PA2GF_HUMAN
ID PA2GF_HUMAN Reviewed; 168 AA.
AC Q9BZM2; Q5R385; Q8N217; Q9H506;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Group IIF secretory phospholipase A2 {ECO:0000303|PubMed:11877435};
DE Short=GIIF sPLA2;
DE Short=sPLA2-IIF;
DE EC=3.1.1.4 {ECO:0000269|PubMed:11112443};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2F;
DE Flags: Precursor;
GN Name=PLA2G2F;
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), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal lung, Heart, and Spleen;
RX PubMed=11112443; DOI=10.1006/bbrc.2000.3908;
RA Valentin E., Singer A.G., Ghomashchi F., Lazdunski M., Gelb M.H.,
RA Lambeau G.;
RT "Cloning and recombinant expression of human group IIF-secreted
RT phospholipase A(2).";
RL Biochem. Biophys. Res. Commun. 279:223-228(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11877435; DOI=10.1074/jbc.m112385200;
RA Murakami M., Yoshihara K., Shimbara S., Lambeau G., Gelb M.H., Singer A.G.,
RA Sawada M., Inagaki N., Nagai H., Ishihara M., Ishikawa Y., Ishii T.,
RA Kudo I.;
RT "Cellular arachidonate-releasing function and inflammation-associated
RT expression of group IIF secretory phospholipase A2.";
RL J. Biol. Chem. 277:19145-19155(2002).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids. Hydrolyzes the ester bond of the
CC fatty acyl group attached at the sn-2 position of phospholipids
CC (phospholipase A2 activity), the catalytic efficiency decreasing in the
CC following order: phosphatidylglycerols > phosphatidylethanolamines >
CC phosphatidylcholines > phosphatidylserines (PubMed:11112443). May play
CC a role in lipid mediator production in inflammatory conditions, by
CC providing arachidonic acid to downstream cyclooxygenases and
CC lipoxygenases (By similarity). {ECO:0000250|UniProtKB:Q9QZT4,
CC ECO:0000269|PubMed:11112443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10035,
CC ECO:0000269|PubMed:11112443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:11112443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000269|PubMed:11112443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000305|PubMed:11112443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000250|UniProtKB:Q9QZT4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:Q9QZT4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000250|UniProtKB:Q9QZT4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:Q9QZT4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:11112443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:11112443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:75029; Evidence={ECO:0000269|PubMed:11112443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41753;
CC Evidence={ECO:0000305|PubMed:11112443};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11112443};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11112443};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:11112443};
CC -!- INTERACTION:
CC Q9BZM2-2; P41271-2: NBL1; NbExp=3; IntAct=EBI-12826629, EBI-12135485;
CC Q9BZM2-2; O95231: VENTX; NbExp=3; IntAct=EBI-12826629, EBI-10191303;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC {ECO:0000250|UniProtKB:Q9QZT4}. Cell membrane; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9QZT4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BZM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZM2-2; Sequence=VSP_037524;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in placenta, testis,
CC thymus and at lower levels in heart, kidney, liver and prostate
CC (PubMed:11112443). Highly expressed in rheumatoid arthritic tissues,
CC including synovial lining cells in the intima, capillary endothelial
CC cells and plasma cells (PubMed:11877435). {ECO:0000269|PubMed:11112443,
CC ECO:0000269|PubMed:11877435}.
CC -!- MISCELLANEOUS: [Isoform 2]: No signal peptide could be predicted in
CC this isoform, challenging its subcellular location within the secretory
CC pathway and hence the formation of disulfide bonds, which are required
CC for its activity. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 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; AF306566; AAG50242.1; -; mRNA.
DR EMBL; AK093645; BAC04210.1; -; mRNA.
DR EMBL; AL158172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS204.2; -. [Q9BZM2-2]
DR RefSeq; NP_073730.3; NM_022819.3. [Q9BZM2-2]
DR RefSeq; XP_011540258.1; XM_011541956.1. [Q9BZM2-2]
DR AlphaFoldDB; Q9BZM2; -.
DR SMR; Q9BZM2; -.
DR BioGRID; 122219; 4.
DR IntAct; Q9BZM2; 2.
DR STRING; 9606.ENSP00000364243; -.
DR BindingDB; Q9BZM2; -.
DR ChEMBL; CHEMBL4278; -.
DR GuidetoPHARMACOLOGY; 1420; -.
DR SwissLipids; SLP:000000654; -. [Q9BZM2-1]
DR GlyGen; Q9BZM2; 4 sites.
DR iPTMnet; Q9BZM2; -.
DR PhosphoSitePlus; Q9BZM2; -.
DR BioMuta; PLA2G2F; -.
DR DMDM; 20139134; -.
DR MassIVE; Q9BZM2; -.
DR PaxDb; Q9BZM2; -.
DR PRIDE; Q9BZM2; -.
DR Antibodypedia; 68368; 5 antibodies from 3 providers.
DR DNASU; 64600; -.
DR Ensembl; ENST00000375102.4; ENSP00000364243.4; ENSG00000158786.5. [Q9BZM2-2]
DR GeneID; 64600; -.
DR KEGG; hsa:64600; -.
DR MANE-Select; ENST00000375102.4; ENSP00000364243.4; NM_022819.4; NP_073730.3. [Q9BZM2-2]
DR UCSC; uc009vpp.2; human. [Q9BZM2-1]
DR CTD; 64600; -.
DR GeneCards; PLA2G2F; -.
DR HGNC; HGNC:30040; PLA2G2F.
DR HPA; ENSG00000158786; Group enriched (lymphoid tissue, skin, urinary bladder).
DR neXtProt; NX_Q9BZM2; -.
DR OpenTargets; ENSG00000158786; -.
DR PharmGKB; PA134931043; -.
DR VEuPathDB; HostDB:ENSG00000158786; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000161819; -.
DR HOGENOM; CLU_090683_2_0_1; -.
DR InParanoid; Q9BZM2; -.
DR OMA; ETECDKQ; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q9BZM2; -.
DR TreeFam; TF319283; -.
DR PathwayCommons; Q9BZM2; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; Q9BZM2; -.
DR BioGRID-ORCS; 64600; 8 hits in 1063 CRISPR screens.
DR GenomeRNAi; 64600; -.
DR Pharos; Q9BZM2; Tchem.
DR PRO; PR:Q9BZM2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BZM2; protein.
DR Bgee; ENSG00000158786; Expressed in skin of leg and 45 other tissues.
DR Genevisible; Q9BZM2; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; NAS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Immunity; Innate immunity; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..168
FT /note="Group IIF secretory phospholipase A2"
FT /id="PRO_0000022759"
FT REGION 139..168
FT /note="Required for localization on the plasma membrane"
FT /evidence="ECO:0000250|UniProtKB:Q9QZT4"
FT ACT_SITE 67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
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 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..138
FT /evidence="ECO:0000250"
FT DISULFID 48..64
FT /evidence="ECO:0000250"
FT DISULFID 63..120
FT /evidence="ECO:0000250"
FT DISULFID 69..145
FT /evidence="ECO:0000250"
FT DISULFID 70..113
FT /evidence="ECO:0000250"
FT DISULFID 79..106
FT /evidence="ECO:0000250"
FT DISULFID 98..111
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MADGAKANPKGFKKKVLDRCFSGWRGPRFGASCPSRTSRSSLGM
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037524"
FT CONFLICT 149
FT /note="E -> G (in Ref. 2; BAC04210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 18658 MW; 35B159298246A762 CRC64;
MKKFFTVAIL AGSVLSTAHG SLLNLKAMVE AVTGRSAILS FVGYGCYCGL GGRGQPKDEV
DWCCHAHDCC YQELFDQGCH PYVDHYDHTI ENNTEIVCSD LNKTECDKQT CMCDKNMVLC
LMNQTYREEY RGFLNVYCQG PTPNCSIYEP PPEEVTCSHQ SPAPPAPP
