FUT7_RAT
ID FUT7_RAT Reviewed; 370 AA.
AC Q712G6;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 7 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:16218937};
DE AltName: Full=Fucosyltransferase 7;
DE AltName: Full=Fucosyltransferase VII {ECO:0000250|UniProtKB:Q11130};
DE Short=Fuc-TVII {ECO:0000250|UniProtKB:Q11130};
DE Short=FucT-VII;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
DE AltName: Full=Selectin ligand synthase;
GN Name=Fut7 {ECO:0000312|RGD:735019};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION,
RP TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Kidney;
RX PubMed=16218937; DOI=10.1111/j.1600-0463.2005.apm_279.x;
RA Niittymaki J., Mattila P., Renkonen R.;
RT "Cloning and expression of rat fucosyltransferase VII at sites of
RT inflammation.";
RL APMIS 113:613-620(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a
CC distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a
CC glycolipid-linked sialopolylactosamines chain through an alpha-1,3
CC glycosidic linkage and participates in the final fucosylation step in
CC the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate
CC involved in cell and matrix adhesion during leukocyte trafficking and
CC fertilization (PubMed:16218937). In vitro, also synthesizes sialyl-
CC dimeric-Lex structures, from VIM-2 structures and both di-fucosylated
CC and trifucosylated structures from mono-fucosylated precursors. However
CC does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3
CC fucosylation is present in polylactosamine chain and the fucosylation
CC rate of the internal GlcNAc residues is reduced once fucose has been
CC added to the distal GlcNAc. Also catalyzes the transfer of a fucose
CC from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to
CC produce 6-sulfo sLex mediating significant L-selectin-dependent cell
CC adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and
CC SELP-mediated cell adhesion with leukocytes and allows leukocytes
CC tethering and rolling along the endothelial tissue thereby enabling the
CC leukocytes to accumulate at a site of inflammation. May enhance embryo
CC implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo
CC cells to endometrium. May affect insulin signaling by up-regulating the
CC phosphorylation and expression of some signaling molecules involved in
CC the insulin-signaling pathway through SLe(x) which is present on the
CC glycans of the INSRR alpha subunit (By similarity).
CC {ECO:0000250|UniProtKB:Q11130, ECO:0000269|PubMed:16218937}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an
CC alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-
CC GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:136545, ChEBI:CHEBI:139509;
CC Evidence={ECO:0000269|PubMed:16218937};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000305|PubMed:16218937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-NeuAc-nLc4Cer + GDP-beta-L-fucose =
CC GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC (1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide;
CC Xref=Rhea:RHEA:48392, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90390, ChEBI:CHEBI:90392;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48393;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = GDP + H(+) + N-
CC acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide;
CC Xref=Rhea:RHEA:48356, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90336, ChEBI:CHEBI:90339;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48357;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-
CC L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-
CC (1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:52864,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145342, ChEBI:CHEBI:145343;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc6S
CC derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-
CC (1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc6S derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62004, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145344, ChEBI:CHEBI:145345;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62005;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-D-Glc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-D-Glc + GDP + H(+); Xref=Rhea:RHEA:62008,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145346, ChEBI:CHEBI:145347;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62009;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-beta-D-GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC (1->4)-beta-D-GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62060,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145400, ChEBI:CHEBI:145401;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62061;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-
CC GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-
CC [alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-
CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP + H(+);
CC Xref=Rhea:RHEA:62056, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145398, ChEBI:CHEBI:145399;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62057;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- ACTIVITY REGULATION: Inhibited by NaCl. Inhibited by GDP in a
CC concentration dependent manner, with an IC(50) value of 93 uM. Also
CC inhibited by GMP and GTP. Inhibited by N-ethylmaleimide. Activated by
CC poly(ethylene glycol) by enhancing the thermal stability of FUT7.
CC Activated by Mn2+, Ca2+, and Mg2+. Both panosialin A and B inhibit
CC activity with IC(50) values of 4.8 and 5.3 ug/ml, respectively.
CC Inhibited by gallic acid (GA) and (-)-epigallocatechin gallate (EGCG)
CC in a time-dependent and irreversible manner with IC(50) values of 60
CC and 700 nM, respectively. {ECO:0000250|UniProtKB:Q11130}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q11130}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in lymph node and kidney.
CC {ECO:0000269|PubMed:16218937}.
CC -!- INDUCTION: Strongly induced in kidney allograft during rejection.
CC {ECO:0000269|PubMed:16218937}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16218937}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; AJ276068; CAC81972.2; -; mRNA.
DR EMBL; AABR07051241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_955785.1; NM_199491.1.
DR AlphaFoldDB; Q712G6; -.
DR STRING; 10116.ENSRNOP00000033858; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q712G6; 3 sites.
DR PaxDb; Q712G6; -.
DR Ensembl; ENSRNOT00000037169; ENSRNOP00000033858; ENSRNOG00000014156.
DR GeneID; 296564; -.
DR KEGG; rno:296564; -.
DR UCSC; RGD:735019; rat.
DR CTD; 2529; -.
DR RGD; 735019; Fut7.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000161618; -.
DR InParanoid; Q712G6; -.
DR OMA; SDTCTRY; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q712G6; -.
DR BRENDA; 2.4.1.152; 5301.
DR Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q712G6; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000014156; Expressed in thymus and 7 other tissues.
DR ExpressionAtlas; Q712G6; baseline and differential.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0017083; F:4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; ISO:RGD.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; ISO:RGD.
DR GO; GO:0006672; P:ceramide metabolic process; ISO:RGD.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0002522; P:leukocyte migration involved in immune response; ISO:RGD.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0097022; P:lymphocyte migration into lymph node; ISS:UniProtKB.
DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:RGD.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISO:RGD.
DR GO; GO:0060353; P:regulation of cell adhesion molecule production; ISO:RGD.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:1904994; P:regulation of leukocyte adhesion to vascular endothelial cell; ISO:RGD.
DR GO; GO:1903037; P:regulation of leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:1903236; P:regulation of leukocyte tethering or rolling; ISO:RGD.
DR GO; GO:2000389; P:regulation of neutrophil extravasation; ISO:RGD.
DR GO; GO:0001807; P:regulation of type IV hypersensitivity; ISO:RGD.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="Alpha-(1,3)-fucosyltransferase 7"
FT /id="PRO_0000449123"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..59
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..370
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..104
FT /evidence="ECO:0000250|UniProtKB:Q11130"
FT DISULFID 239..242
FT /evidence="ECO:0000250|UniProtKB:Q11130"
FT DISULFID 346..349
FT /evidence="ECO:0000250|UniProtKB:Q11130"
SQ SEQUENCE 370 AA; 42958 MW; 7CA9F59A01E9B957 CRC64;
MVQGCLCWRG CCDLKTSFPW VTNSRRLWMN CIGCNPVWRL RAWGCLAGGT TLMVIWLFWL
LRSVPGGAPA PQPTLTILIW HWPFTNRSPE LSSDTCTRYG MASCHLSANR SLLASADAVV
FHHRELQTRH SRLPLDQRPH GQPWVWATME SPSNTHGLRH FRGIFNWVLS YRRDSDIFVP
YGRLEPFSGP TPPLPAKSRM AAWVVSNFQE RQQRAKLYRQ LAPHLKVDVF GRASGRPLCP
NCLLPTVARY RFYLSFENSQ HRDYITEKFW RNALAAGAVP VVLGPPRTTY EAFVPPDAFI
HVDDFSSARE LAVFLVSMNE SRYRGFFAWR DRLRVRLLND WRERFCTICA RYPYLPRSQV
YEDLESWFQA
