
DR Ensembl; ENST00000418378.5; ENSP00000414856.1; ENSG00000152583.13. [Q14515-1]
DR Ensembl; ENST00000503414.5; ENSP00000422903.1; ENSG00000152583.13. [Q14515-2]
DR GeneID; 8404; -.
DR KEGG; hsa:8404; -.
DR MANE-Select; ENST00000282470.11; ENSP00000282470.6; NM_004684.6; NP_004675.3.
DR UCSC; uc003hqs.5; human. [Q14515-1]
DR CTD; 8404; -.
DR DisGeNET; 8404; -.
DR GeneCards; SPARCL1; -.
DR HGNC; HGNC:11220; SPARCL1.
DR HPA; ENSG00000152583; Low tissue specificity.
DR MIM; 606041; gene.
DR neXtProt; NX_Q14515; -.
DR OpenTargets; ENSG00000152583; -.
DR PharmGKB; PA36056; -.
DR VEuPathDB; HostDB:ENSG00000152583; -.
DR eggNOG; KOG4004; Eukaryota.
DR GeneTree; ENSGT00510000046787; -.
DR HOGENOM; CLU_026297_0_1_1; -.
DR InParanoid; Q14515; -.
DR OMA; CKRGHVC; -.
DR PhylomeDB; Q14515; -.
DR TreeFam; TF319356; -.
DR PathwayCommons; Q14515; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q14515; -.
DR BioGRID-ORCS; 8404; 12 hits in 1068 CRISPR screens.
DR ChiTaRS; SPARCL1; human.
DR GeneWiki; SPARCL1; -.
DR GenomeRNAi; 8404; -.
DR Pharos; Q14515; Tbio.
DR PRO; PR:Q14515; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q14515; protein.
DR Bgee; ENSG00000152583; Expressed in middle temporal gyrus and 213 other tissues.
DR ExpressionAtlas; Q14515; baseline and differential.
DR Genevisible; Q14515; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001999; Osteonectin_CS.
DR InterPro; IPR016359; SPARC-like_p1.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR PIRSF; PIRSF002574; SPARC-like_p1; 1.
DR SMART; SM00274; FOLN; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00612; OSTEONECTIN_1; 1.
DR PROSITE; PS00613; OSTEONECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..664
FT /note="SPARC-like protein 1"
FT /id="PRO_0000020312"
FT DOMAIN 432..454
FT /note="Follistatin-like"
FT DOMAIN 450..511
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 622..657
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 25..34
FT /note="O-glycosylated at one additional site"
FT REGION 28..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 635
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 637
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 639
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70663"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70663"
FT CARBOHYD 31
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 40
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 44
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 116
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="O-linked (GalNAc...) threonine"
FT CARBOHYD 398
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:23234360"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 433..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 438..454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 456..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 462..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 472..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 515..626
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 634..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056678"
FT VARIANT 49
FT /note="A -> D (in dbSNP:rs13051)"
FT /evidence="ECO:0000269|PubMed:7600298"
FT /id="VAR_016107"
FT VARIANT 106
FT /note="H -> D (in dbSNP:rs1049544)"
FT /evidence="ECO:0000269|PubMed:7600298"
FT /id="VAR_058849"
FT VARIANT 419
FT /note="T -> A (in dbSNP:rs1130643)"
FT /id="VAR_056578"
FT CONFLICT 5
FT /note="L -> P (in Ref. 2; CAA60386)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="R -> W (in Ref. 2; CAA60386)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="T -> S (in Ref. 1; CAA57650)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="S -> I (in Ref. 2; CAA60386)"
FT /evidence="ECO:0000305"
FT TURN 432..435
FT /evidence="ECO:0007829|PDB:7KBU"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:7KBU"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:7KBU"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:7KBU"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 482..491
FT /evidence="ECO:0007829|PDB:7KBU"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:7KBU"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 525..542
FT /evidence="ECO:0007829|PDB:7KBU"
FT TURN 558..561
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 562..568
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 573..577
FT /evidence="ECO:0007829|PDB:7KBU"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:7KBU"
FT TURN 585..588
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 589..599
FT /evidence="ECO:0007829|PDB:7KBU"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 610..624
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 630..633
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 644..650
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:7KBU"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:7KBU"
SQ SEQUENCE 664 AA; 75208 MW; 0750B0080FDB96B6 CRC64;
MKTGLFFLCL LGTAAAIPTN ARLLSDHSKP TAETVAPDNT AIPSLRAEAE ENEKETAVST
EDDSHHKAEK SSVLKSKEES HEQSAEQGKS SSQELGLKDQ EDSDGHLSVN LEYAPTEGTL
DIKEDMSEPQ EKKLSENTDF LAPGVSSFTD SNQQESITKR EENQEQPRNY SHHQLNRSSK
HSQGLRDQGN QEQDPNISNG EEEEEKEPGE VGTHNDNQER KTELPREHAN SKQEEDNTQS
DDILEESDQP TQVSKMQEDE FDQGNQEQED NSNAEMEEEN ASNVNKHIQE TEWQSQEGKT
GLEAISNHKE TEEKTVSEAL LMEPTDDGNT TPRNHGVDDD GDDDGDDGGT DGPRHSASDD
YFIPSQAFLE AERAQSIAYH LKIEEQREKV HENENIGTTE PGEHQEAKKA ENSSNEEETS
SEGNMRVHAV DSCMSFQCKR GHICKADQQG KPHCVCQDPV TCPPTKPLDQ VCGTDNQTYA
SSCHLFATKC RLEGTKKGHQ LQLDYFGACK SIPTCTDFEV IQFPLRMRDW LKNILMQLYE
ANSEHAGYLN EKQRNKVKKI YLDEKRLLAG DHPIDLLLRD FKKNYHMYVY PVHWQFSELD
QHPMDRVLTH SELAPLRASL VPMEHCITRF FEECDPNKDK HITLKEWGHC FGIKEEDIDE
NLLF
