PIPE_DROME
ID PIPE_DROME Reviewed; 514 AA.
AC Q86BJ3; B9EQT7; E1JI38; E4NKL9; E8NH03; F2FB47; O96662; Q7KNQ1; Q86BJ2;
AC Q86BJ4; Q86BJ5; Q86BJ6; Q86BJ7; Q86BJ8; Q86BJ9; Q86BK0; Q8IQU0; Q968U2;
AC Q9VVY5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Heparan sulfate 2-O-sulfotransferase pipe;
DE EC=2.8.2.-;
GN Name=pip; ORFNames=CG9614;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1-379 (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9827800; DOI=10.1016/s0092-8674(00)81615-3;
RA Sen J., Goltz J.S., Stevens L., Stein D.;
RT "Spatially restricted expression of pipe in the Drosophila egg chamber
RT defines embryonic dorsal-ventral polarity.";
RL Cell 95:471-481(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORMS 1;
RP 3; 4; 5; 7; 8; 9; 10 AND 11), AND TISSUE SPECIFICITY.
RX PubMed=11169845;
RX DOI=10.1002/1097-0177(2000)9999:9999<::aid-dvdy1094>3.0.co;2-a;
RA Sergeev P., Streit A., Heller A., Steinmann-Zwicky M.;
RT "The Drosophila dorsoventral determinant PIPE contains ten copies of a
RT variable domain homologous to mammalian heparan sulfate 2-
RT sulfotransferase.";
RL Dev. Dyn. 220:122-132(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5; 7; 10 AND 13).
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Booth B., Carlson J.W.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=9568717; DOI=10.1016/s0092-8674(00)81576-7;
RA Nilson L.A., Schuepbach T.;
RT "Localized requirements for windbeutel and pipe reveal a dorsoventral
RT prepattern within the follicular epithelium of the Drosophila ovary.";
RL Cell 93:253-262(1998).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11076773; DOI=10.1242/dev.127.24.5541;
RA Sen J., Goltz J.S., Konsolaki M., Schuepbach T., Stein D.;
RT "Windbeutel is required for function and correct subcellular localization
RT of the Drosophila patterning protein Pipe.";
RL Development 127:5541-5550(2000).
RN [8]
RP INDUCTION.
RX PubMed=12050143; DOI=10.1242/dev.129.12.2965;
RA Peri F., Technau M., Roth S.;
RT "Mechanisms of Gurken-dependent pipe regulation and the robustness of
RT dorsoventral patterning in Drosophila.";
RL Development 129:2965-2975(2002).
RN [9]
RP INTERACTION WITH WBL.
RX PubMed=15252019; DOI=10.1074/jbc.m406839200;
RA Barnewitz K., Guo C., Sevvana M., Ma Q., Sheldrick G.M., Soeling H.-D.,
RA Ferrari D.M.;
RT "Mapping of a substrate binding site in the protein disulfide isomerase-
RT related chaperone wind based on protein function and crystal structure.";
RL J. Biol. Chem. 279:39829-39837(2004).
CC -!- FUNCTION: Sulfotransferase involved in dorsoventral axis patterning in
CC early embryos. Required for the specific ventral activation of a series
CC of proteases acting in the perivitelline space between the embryonic
CC membrane and the eggshell. Probably acts by mediating the sulfation of
CC some glycoprotein or glycosaminoglycan stably deposited in the egg,
CC whose ventrally localized modification leads to spatially restricted
CC activation of the protease cascade. {ECO:0000269|PubMed:9568717,
CC ECO:0000269|PubMed:9827800}.
CC -!- SUBUNIT: Interacts directly with windbeutel (wbl).
CC {ECO:0000269|PubMed:15252019}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11076773}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:11076773}. Note=Wbl is required for its processing
CC into the Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1; Synonyms=Box 2, L, st2;
CC IsoId=Q86BJ3-1; Sequence=Displayed;
CC Name=2; Synonyms=Box 3, C, st3;
CC IsoId=Q86BJ3-2; Sequence=VSP_014075, VSP_014076;
CC Name=3; Synonyms=Box 6, G, st6;
CC IsoId=Q86BJ3-3; Sequence=VSP_014069, VSP_014070;
CC Name=4; Synonyms=A, Box 10, Pipe-ST2, st10;
CC IsoId=Q86BJ3-4; Sequence=VSP_014067, VSP_014068;
CC Name=5; Synonyms=Box 7, H, st7;
CC IsoId=Q86BJ3-5; Sequence=VSP_014073, VSP_014074;
CC Name=7; Synonyms=Box 1, K, st1;
CC IsoId=Q86BJ3-7; Sequence=VSP_014071, VSP_014072;
CC Name=8; Synonyms=Box 9, J, Pipe-ST1, st9;
CC IsoId=Q86BJ3-8; Sequence=VSP_014077, VSP_014078;
CC Name=9; Synonyms=Box 8, I, st8;
CC IsoId=Q86BJ3-9; Sequence=VSP_014081, VSP_014082;
CC Name=10; Synonyms=Box 4, F, st4;
CC IsoId=Q86BJ3-10; Sequence=VSP_014079, VSP_014080;
CC Name=11; Synonyms=Box 5, D, st5;
CC IsoId=Q86BJ3-11; Sequence=VSP_014065, VSP_014066;
CC Name=12; Synonyms=N;
CC IsoId=Q86BJ3-12; Sequence=VSP_054035;
CC Name=13; Synonyms=M;
CC IsoId=Q86BJ3-13; Sequence=VSP_054034, VSP_054036;
CC -!- TISSUE SPECIFICITY: Isoform 4 is ovary-specific. Isoform 4 and isoform
CC 5 are specifically expressed in the ventral follicle cells of the egg
CC chamber. {ECO:0000269|PubMed:11169845, ECO:0000269|PubMed:9827800}.
CC -!- DEVELOPMENTAL STAGE: Expressed from stage 12 embryos and continues
CC throughout development. Isoform 4 is expressed from stage 14 in the
CC somatic component of the embryonic ovary.
CC -!- INDUCTION: Down-regulated by gurken (grk) and EGF receptor signaling,
CC preventing its expression in dorsal follicle cells.
CC {ECO:0000269|PubMed:12050143, ECO:0000269|PubMed:9827800}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD04925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACM16727.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ADZ49072.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=ADZ49072.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AED98571.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AF102135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF102136; AAD04925.1; ALT_INIT; mRNA.
DR EMBL; AF263993; AAK56855.1; -; mRNA.
DR EMBL; AE014296; AAF49170.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11662.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41225.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41226.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41227.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41228.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41229.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41230.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41231.2; -; Genomic_DNA.
DR EMBL; AE014296; AAO41232.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41233.1; -; Genomic_DNA.
DR EMBL; AE014296; ACZ94738.1; -; Genomic_DNA.
DR EMBL; BT010278; AAQ23596.1; -; mRNA.
DR EMBL; BT058012; ACM16727.1; ALT_INIT; mRNA.
DR EMBL; BT125816; ADR71725.1; -; mRNA.
DR EMBL; BT125857; ADU79245.1; -; mRNA.
DR EMBL; BT126134; ADZ49072.1; ALT_SEQ; mRNA.
DR EMBL; BT126392; AED98571.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001163467.1; NM_001169996.2.
DR RefSeq; NP_524158.2; NM_079434.3. [Q86BJ3-4]
DR RefSeq; NP_730402.1; NM_168793.2. [Q86BJ3-2]
DR RefSeq; NP_788529.1; NM_176351.4. [Q86BJ3-8]
DR RefSeq; NP_788530.1; NM_176352.2. [Q86BJ3-9]
DR RefSeq; NP_788531.1; NM_176353.2. [Q86BJ3-5]
DR RefSeq; NP_788532.1; NM_176354.2. [Q86BJ3-3]
DR RefSeq; NP_788533.1; NM_176355.2. [Q86BJ3-11]
DR RefSeq; NP_788534.1; NM_176356.2. [Q86BJ3-10]
DR RefSeq; NP_788535.2; NM_176357.2. [Q86BJ3-12]
DR RefSeq; NP_788536.1; NM_176358.2. [Q86BJ3-1]
DR RefSeq; NP_788537.1; NM_176359.2. [Q86BJ3-7]
DR AlphaFoldDB; Q86BJ3; -.
DR SMR; Q86BJ3; -.
DR BioGRID; 65379; 21.
DR IntAct; Q86BJ3; 8.
DR STRING; 7227.FBpp0074780; -.
DR GlyGen; Q86BJ3; 5 sites.
DR PaxDb; Q86BJ3; -.
DR DNASU; 40104; -.
DR EnsemblMetazoa; FBtr0075003; FBpp0074770; FBgn0003089. [Q86BJ3-4]
DR EnsemblMetazoa; FBtr0075004; FBpp0074771; FBgn0003089. [Q86BJ3-2]
DR EnsemblMetazoa; FBtr0075005; FBpp0074772; FBgn0003089. [Q86BJ3-11]
DR EnsemblMetazoa; FBtr0075007; FBpp0074774; FBgn0003089. [Q86BJ3-10]
DR EnsemblMetazoa; FBtr0075008; FBpp0074775; FBgn0003089. [Q86BJ3-3]
DR EnsemblMetazoa; FBtr0075009; FBpp0074776; FBgn0003089. [Q86BJ3-5]
DR EnsemblMetazoa; FBtr0075010; FBpp0074777; FBgn0003089. [Q86BJ3-9]
DR EnsemblMetazoa; FBtr0075011; FBpp0074778; FBgn0003089. [Q86BJ3-8]
DR EnsemblMetazoa; FBtr0075012; FBpp0074779; FBgn0003089. [Q86BJ3-7]
DR EnsemblMetazoa; FBtr0075013; FBpp0074780; FBgn0003089. [Q86BJ3-1]
DR EnsemblMetazoa; FBtr0333897; FBpp0306029; FBgn0003089. [Q86BJ3-12]
DR GeneID; 40104; -.
DR KEGG; dme:Dmel_CG9614; -.
DR UCSC; CG9614-RA; d. melanogaster. [Q86BJ3-1]
DR CTD; 5304; -.
DR FlyBase; FBgn0003089; pip.
DR VEuPathDB; VectorBase:FBgn0003089; -.
DR eggNOG; KOG3922; Eukaryota.
DR GeneTree; ENSGT00530000063408; -.
DR InParanoid; Q86BJ3; -.
DR OMA; YHYVREQ; -.
DR PhylomeDB; Q86BJ3; -.
DR Reactome; R-DME-2022923; Dermatan sulfate biosynthesis.
DR SignaLink; Q86BJ3; -.
DR BioGRID-ORCS; 40104; 0 hits in 1 CRISPR screen.
DR ChiTaRS; psq; fly.
DR GenomeRNAi; 40104; -.
DR PRO; PR:Q86BJ3; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003089; Expressed in saliva-secreting gland and 25 other tissues.
DR Genevisible; Q86BJ3; DM.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0030173; C:integral component of Golgi membrane; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0008146; F:sulfotransferase activity; IMP:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:FlyBase.
DR GO; GO:1900005; P:positive regulation of serine-type endopeptidase activity; IMP:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:FlyBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007734; Heparan_SO4_2-O-STrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12129; PTHR12129; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..514
FT /note="Heparan sulfate 2-O-sulfotransferase pipe"
FT /id="PRO_0000207683"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..50
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..514
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 112..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..145
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 106..418
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEA
FT AMQKAKRTVETEYAVVGTWEDTNIT -> ILQLSPDKLNNTPKAEIDVLFFNRVPKTGS
FT MQLIELMRQLGKVHDYDVEKDPQQGGVIPILETAEQSDLIDNIVNLDDGTVFASHVNFL
FT NFTKHEQPRPIYINMVRDPVERVISWYYYIRAPWVFVPGRRRNNREMPNPKWVNTEFDQ
FT CVTSGEKVCTYIENSLLEHVGDHRRQTLFFCGHNEFQCTPFNARLPLQLAKMNVEREYS
FT VVGTWEHTNETLAVLEAYVPRYFADASKMYYSGLHADKQNVNPMKPHISQDILDMVRRN
FT FTREIEFYQFCRQRLHKQYLALKLNDLKRVDKSLAMLSEAKEMAINN (in isoform
FT 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_014065"
FT VAR_SEQ 106..413
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEA
FT AMQKAKRTVETEYAVVGTWE -> MSSLNVRDLNNTRKAQMELVFFNRVPKVGSQTFME
FT LLRRLSERNNFQFHRDAVQKVETIRLAEDQQQEMAEVISELPEPSVFIKHVCFTNFTKF
FT NLPRPIYLNVVRDPVERVISWFYYVRAPWYFVERKAAFPDLPLPHPAWLKKDFETCVLN
FT GDQECTYTQGVTVEGIGDHRRQSLFFCGHDYECTPFNTVGALERAKFAVEQQYAVVGVL
FT EDLNTTLSVLEKYVPRFFEGVRDIYATSAEYLTKINKNNFKPPVSEHVKDIVRRNFTNE
FT IEFYQFCRQRLHKQYLAAHLPQRIITDSAHLPGLIGN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9827800"
FT /id="VSP_014067"
FT VAR_SEQ 106..407
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEA
FT AMQKAKRTVETEYA -> LQQLSANRLNNTKNAEIEVLFFNRAAKVGSESMLELFMALE
FT KYNDDLTLERRGLHTRTVRQMDKKQRRESAEFVADLEEGTMYIEHINWLDFDEFDLPKP
FT IYINLVRDPVERVISWFFYARSSYKNAIEYRKRPNQKIKPESWYKKNFNDCVRSGDPEC
FT QYVPHTVKDSIANFKRQSLFYCGHHDDCLPFNSPTAVQMAKEHVERDYAVVGSWEDTNI
FT TLTVLENYIPRFFRGAKLMYEMHNSKITNRNKNKRKPFVEPEVKEMIRKNFTNEYEFYY
FT FCKQRLYKQYLALNLKELEVHGLLN (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_014069"
FT VAR_SEQ 106..406
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEA
FT AMQKAKRTVETEY -> LKHLTTAQLNNTPRAQVDTLFFNRITKTGSEKMMELLKILGK
FT RHNFEARRDVEGFYEVVIMHDAFAKNFIRTEVLNCTKANSYTKHVAFLDFDLLDEPWPI
FT YINMVRDPIERLVSWFYYVRAPWHFAERKEMFGDAIVLPSIDWLRKDFNRCIEERDPEC
FT VYEQMEMGNLGDHRRQSLYLCGQNMAVCMPFNSHEAMQRAKKNVEEHYAVVGTWEDTNT
FT TLSVLEGYIPRFFSGAKDQYYALRKSLGNYNRNTYRPSLSDKARAVLSQNLTREIELYQ
FT FVRHRLYKQYIALKLEEDPKLWD (in isoform 7)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_014071"
FT VAR_SEQ 106..405
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEA
FT AMQKAKRTVETE -> LGSLTPSQLNNTAKAEMDRLFFTRCAKVGSESLTEFMEHLQKI
FT NNFQVDKYGIMKKSKRQLKPRAQAETAGYIYNLDEGSVYIEHVPWIDFNEYNLPKPIFI
FT NLVRDPVERMISWYYYVRNSYRNAIFYRNNPLAPLKPTAWFKKSYNDCVRSGDPECQYV
FT PLAVRDVEGNFKRQTLFFCGHDQDCLPFNSPLAVQIAKRRVETEYAVVGTWEETNITLT
FT VLEHYIPRYFARAKMIFNLYQKSLQNRNRNNRKPHVDADVRAMVRRNFTHEYDFYYFCK
FT QRLYMQYIALKRTELERLNFS (in isoform 5)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_014073"
FT VAR_SEQ 106..403
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEA
FT AMQKAKRTVE -> LWRLNPKFLNNTKFHFRDIIFYNRVPKTGSETLIELMIQLGKKND
FT FQNERSPFSKPTGMYWDVKRQKQEATRILELQEEPAFVYVEHMNYMNIRPFHLPQPIYI
FT NMIRDPVERVISWFYYKRTPWNSVKMYKVTGKFQNRTHYTKNFEECVLTHDPECRYDYG
FT LLFKDDSADHKRQSLFFCGHSPICEPFNTPAAIARAKQNVERDFSVVGSWEDTNVTLTV
FT LEHYIPRFFKGTMELYYEPNIGLAFKKANINPWKPKISERIKQIMRANFTQEYEFYYFC
FT KQRLYRQYFAINKQLHF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11169845, ECO:0000303|Ref.5"
FT /id="VSP_014075"
FT VAR_SEQ 106..401
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEA
FT AMQKAKRT -> LGRVNPMHLNNTRFAGSETVIFNRPTRVDSEQMVPLFRQLAAMNDIN
FT VVLNGPVRTMNRTRTEKEELTEAEWTIELEKGSIYMAHSNWLDFASFGFKKPIYISLVK
FT DPIDRMITDFYKRRSRVKRAIYRRMYPGRRERPDEWYQLSFNECVRNRSPECLFVQHAV
FT ADYIQDFKRQTLYFCGNAADCLPFNSHHATQVAKRRVEKEYSVVGTWEERNITLTVLEK
FT YVPRFFNHARFLYKLHSKSIRNRNRNNRKPHIDADVREMVRRNFTNEYEFYYFCKQRLY
FT KQYLALQLENNLH (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_014077"
FT VAR_SEQ 106..397
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEA
FT AMQK -> LENLEPAHLNNTPKAERDFIFYNRLEKTGSQSMTRLIKQLGDRLGFDTYRN
FT IVRPSRSITESEEDEKDLVEQLFELGEHAVYVEHANWVNFTQHDSPRPIYINMVRHPIQ
FT KVISAYYYQRHPLIFAQSLLRNPNKPMQTKKFFDTNFNDCVRKRVRPHCVFDAHNPFNG
FT DWRRFSLHLCGNSEICTHFNSETTTQIAKMNVEREYAVVGSWEDTNVTLAVLEAYIPRF
FT FTDATKVYYSNTENFTINNVSHDTHLDKDVEEYLKSSFSFEIELYLFIKQRLYKQYIAV
FT HKNEF (in isoform 10)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_014079"
FT VAR_SEQ 106..358
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDF
FT VFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPK
FT PHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAI
FT PMPSEEFMNLDLDTCVRNHDPHCT -> LASLSSKKLNNTRHSRLEVIFFNRGAKVGSE
FT ALMELTQTMAPYNNMTVVTKGPMDIKSRTRSPKEQMIQAIWVTELEPGTIYIEHCNWLD
FT FRRYQLPRPIYINLVRDPVERMISWYYYVRSGYRNAIHHRRFPNATIKSEKWFKKSYND
FT CVRSGDPECQYVPGSIKDPEGNYKRQTLFFCGHSRECLPFDSQRAIQLAKLNVERDYAV
FT VGTWEETNITLTVFEAYIPRFFKGVRNIFECRFHYERFKNVSGTT (in isoform
FT 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_014081"
FT VAR_SEQ 106..205
FT /note="KVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDK
FT QLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADL -> LGRVNPM
FT HLNNTRFAGSETVIFNRPTRVDSEQMVPLFRQLAAMNDINVVLNGPVRTMNRTRTEKEE
FT LTEAEWTIELEKGSIYMAHSNWLDFASFGFKKPIYISLVKDPIDRMITDFYKRRSRVKR
FT AIYRRMYPGRRERPDEWYQLSFNECVRNRSPECLFVQHAVADYIQDFKRQTLYFCGNAA
FT DCL (in isoform 13)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_054034"
FT VAR_SEQ 106
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000305"
FT /id="VSP_054035"
FT VAR_SEQ 206..514
FT /note="Missing (in isoform 13)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_054036"
FT VAR_SEQ 359..514
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_014082"
FT VAR_SEQ 398..514
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_014080"
FT VAR_SEQ 402..514
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_014078"
FT VAR_SEQ 404..514
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11169845, ECO:0000303|Ref.5"
FT /id="VSP_014076"
FT VAR_SEQ 406..514
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_014074"
FT VAR_SEQ 407..514
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_014072"
FT VAR_SEQ 408..514
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_014070"
FT VAR_SEQ 414..514
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9827800"
FT /id="VSP_014068"
FT VAR_SEQ 419..514
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_014066"
FT CONFLICT Q86BJ3-2:401
FT /note="L -> M (in Ref. 2; AAK56855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 60260 MW; 84515CF230490F6B CRC64;
MSLNAERSYK MKLRDVENAF KYRRIPYPKR SVELIALLAI SCTFFLFMHT NKLNSRLKEM
EVKLQPSEFS ALGLTGNHIS GHDAGKHDDI NTLHGTYQYL KSTGQKVGYN VHDRRSSEEQ
LRTPTAHGHH HDHHSHHHHM HQQEKIDGHK HKASHDKQLA VPDNKHKEDE VHYEDDEDEV
EENDDDLAND VGTTDSEGFN FKADLLNNTK YAEVDFVFFN RVPKVGSQSL MELMARLGKI
NGFTHARNKG SAHETIVMNK QRQNDLIADL LTRPKPHIYS QHIAYINFTR FHLPKPIYIN
LIRDPIDRII SWHYYIRAPW YYRDMQAKLG ENAIPMPSEE FMNLDLDTCV RNHDPHCTFT
QMQIKNPVGD HRRQTLFFCG MNQKLCMPFN SEAAMQKAKR TVETEYAVVG TWEDTNITLS
VLEAYIPRYF RNAKVAYYLG KDRLSRVNRN NVTRIVSDET RLILRKNLTN EIEFYEFCKQ
RLYLQYAALS HGKRFGEDDY LLVPEQQNEY NEDY
