MIG17_CAEEL
ID MIG17_CAEEL Reviewed; 509 AA.
AC Q20930; Q9NDL4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Metalloprotease mig-17 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:18637819};
DE AltName: Full=Abnormal cell migration protein 17 {ECO:0000312|WormBase:F57B7.4};
DE Flags: Precursor;
GN Name=mig-17 {ECO:0000312|WormBase:F57B7.4};
GN ORFNames=F57B7.4 {ECO:0000312|WormBase:F57B7.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ASP-79 AND GLU-303.
RX PubMed=10864868; DOI=10.1126/science.288.5474.2205;
RA Nishiwaki K., Hisamoto N., Matsumoto K.;
RT "A metalloprotease disintegrin that controls cell migration in
RT Caenorhabditis elegans.";
RL Science 288:2205-2208(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GLYCOSYLATION, AND MUTAGENESIS OF ASN-52; ASN-65; ASN-123; ASN-172;
RP ASN-183; ASN-189; 218-ASN-ASN-219 AND ASN-350.
RX PubMed=14688791; DOI=10.1038/ncb1079;
RA Nishiwaki K., Kubota Y., Chigira Y., Roy S.K., Suzuki M., Schvarzstein M.,
RA Jigami Y., Hisamoto N., Matsumoto K.;
RT "An NDPase links ADAM protease glycosylation with organ morphogenesis in C.
RT elegans.";
RL Nat. Cell Biol. 6:31-37(2004).
RN [4]
RP FUNCTION.
RX PubMed=15556863; DOI=10.1016/j.cub.2004.10.047;
RA Kubota Y., Kuroki R., Nishiwaki K.;
RT "A fibulin-1 homolog interacts with an ADAM protease that controls cell
RT migration in C. elegans.";
RL Curr. Biol. 14:2011-2018(2004).
RN [5]
RP GLYCOSYLATION.
RX PubMed=16354716; DOI=10.1242/dev.02195;
RA Kubota Y., Sano M., Goda S., Suzuki N., Nishiwaki K.;
RT "The conserved oligomeric Golgi complex acts in organ morphogenesis via
RT glycosylation of an ADAM protease in C. elegans.";
RL Development 133:263-273(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-350, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, GLYCOSYLATION,
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASN-52; ASN-65; ASP-79; ASN-123;
RP ASN-172; ASN-183; ASN-189; 162-ARG-ARG-163; 202-LYS-LYS-203;
RP 205-ARG-LYS-206; 218-ASN-ASN-219; GLY-292; GLU-303 AND ASN-350.
RX PubMed=17491590; DOI=10.1038/sj.emboj.7601718;
RA Ihara S., Nishiwaki K.;
RT "Prodomain-dependent tissue targeting of an ADAMTS protease controls cell
RT migration in Caenorhabditis elegans.";
RL EMBO J. 26:2607-2620(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF 202-LYS-LYS-203 AND GLU-303.
RX PubMed=18637819; DOI=10.1111/j.1742-4658.2008.06573.x;
RA Ihara S., Nishiwaki K.;
RT "Stage-specific activation of MIG-17/ADAMTS controls cell migration in
RT Caenorhabditis elegans.";
RL FEBS J. 275:4296-4305(2008).
RN [9]
RP FUNCTION.
RX PubMed=19104038; DOI=10.1073/pnas.0804055106;
RA Kubota Y., Ohkura K., Tamai K.K., Nagata K., Nishiwaki K.;
RT "MIG-17/ADAMTS controls cell migration by recruiting nidogen to the
RT basement membrane in C. elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20804-20809(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24318535; DOI=10.1534/genetics.113.157685;
RA Kim H.S., Kitano Y., Mori M., Takano T., Harbaugh T.E., Mizutani K.,
RA Yanagimoto H., Miwa S., Ihara S., Kubota Y., Shibata Y., Ikenishi K.,
RA Garriga G., Nishiwaki K.;
RT "The novel secreted factor MIG-18 acts with MIG-17/ADAMTS to control cell
RT migration in Caenorhabditis elegans.";
RL Genetics 196:471-479(2014).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, GLYCOSYLATION,
RP AND MUTAGENESIS OF ASN-52; ASN-65; ASP-79; ASN-123; ASN-172; ASN-183;
RP ASN-189; 218-ASN-ASN-219; GLY-292; GLU-303 AND ASN-350.
RX PubMed=26994289; DOI=10.1534/g3.116.028019;
RA Shibata Y., Kawakado Y., Hori N., Tanaka K., Inoue R., Takano T.,
RA Kubota Y., Nishiwaki K.;
RT "Organ length control by an ADAMTS extracellular protease in Caenorhabditis
RT elegans.";
RL G3 (Bethesda) 6:1449-1457(2016).
CC -!- FUNCTION: Metalloprotease (PubMed:17491590, PubMed:18637819). Acts in
CC the basement membrane to control directional migration of distal tip
CC cells (DTCs) along the body wall basement membranes, a key step that
CC promotes gonad morphogenesis (PubMed:10864868, PubMed:15556863,
CC PubMed:17491590,PubMed:19104038, PubMed:24318535, PubMed:26994289).
CC Regulates DTC migration probably by recruiting fibulin fbl-1, type IV
CC collagen let-2 and nidogen nid-1 to the gonad basement membrane thereby
CC promoting the remodeling of the basement membrane (PubMed:19104038).
CC During larval development and probably upstream of basement membrane
CC proteins fbl-1, let-2 and nid-1, regulates pharynx length, probably by
CC regulating pharyngeal cell length (PubMed:26994289). Does not recruit
CC fbl-1 to the pharynx basement membrane (PubMed:26994289).
CC {ECO:0000269|PubMed:10864868, ECO:0000269|PubMed:15556863,
CC ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:18637819,
CC ECO:0000269|PubMed:19104038, ECO:0000269|PubMed:24318535,
CC ECO:0000269|PubMed:26994289}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UHI8};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:10864868,
CC ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:18637819,
CC ECO:0000269|PubMed:24318535, ECO:0000269|PubMed:26994289}.
CC Note=Secreted as a zymogen (PubMed:17491590, PubMed:18637819). The
CC zymogen localizes to the basement membrane of gonads, intestine and
CC hypodermis (PubMed:17491590, PubMed:18637819). The mature and active
CC form displays a similar localization but only during the L3 larval
CC stage (PubMed:18637819). {ECO:0000269|PubMed:17491590,
CC ECO:0000269|PubMed:18637819}.
CC -!- TISSUE SPECIFICITY: Secreted from muscle cells and functions in the
CC basement membrane of the gonad to guide DTC migration (PubMed:10864868,
CC PubMed:24318535). Localizes to the pharyngeal basement membrane
CC (PubMed:26994289). {ECO:0000269|PubMed:10864868,
CC ECO:0000269|PubMed:24318535, ECO:0000269|PubMed:26994289}.
CC -!- DEVELOPMENTAL STAGE: First expressed in late embryos and continues
CC through the adult stage. Observed on the surface of gonad, starting
CC when distal tip cells migrate over the lateral hypodermis toward the
CC dorsal muscles. {ECO:0000269|PubMed:10864868,
CC ECO:0000269|PubMed:18637819}.
CC -!- DOMAIN: The propeptide is required for localization to the gonad
CC basement membrane. {ECO:0000269|PubMed:17491590}.
CC -!- DOMAIN: The disintegrin domain is required for distal tip cell
CC migration and partially for mig-17 localization to the gonad
CC (PubMed:17491590). Required for the control of pharynx length
CC (PubMed:26994289). {ECO:0000269|PubMed:17491590,
CC ECO:0000269|PubMed:26994289}.
CC -!- DOMAIN: The PLAC domain is required for distal tip cell migration but
CC not for gonadal localization. {ECO:0000269|PubMed:17491590}.
CC -!- PTM: N-glycosylated by the COG complex; required for gonadal
CC localization (PubMed:14688791, PubMed:16354716, PubMed:17761667,
CC PubMed:17491590). N-glycosylation of the propeptide is required for
CC gonadal localization but not for distal tip cell migration
CC (PubMed:17491590). Required for the regulation of pharynx length
CC (PubMed:26994289). N-glycosylation is not required for mig-17 secretion
CC (PubMed:17491590). {ECO:0000269|PubMed:14688791,
CC ECO:0000269|PubMed:16354716, ECO:0000269|PubMed:17491590,
CC ECO:0000269|PubMed:17761667, ECO:0000269|PubMed:26994289}.
CC -!- PTM: The precursor is cleaved into the active mature form by
CC autoproteolysis (PubMed:17491590, PubMed:18637819). Cleavage occurs
CC after secretion and only during the L3-L4 larval stages
CC (PubMed:18637819). {ECO:0000269|PubMed:17491590,
CC ECO:0000269|PubMed:18637819}.
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DR EMBL; AB044562; BAA96734.1; -; mRNA.
DR EMBL; Z74037; CAA98493.3; -; Genomic_DNA.
DR PIR; T22836; T22836.
DR RefSeq; NP_505901.2; NM_073500.6.
DR AlphaFoldDB; Q20930; -.
DR STRING; 6239.F57B7.4; -.
DR MEROPS; M12.019; -.
DR iPTMnet; Q20930; -.
DR EPD; Q20930; -.
DR PaxDb; Q20930; -.
DR PeptideAtlas; Q20930; -.
DR EnsemblMetazoa; F57B7.4.1; F57B7.4.1; WBGene00003248.
DR GeneID; 179575; -.
DR KEGG; cel:CELE_F57B7.4; -.
DR UCSC; F57B7.4; c. elegans.
DR CTD; 179575; -.
DR WormBase; F57B7.4; CE31010; WBGene00003248; mig-17.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000166961; -.
DR HOGENOM; CLU_041055_0_0_1; -.
DR InParanoid; Q20930; -.
DR OMA; SICERIW; -.
DR OrthoDB; 343125at2759; -.
DR PhylomeDB; Q20930; -.
DR PRO; PR:Q20930; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003248; Expressed in material anatomical entity and 5 other tissues.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:WormBase.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:1903354; P:regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
DR CDD; cd04267; ZnMc_ADAM_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR033817; MIG-17.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR010909; PLAC.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cleavage on pair of basic residues;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..206
FT /evidence="ECO:0000269|PubMed:18637819"
FT /id="PRO_0000441252"
FT CHAIN 207..509
FT /note="Metalloprotease mig-17"
FT /id="PRO_0000250562"
FT DOMAIN 207..372
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 390..464
FT /note="Disintegrin"
FT DOMAIN 465..506
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT ACT_SITE 303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT SITE 206..207
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:18637819"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 279..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT MUTAGEN 52
FT /note="N->Q: Impaired gonadal localization and slight
FT impairment in DTC posterior migration. Impaired gonadal
FT localization and DTC posterior migration; when associated
FT with Q-65; Q-123; Q-172; Q-183 and Q-189. Elongated
FT pharynx; when associated with Q-65; Q-123; Q-172; Q-183; Q-
FT 189; Q-218; Q-219 and Q-350."
FT /evidence="ECO:0000269|PubMed:14688791,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
FT MUTAGEN 65
FT /note="N->Q: Impaired gonadal localization and slight
FT impairment in DTC posterior migration. Impaired gonadal
FT localization and DTC posterior migration; when associated
FT with Q-52; Q-123; Q-172; Q-183 and Q-189. Elongated
FT pharynx; when associated with Q-52; Q-123; Q-172; Q-183; Q-
FT 189; Q-218; Q-219 and Q-350."
FT /evidence="ECO:0000269|PubMed:14688791,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
FT MUTAGEN 79
FT /note="D->N: In k135; DTCs migrate along the ventral
FT surface but then return toward the dorsal surface. Loss of
FT gonadal basement membrane localization. Pharyngeal corpus
FT and isthmus are elongated in larvae and adults."
FT /evidence="ECO:0000269|PubMed:10864868,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
FT MUTAGEN 123
FT /note="N->Q: Impaired gonadal localization and DTC
FT posterior migration; when associated with Q-52; Q-65; Q-
FT 172; Q-183 and Q-189. Elongated pharynx; when associated
FT with Q-52; Q-65; Q-172; Q-183; Q-189; Q-218; Q-219 and Q-
FT 350."
FT /evidence="ECO:0000269|PubMed:14688791,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
FT MUTAGEN 162..163
FT /note="RR->LL: Normal propeptide cleavage, gonadal
FT localization and DTC migration."
FT /evidence="ECO:0000269|PubMed:17491590"
FT MUTAGEN 172
FT /note="N->Q: Impaired gonadal localization and slight
FT impairment in DTC migration. Impaired gonadal localization
FT and DTC posterior migration; when associated with Q-52; Q-
FT 65; Q-123; Q-183 and Q-189. Elongated pharynx; when
FT associated with Q-52; Q-65; Q-123; Q-183; Q-189; Q-218; Q-
FT 219 and Q-350."
FT /evidence="ECO:0000269|PubMed:14688791,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
FT MUTAGEN 183
FT /note="N->Q: Impaired gonadal localization and DTC
FT posterior migration; when associated with Q-52; Q-65; Q-
FT 123; Q-172 and Q-189. Elongated pharynx; when associated
FT with Q-52; Q-65; Q-123; Q-172; Q-189; Q-218; Q-219 and Q-
FT 350."
FT /evidence="ECO:0000269|PubMed:14688791,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
FT MUTAGEN 189
FT /note="N->Q: Impaired gonadal localization and slight
FT impairment in DTC posterior migration. Impaired gonadal
FT localization and DTC posterior migration; when associated
FT with Q-52; Q-65; Q-123; Q-172 and Q-183. Elongated pharynx;
FT when associated with Q-52; Q-65; Q-123; Q-172; Q-189; Q-
FT 218; Q-219 and Q-350."
FT /evidence="ECO:0000269|PubMed:14688791,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
FT MUTAGEN 202..203
FT /note="KK->LL: No cleavage of the propeptide."
FT /evidence="ECO:0000269|PubMed:17491590,
FT ECO:0000269|PubMed:18637819"
FT MUTAGEN 203..206
FT /note="KLRK->RRRR: Increased propeptide cleavage and
FT impaired DTC migration. Normal gonadal localization."
FT /evidence="ECO:0000269|PubMed:17491590"
FT MUTAGEN 205..206
FT /note="RK->LL: Normal propeptide cleavage, gonadal
FT localization and DTC migration."
FT /evidence="ECO:0000269|PubMed:17491590"
FT MUTAGEN 218..219
FT /note="NN->QQ: Impaired gonadal localization and DTC
FT posterior migration; when associated with Q-52; Q-65; Q-123
FT and Q-350. Normal localization and slight impairment in DTC
FT posterior migration; when associated with Q-350. Elongated
FT pharynx; when associated with Q-52; Q-65; Q-123; Q-172; Q-
FT 183; Q-189 and Q-350."
FT /evidence="ECO:0000269|PubMed:14688791,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
FT MUTAGEN 219
FT /note="N->Q: Slight impairment in DTC posterior migration."
FT /evidence="ECO:0000269|PubMed:17491590"
FT MUTAGEN 292
FT /note="G->E: In k176 and k169; Impaired DTC migration and
FT loss of gonadal basement membrane localization in 20
FT percent of mutants. Pharynx is elongated."
FT /evidence="ECO:0000269|PubMed:17491590,
FT ECO:0000269|PubMed:26994289"
FT MUTAGEN 303
FT /note="E->A: Loss of function; induces defects in DTCs
FT migration."
FT /evidence="ECO:0000269|PubMed:10864868"
FT MUTAGEN 303
FT /note="E->Q: Probable loss of catalytic activity. No
FT cleavage of the propeptide. Loss of gonadal basement
FT membrane localization in 60 percent of mutants and abnormal
FT DTC migration. Pharynx is elongated."
FT /evidence="ECO:0000269|PubMed:17491590,
FT ECO:0000269|PubMed:18637819, ECO:0000269|PubMed:26994289"
FT MUTAGEN 350
FT /note="N->Q: Slight impairment in DTC posterior migration.
FT Impaired gonadal localization and DTC posterior migration;
FT when associated with Q-52; Q-65; Q-123; Q-218 and Q-219.
FT Normal localization and slight impairment in DTC posterior
FT migration; when associated with Q-218 and Q-219. Elongated
FT pharynx; when associated with Q-52; Q-65; Q-123; Q-172; Q-
FT 183; Q-189; Q-218 and Q-219."
FT /evidence="ECO:0000269|PubMed:14688791,
FT ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:26994289"
SQ SEQUENCE 509 AA; 57976 MW; 812A0219F60398E2 CRC64;
MHTFCILIPT FLVLVWTTES ARREKQQSND ISFVKRKVQD GLKFSRVIKY TNETIQGMKT
NFNSNKTQEL SLDVLVVADF LSYQAFLEMS NGDSHRAIHN LKEYLHALFE QTKIIYDGIS
FGNETLHMVF AGTWIATQER DCPLWISWAE EEEERVLNEE IRRLEEKERD LNSTFVDDTF
FMNSTDSDNS STDALISSDM PKKLRKFVDI TLEEMQENNS TEMTLKIDSK KAIDKFTIWL
KEQTGLPRHE HAVLITKFDL ISINGNSATQ GMAYVGNICE NGDSSSVVED IGAGLTSLIM
AHEIGHSLGA LHDGAYETAE CDSNDNYLMA VAVSGSADRQ SFLNSRRMSN CSINSIIENL
KEPTANCVKK WKTKKGKDVS QKDFIKKPGE LVKITRQCQV AFGPTFIPCL HIGYFHEQSI
CERIWCSDGE SDECQTLNYF PAFDGTECGY NMWCLEGSCV QNTKKWMDCK DINSKTCSKY
STSKLKHYCK SKDFREICCR TCAKKGKIY
