ID   SVEP1_HUMAN             Reviewed;        3571 AA.
AC   Q4LDE5; Q0P675; Q5D213; Q5T938; Q5VTE4; Q5VTE5; Q7Z387; Q7Z3G3; Q8NBT9;
AC   Q96JU7; Q9H284; Q9H8J9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1;
DE   AltName: Full=CCP module-containing protein 22;
DE   AltName: Full=Polydom;
DE   AltName: Full=Selectin-like osteoblast-derived protein;
DE            Short=SEL-OB;
DE   AltName: Full=Serologically defined breast cancer antigen NY-BR-38;
DE   Flags: Precursor;
GN   Name=SVEP1; Synonyms=C9orf13, CCP22, SELOB;
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), SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16206243; DOI=10.1002/jcp.20497;
RA   Shur I., Socher R., Hameiri M., Fried A., Benayahu D.;
RT   "Molecular and cellular characterization of SEL-OB/SVEP1 in osteogenic
RT   cells in vivo and in vitro.";
RL   J. Cell. Physiol. 206:420-427(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Mammary gland;
RA   Han J., Fang Y., Yan J., Ye Q.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 195-3571 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 318-868 (ISOFORM 2), AND VARIANTS ALA-332 AND VAL-2750.
RC   TISSUE=Placenta;
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=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2131-3571, AND VARIANT ILE-3161.
RC   TISSUE=Colon endothelium;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2269-2756.
RC   TISSUE=Mammary gland;
RX   PubMed=12747765;
RA   Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O.,
RA   Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.;
RT   "Humoral immunity to human breast cancer: antigen definition and
RT   quantitative analysis of mRNA expression.";
RL   Cancer Immun. 1:4-4(2001).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=11062057; DOI=10.1042/bj3520049;
RA   Gilges D., Vinit M.-A., Callebaut I., Coulombel L., Cacheux V.,
RA   Romeo P.-H., Vigon I.;
RT   "Polydom: a secreted protein with pentraxin, complement control protein,
RT   epidermal growth factor and von Willebrand factor A domains.";
RL   Biochem. J. 352:49-59(2000).
RN   [9]
RP   GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT   O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=27892606; DOI=10.1111/exd.13256;
RA   Samuelov L., Li Q., Bochner R., Najor N.A., Albrecht L., Malchin N.,
RA   Goldsmith T., Grafi-Cohen M., Vodo D., Fainberg G., Meilik B., Goldberg I.,
RA   Warshauer E., Rogers T., Edie S., Ishida-Yamamoto A., Burzenski L.,
RA   Erez N., Murray S.A., Irvine A.D., Shultz L., Green K.J., Uitto J.,
RA   Sprecher E., Sarig O.;
RT   "SVEP1 plays a crucial role in epidermal differentiation.";
RL   Exp. Dermatol. 26:423-430(2017).
RN   [11]
RP   FUNCTION, INTERACTION WITH ITGA4:ITGB1 AND ITGA9:ITGB1, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=35802072; DOI=10.1111/bph.15921;
RA   Morris G.E., Denniff M.J., Karamanavi E., Andrews S.A., Kostogrys R.B.,
RA   Bountziouka V., Ghaderi-Najafabadi M., Shamkhi N., McConnell G.,
RA   Kaiser M.A., Carleton L., Schofield C., Kessler T., Rainbow R.D.,
RA   Samani N.J., Webb T.R.;
RT   "The integrin ligand SVEP1 regulates GPCR-mediated vasoconstriction via
RT   integrins alpha9beta1 and alpha4beta1.";
RL   Br. J. Pharmacol. 179:4958-4973(2022).
RN   [12]
RP   INTERACTION WITH TIE1.
RX   PubMed=37097004; DOI=10.7554/elife.82969;
RA   Hussmann M., Schulte D., Weischer S., Carlantoni C., Nakajima H.,
RA   Mochizuki N., Stainier D.Y.R., Zobel T., Koch M., Schulte-Merker S.;
RT   "Svep1 is a binding ligand of Tie1 and affects specific aspects of facial
RT   lymphatic development in a Vegfc-independent manner.";
RL   Elife 12:0-0(2023).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH PEAR1.
RX   PubMed=36792666; DOI=10.1038/s41467-023-36486-0;
RA   Elenbaas J.S., Pudupakkam U., Ashworth K.J., Kang C.J., Patel V.,
RA   Santana K., Jung I.H., Lee P.C., Burks K.H., Amrute J.M., Mecham R.P.,
RA   Halabi C.M., Alisio A., Di Paola J., Stitziel N.O.;
RT   "SVEP1 is an endogenous ligand for the orphan receptor PEAR1.";
RL   Nat. Commun. 14:850-850(2023).
CC   -!- FUNCTION: Required for morphological development, cell alignment and
CC       migration of lymphatic endothelial cells during embryonic development,
CC       potentially via modulation of ANGPT2-TIE1 signaling and subsequent
CC       activation of FOXC2 transcription (By similarity). Required for
CC       embryonic lymphatic vascular development, via mediating the correct
CC       formation of the first lymphovenous contact site and tight association
CC       of the lymphatic endothelium with the venous endothelium (By
CC       similarity). Represses PRKCA-mediated L-type voltage-gated channel
CC       Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth
CC       muscle cells, via its interaction with integrins, thereby inhibiting
CC       vasocontraction (PubMed:35802072). Promotes platelet activation, via
CC       its interaction with PEAR1 and subsequent activation of AKT/mTOR
CC       signaling (PubMed:36792666). Plays a role in epidermal development and
CC       keratinocyte differentiation, independent of cell-cell adhesion
CC       (PubMed:27892606). May play a role in initial cell attachment of
CC       stromal osteogenic cells (By similarity). May promote myoblast cell
CC       adhesion when in the presence of integrin ITGA9:ITGB1 (By similarity).
CC       {ECO:0000250|UniProtKB:A2AVA0, ECO:0000269|PubMed:27892606,
CC       ECO:0000269|PubMed:35802072, ECO:0000269|PubMed:36792666}.
CC   -!- SUBUNIT: Interacts (via Sushi domain 21) with ITGA9:ITGB1; thereby
CC       inhibits Ca(2+) intracellular signaling and as a result represses
CC       vasocontraction (PubMed:35802072). Interacts (via Sushi domain 21) with
CC       ITGA4:ITGB1; thereby inhibits Ca(2+) intracellular signaling and as a
CC       result represses vasocontraction (PubMed:35802072). Interacts with
CC       ANGPT1 and ANGPT2 (By similarity). Interacts with PEAR1 (via
CC       extracellular domain) (PubMed:36792666). Interacts with HSPG2, TLN1,
CC       FN1, COPA, CCT2, IQGAP1, LAMC1 and NID1 (By similarity). Interacts (via
CC       C-terminus) with TIE1 (PubMed:37097004). {ECO:0000250|UniProtKB:A2AVA0,
CC       ECO:0000269|PubMed:35802072, ECO:0000269|PubMed:36792666,
CC       ECO:0000269|PubMed:37097004}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A2AVA0}. Nucleus
CC       {ECO:0000269|PubMed:27892606}. Cytoplasm {ECO:0000269|PubMed:16206243,
CC       ECO:0000269|PubMed:27892606}. Membrane {ECO:0000269|PubMed:16206243};
CC       Peripheral membrane protein {ECO:0000269|PubMed:16206243}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q4LDE5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4LDE5-2; Sequence=VSP_031626, VSP_031627;
CC       Name=3;
CC         IsoId=Q4LDE5-3; Sequence=VSP_031625;
CC       Name=4;
CC         IsoId=Q4LDE5-4; Sequence=VSP_031628;
CC   -!- TISSUE SPECIFICITY: Expressed in mesenchymal cells (at protein level)
CC       (PubMed:16206243). Expressed in vascular smooth muscle cells (at
CC       protein level) (PubMed:35802072). Expressed throughout the epidermis,
CC       expression is most prominent in the basal and lower suprabasal layers
CC       of the epidermis and in dermal fibroblasts in the upper dermis (at
CC       protein level) (PubMed:27892606). Abundantly expressed in the placenta,
CC       weakly expressed in heart and skeletal muscle (PubMed:11062057,
CC       PubMed:27892606). Also expressed in the lung, adrenal gland and
CC       cerebellum (PubMed:27892606). {ECO:0000269|PubMed:11062057,
CC       ECO:0000269|PubMed:16206243, ECO:0000269|PubMed:27892606,
CC       ECO:0000269|PubMed:35802072}.
CC   -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans.
CC       {ECO:0000269|PubMed:22171320}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG48257.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAG48257.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB14617.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55420.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ619977; CAF04067.1; -; mRNA.
DR   EMBL; AY916667; AAX12481.1; -; mRNA.
DR   EMBL; AK023591; BAB14617.1; ALT_INIT; mRNA.
DR   EMBL; AK075235; BAC11489.1; -; mRNA.
DR   EMBL; AK027870; BAB55420.1; ALT_INIT; mRNA.
DR   EMBL; AL158158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL592463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030816; AAH30816.1; -; mRNA.
DR   EMBL; BX537918; CAD97901.1; -; mRNA.
DR   EMBL; BX538049; CAD97988.1; -; mRNA.
DR   EMBL; AF308289; AAG48257.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS48004.1; -. [Q4LDE5-1]
DR   RefSeq; NP_699197.3; NM_153366.3. [Q4LDE5-1]
DR   BioGRID; 123051; 9.
DR   IntAct; Q4LDE5; 15.
DR   MINT; Q4LDE5; -.
DR   STRING; 9606.ENSP00000363593; -.
DR   GlyConnect; 1781; 17 N-Linked glycans (9 sites).
DR   GlyCosmos; Q4LDE5; 17 sites, 19 glycans.
DR   GlyGen; Q4LDE5; 21 sites, 16 N-linked glycans (8 sites), 3 O-linked glycans (10 sites).
DR   iPTMnet; Q4LDE5; -.
DR   PhosphoSitePlus; Q4LDE5; -.
DR   BioMuta; SVEP1; -.
DR   DMDM; 296452942; -.
DR   EPD; Q4LDE5; -.
DR   jPOST; Q4LDE5; -.
DR   MassIVE; Q4LDE5; -.
DR   MaxQB; Q4LDE5; -.
DR   PaxDb; 9606-ENSP00000384917; -.
DR   PeptideAtlas; Q4LDE5; -.
DR   ProteomicsDB; 62229; -. [Q4LDE5-1]
DR   ProteomicsDB; 62230; -. [Q4LDE5-2]
DR   ProteomicsDB; 62231; -. [Q4LDE5-3]
DR   ProteomicsDB; 62232; -. [Q4LDE5-4]
DR   Antibodypedia; 7229; 19 antibodies from 8 providers.
DR   DNASU; 79987; -.
DR   Ensembl; ENST00000374461.1; ENSP00000363585.2; ENSG00000165124.19. [Q4LDE5-2]
DR   Ensembl; ENST00000374469.6; ENSP00000363593.2; ENSG00000165124.19. [Q4LDE5-1]
DR   GeneID; 79987; -.
DR   KEGG; hsa:79987; -.
DR   MANE-Select; ENST00000374469.6; ENSP00000363593.2; NM_153366.4; NP_699197.3.
DR   UCSC; uc010mtz.4; human. [Q4LDE5-1]
DR   AGR; HGNC:15985; -.
DR   CTD; 79987; -.
DR   DisGeNET; 79987; -.
DR   GeneCards; SVEP1; -.
DR   HGNC; HGNC:15985; SVEP1.
DR   HPA; ENSG00000165124; Tissue enhanced (adipose tissue, placenta).
DR   MIM; 611691; gene.
DR   neXtProt; NX_Q4LDE5; -.
DR   OpenTargets; ENSG00000165124; -.
DR   PharmGKB; PA25971; -.
DR   VEuPathDB; HostDB:ENSG00000165124; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000156061; -.
DR   HOGENOM; CLU_000343_0_0_1; -.
DR   InParanoid; Q4LDE5; -.
DR   OMA; RLCLQNK; -.
DR   OrthoDB; 2880384at2759; -.
DR   PhylomeDB; Q4LDE5; -.
DR   TreeFam; TF342247; -.
DR   PathwayCommons; Q4LDE5; -.
DR   SignaLink; Q4LDE5; -.
DR   BioGRID-ORCS; 79987; 9 hits in 1110 CRISPR screens.
DR   ChiTaRS; SVEP1; human.
DR   GenomeRNAi; 79987; -.
DR   Pharos; Q4LDE5; Tbio.
DR   PRO; PR:Q4LDE5; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q4LDE5; Protein.
DR   Bgee; ENSG00000165124; Expressed in pericardium and 167 other cell types or tissues.
DR   ExpressionAtlas; Q4LDE5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0098640; F:integrin binding involved in cell-matrix adhesion; ISS:UniProtKB.
DR   GO; GO:0008544; P:epidermis development; IBA:GO_Central.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0003017; P:lymph circulation; IEA:Ensembl.
DR   GO; GO:0036303; P:lymph vessel morphogenesis; IBA:GO_Central.
DR   GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR   GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:UniProtKB.
DR   GO; GO:0010572; P:positive regulation of platelet activation; IMP:UniProtKB.
DR   GO; GO:0048014; P:Tie signaling pathway; IEA:Ensembl.
DR   GO; GO:0120193; P:tight junction organization; IEA:Ensembl.
DR   CDD; cd00033; CCP; 32.
DR   CDD; cd00054; EGF_CA; 8.
DR   CDD; cd01450; vWFA_subfamily_ECM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 33.
DR   Gene3D; 2.10.25.10; Laminin; 10.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR003410; HYR_dom.
DR   InterPro; IPR001759; Pentraxin-related.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR19325:SF573; SUSHI DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00008; EGF; 6.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF07699; Ephrin_rec_like; 4.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF02494; HYR; 2.
DR   Pfam; PF00354; Pentaxin; 1.
DR   Pfam; PF00084; Sushi; 33.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM00032; CCP; 34.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00179; EGF_CA; 8.
DR   SMART; SM01411; Ephrin_rec_like; 4.
DR   SMART; SM00159; PTX; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 33.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 6.
DR   PROSITE; PS00022; EGF_1; 9.
DR   PROSITE; PS01186; EGF_2; 11.
DR   PROSITE; PS50026; EGF_3; 9.
DR   PROSITE; PS01187; EGF_CA; 6.
DR   PROSITE; PS50825; HYR; 2.
DR   PROSITE; PS51828; PTX_2; 1.
DR   PROSITE; PS50923; SUSHI; 34.
DR   PROSITE; PS50234; VWFA; 1.
DR   Genevisible; Q4LDE5; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cytoplasm; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Nucleus; Reference proteome;
KW   Repeat; Secreted; Signal; Sushi.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..3571
FT                   /note="Sushi, von Willebrand factor type A, EGF and
FT                   pentraxin domain-containing protein 1"
FT                   /id="PRO_0000320179"
FT   DOMAIN          83..264
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          376..435
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          436..495
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          496..561
FT                   /note="Sushi 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          560..642
FT                   /note="HYR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT   DOMAIN          643..724
FT                   /note="HYR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT   DOMAIN          725..789
FT                   /note="Sushi 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          1193..1229
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1231..1267
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1269..1305
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1307..1343
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1345..1381
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1383..1419
FT                   /note="EGF-like 6; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1424..1628
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   DOMAIN          1629..1687
FT                   /note="Sushi 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          1688..1745
FT                   /note="Sushi 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          1745..1784
FT                   /note="EGF-like 7; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1787..1844
FT                   /note="Sushi 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          1845..1902
FT                   /note="Sushi 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          1903..1960
FT                   /note="Sushi 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          1961..2018
FT                   /note="Sushi 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2019..2080
FT                   /note="Sushi 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2081..2143
FT                   /note="Sushi 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2144..2201
FT                   /note="Sushi 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2202..2261
FT                   /note="Sushi 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2262..2320
FT                   /note="Sushi 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2321..2378
FT                   /note="Sushi 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2379..2437
FT                   /note="Sushi 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2438..2495
FT                   /note="Sushi 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2496..2553
FT                   /note="Sushi 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2554..2610
FT                   /note="Sushi 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2663..2714
FT                   /note="Sushi 21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2715..2772
FT                   /note="Sushi 22"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2773..2830
FT                   /note="Sushi 23"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2831..2888
FT                   /note="Sushi 24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2889..2946
FT                   /note="Sushi 25"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          2947..3004
FT                   /note="Sushi 26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3005..3061
FT                   /note="Sushi 27"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3062..3119
FT                   /note="Sushi 28"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3120..3178
FT                   /note="Sushi 29"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3179..3238
FT                   /note="Sushi 30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3239..3296
FT                   /note="Sushi 31"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3297..3354
FT                   /note="Sushi 32"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3355..3413
FT                   /note="Sushi 33"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3414..3470
FT                   /note="Sushi 34"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          3500..3532
FT                   /note="EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          3533..3564
FT                   /note="EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          887..894
FT                   /note="O-glycosylated at one site"
FT   REGION          2639..2646
FT                   /note="Important for the interaction with integrin
FT                   ITGA9:ITGB1"
FT                   /evidence="ECO:0000250|UniProtKB:A2AVA0"
FT   MOTIF           2845..2847
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   SITE            2642
FT                   /note="Required for interaction with integrin ITGA9:ITGB1"
FT                   /evidence="ECO:0000250|UniProtKB:A2AVA0"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        847
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3018
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        378..420
FT                   /evidence="ECO:0000250"
FT   DISULFID        406..433
FT                   /evidence="ECO:0000250"
FT   DISULFID        438..480
FT                   /evidence="ECO:0000250"
FT   DISULFID        466..493
FT                   /evidence="ECO:0000250"
FT   DISULFID        498..544
FT                   /evidence="ECO:0000250"
FT   DISULFID        529..559
FT                   /evidence="ECO:0000250"
FT   DISULFID        727..769
FT                   /evidence="ECO:0000250"
FT   DISULFID        753..787
FT                   /evidence="ECO:0000250"
FT   DISULFID        1197..1208
FT                   /evidence="ECO:0000250"
FT   DISULFID        1202..1217
FT                   /evidence="ECO:0000250"
FT   DISULFID        1219..1228
FT                   /evidence="ECO:0000250"
FT   DISULFID        1235..1246
FT                   /evidence="ECO:0000250"
FT   DISULFID        1240..1255
FT                   /evidence="ECO:0000250"
FT   DISULFID        1257..1266
FT                   /evidence="ECO:0000250"
FT   DISULFID        1273..1284
FT                   /evidence="ECO:0000250"
FT   DISULFID        1278..1293
FT                   /evidence="ECO:0000250"
FT   DISULFID        1295..1304
FT                   /evidence="ECO:0000250"
FT   DISULFID        1311..1322
FT                   /evidence="ECO:0000250"
FT   DISULFID        1316..1331
FT                   /evidence="ECO:0000250"
FT   DISULFID        1333..1342
FT                   /evidence="ECO:0000250"
FT   DISULFID        1349..1360
FT                   /evidence="ECO:0000250"
FT   DISULFID        1354..1369
FT                   /evidence="ECO:0000250"
FT   DISULFID        1371..1380
FT                   /evidence="ECO:0000250"
FT   DISULFID        1387..1398
FT                   /evidence="ECO:0000250"
FT   DISULFID        1392..1407
FT                   /evidence="ECO:0000250"
FT   DISULFID        1409..1418
FT                   /evidence="ECO:0000250"
FT   DISULFID        1631..1672
FT                   /evidence="ECO:0000250"
FT   DISULFID        1658..1685
FT                   /evidence="ECO:0000250"
FT   DISULFID        1690..1730
FT                   /evidence="ECO:0000250"
FT   DISULFID        1716..1743
FT                   /evidence="ECO:0000250"
FT   DISULFID        1749..1761
FT                   /evidence="ECO:0000250"
FT   DISULFID        1755..1770
FT                   /evidence="ECO:0000250"
FT   DISULFID        1772..1783
FT                   /evidence="ECO:0000250"
FT   DISULFID        1789..1829
FT                   /evidence="ECO:0000250"
FT   DISULFID        1815..1842
FT                   /evidence="ECO:0000250"
FT   DISULFID        1847..1887
FT                   /evidence="ECO:0000250"
FT   DISULFID        1873..1900
FT                   /evidence="ECO:0000250"
FT   DISULFID        1905..1945
FT                   /evidence="ECO:0000250"
FT   DISULFID        1931..1958
FT                   /evidence="ECO:0000250"
FT   DISULFID        1963..2003
FT                   /evidence="ECO:0000250"
FT   DISULFID        1989..2016
FT                   /evidence="ECO:0000250"
FT   DISULFID        2021..2061
FT                   /evidence="ECO:0000250"
FT   DISULFID        2047..2078
FT                   /evidence="ECO:0000250"
FT   DISULFID        2083..2126
FT                   /evidence="ECO:0000250"
FT   DISULFID        2112..2141
FT                   /evidence="ECO:0000250"
FT   DISULFID        2146..2186
FT                   /evidence="ECO:0000250"
FT   DISULFID        2172..2199
FT                   /evidence="ECO:0000250"
FT   DISULFID        2204..2245
FT                   /evidence="ECO:0000250"
FT   DISULFID        2231..2259
FT                   /evidence="ECO:0000250"
FT   DISULFID        2264..2304
FT                   /evidence="ECO:0000250"
FT   DISULFID        2290..2318
FT                   /evidence="ECO:0000250"
FT   DISULFID        2323..2363
FT                   /evidence="ECO:0000250"
FT   DISULFID        2349..2376
FT                   /evidence="ECO:0000250"
FT   DISULFID        2381..2422
FT                   /evidence="ECO:0000250"
FT   DISULFID        2408..2435
FT                   /evidence="ECO:0000250"
FT   DISULFID        2440..2480
FT                   /evidence="ECO:0000250"
FT   DISULFID        2466..2493
FT                   /evidence="ECO:0000250"
FT   DISULFID        2498..2538
FT                   /evidence="ECO:0000250"
FT   DISULFID        2524..2551
FT                   /evidence="ECO:0000250"
FT   DISULFID        2556..2596
FT                   /evidence="ECO:0000250"
FT   DISULFID        2582..2608
FT                   /evidence="ECO:0000250"
FT   DISULFID        2685..2712
FT                   /evidence="ECO:0000250"
FT   DISULFID        2717..2757
FT                   /evidence="ECO:0000250"
FT   DISULFID        2743..2770
FT                   /evidence="ECO:0000250"
FT   DISULFID        2775..2815
FT                   /evidence="ECO:0000250"
FT   DISULFID        2801..2828
FT                   /evidence="ECO:0000250"
FT   DISULFID        2833..2873
FT                   /evidence="ECO:0000250"
FT   DISULFID        2859..2886
FT                   /evidence="ECO:0000250"
FT   DISULFID        2891..2931
FT                   /evidence="ECO:0000250"
FT   DISULFID        2917..2944
FT                   /evidence="ECO:0000250"
FT   DISULFID        2949..2989
FT                   /evidence="ECO:0000250"
FT   DISULFID        2975..3002
FT                   /evidence="ECO:0000250"
FT   DISULFID        3007..3046
FT                   /evidence="ECO:0000250"
FT   DISULFID        3032..3059
FT                   /evidence="ECO:0000250"
FT   DISULFID        3064..3104
FT                   /evidence="ECO:0000250"
FT   DISULFID        3090..3117
FT                   /evidence="ECO:0000250"
FT   DISULFID        3122..3163
FT                   /evidence="ECO:0000250"
FT   DISULFID        3148..3176
FT                   /evidence="ECO:0000250"
FT   DISULFID        3181..3221
FT                   /evidence="ECO:0000250"
FT   DISULFID        3207..3236
FT                   /evidence="ECO:0000250"
FT   DISULFID        3241..3281
FT                   /evidence="ECO:0000250"
FT   DISULFID        3267..3294
FT                   /evidence="ECO:0000250"
FT   DISULFID        3299..3339
FT                   /evidence="ECO:0000250"
FT   DISULFID        3325..3352
FT                   /evidence="ECO:0000250"
FT   DISULFID        3384..3411
FT                   /evidence="ECO:0000250"
FT   DISULFID        3416..3456
FT                   /evidence="ECO:0000250"
FT   DISULFID        3442..3468
FT                   /evidence="ECO:0000250"
FT   DISULFID        3504..3514
FT                   /evidence="ECO:0000250"
FT   DISULFID        3508..3520
FT                   /evidence="ECO:0000250"
FT   DISULFID        3522..3531
FT                   /evidence="ECO:0000250"
FT   DISULFID        3536..3546
FT                   /evidence="ECO:0000250"
FT   DISULFID        3540..3552
FT                   /evidence="ECO:0000250"
FT   DISULFID        3554..3563
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..2074
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT                   /id="VSP_031625"
FT   VAR_SEQ         868
FT                   /note="P -> N (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031626"
FT   VAR_SEQ         869..3571
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031627"
FT   VAR_SEQ         1547..3571
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031628"
FT   VARIANT         332
FT                   /note="G -> A (in dbSNP:rs3818764)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_039153"
FT   VARIANT         428
FT                   /note="G -> S (in dbSNP:rs10980419)"
FT                   /id="VAR_039154"
FT   VARIANT         507
FT                   /note="V -> I (in dbSNP:rs872665)"
FT                   /id="VAR_039155"
FT   VARIANT         581
FT                   /note="Q -> H (in dbSNP:rs10817033)"
FT                   /id="VAR_039156"
FT   VARIANT         637
FT                   /note="I -> V (in dbSNP:rs13286541)"
FT                   /id="VAR_039157"
FT   VARIANT         899
FT                   /note="K -> R (in dbSNP:rs10817025)"
FT                   /id="VAR_039158"
FT   VARIANT         1157
FT                   /note="I -> V (in dbSNP:rs7038903)"
FT                   /id="VAR_039159"
FT   VARIANT         1330
FT                   /note="L -> M (in dbSNP:rs10817021)"
FT                   /id="VAR_039160"
FT   VARIANT         1416
FT                   /note="K -> Q (in dbSNP:rs1889323)"
FT                   /id="VAR_039161"
FT   VARIANT         1444
FT                   /note="M -> L (in dbSNP:rs7863519)"
FT                   /id="VAR_039162"
FT   VARIANT         1648
FT                   /note="L -> V (in dbSNP:rs7852962)"
FT                   /id="VAR_039163"
FT   VARIANT         1810
FT                   /note="E -> A (in dbSNP:rs2986671)"
FT                   /id="VAR_039164"
FT   VARIANT         1953
FT                   /note="R -> K (in dbSNP:rs17204832)"
FT                   /id="VAR_039165"
FT   VARIANT         2607
FT                   /note="T -> A (in dbSNP:rs3802433)"
FT                   /id="VAR_039166"
FT   VARIANT         2750
FT                   /note="A -> V (in dbSNP:rs7030192)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_039167"
FT   VARIANT         2922
FT                   /note="I -> V (in dbSNP:rs16914996)"
FT                   /id="VAR_039168"
FT   VARIANT         3161
FT                   /note="F -> I (in dbSNP:rs3739451)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_039169"
FT   VARIANT         3230
FT                   /note="P -> T (in dbSNP:rs16914992)"
FT                   /id="VAR_039170"
FT   VARIANT         3559
FT                   /note="T -> M (in dbSNP:rs17204533)"
FT                   /id="VAR_039171"
FT   CONFLICT        429
FT                   /note="S -> L (in Ref. 1; CAF04067 and 3; BAB55420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        604
FT                   /note="H -> R (in Ref. 3; BAB14617)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        822
FT                   /note="F -> L (in Ref. 3; BAB14617)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        842
FT                   /note="C -> W (in Ref. 1; CAF04067 and 3; BAB55420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        980
FT                   /note="E -> G (in Ref. 1; CAF04067 and 3; BAB55420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1063
FT                   /note="Y -> C (in Ref. 1; CAF04067 and 3; BAB55420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1442
FT                   /note="D -> V (in Ref. 1; CAF04067 and 3; BAB55420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1546
FT                   /note="P -> PGMF (in Ref. 1; CAF04067)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1775
FT                   /note="P -> S (in Ref. 1; CAF04067)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2179
FT                   /note="K -> E (in Ref. 6; CAD97901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2189
FT                   /note="T -> S (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2237
FT                   /note="S -> P (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2246
FT                   /note="Q -> H (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2259
FT                   /note="C -> W (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2299
FT                   /note="D -> G (in Ref. 6; CAD97988)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2454
FT                   /note="Q -> R (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2519
FT                   /note="T -> I (in Ref. 6; CAD97901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2623
FT                   /note="D -> A (in Ref. 7; AAG48257)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2705
FT                   /note="W -> R (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2753
FT                   /note="D -> G (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2833
FT                   /note="C -> R (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2857
FT                   /note="Y -> H (in Ref. 6; CAD97901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3005
FT                   /note="C -> F (in Ref. 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3186
FT                   /note="N -> S (in Ref. 6; CAD97988)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3302
FT                   /note="P -> Q (in Ref. 1; CAF04067 and 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3398
FT                   /note="C -> Y (in Ref. 1; CAF04067 and 3; BAC11489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3565
FT                   /note="R -> G (in Ref. 6; CAD97988)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3567
FT                   /note="R -> G (in Ref. 6; CAD97988)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3571 AA;  390170 MW;  8F52DE456CED5DED CRC64;
     MWPRLAFCCW GLALVSGWAT FQQMSPSRNF SFRLFPETAP GAPGSIPAPP APGDEAAGSR
     VERLGQAFRR RVRLLRELSE RLELVFLVDD SSSVGEVNFR SELMFVRKLL SDFPVVPTAT
     RVAIVTFSSK NYVVPRVDYI STRRARQHKC ALLLQEIPAI SYRGGGTYTK GAFQQAAQIL
     LHARENSTKV VFLITDGYSN GGDPRPIAAS LRDSGVEIFT FGIWQGNIRE LNDMASTPKE
     EHCYLLHSFE EFEALARRAL HEDLPSGSFI QDDMVHCSYL CDEGKDCCDR MGSCKCGTHT
     GHFECICEKG YYGKGLQYEC TACPSGTYKP EGSPGGISSC IPCPDENHTS PPGSTSPEDC
     VCREGYRASG QTCELVHCPA LKPPENGYFI QNTCNNHFNA ACGVRCHPGF DLVGSSIILC
     LPNGLWSGSE SYCRVRTCPH LRQPKHGHIS CSTREMLYKT TCLVACDEGY RLEGSDKLTC
     QGNSQWDGPE PRCVERHCST FQMPKDVIIS PHNCGKQPAK FGTICYVSCR QGFILSGVKE
     MLRCTTSGKW NVGVQAAVCK DVEAPQINCP KDIEAKTLEQ QDSANVTWQI PTAKDNSGEK
     VSVHVHPAFT PPYLFPIGDV AIVYTATDLS GNQASCIFHI KVIDAEPPVI DWCRSPPPVQ
     VSEKVHAASW DEPQFSDNSG AELVITRSHT QGDLFPQGET IVQYTATDPS GNNRTCDIHI
     VIKGSPCEIP FTPVNGDFIC TPDNTGVNCT LTCLEGYDFT EGSTDKYYCA YEDGVWKPTY
     TTEWPDCAKK RFANHGFKSF EMFYKAARCD DTDLMKKFSE AFETTLGKMV PSFCSDAEDI
     DCRLEENLTK KYCLEYNYDY ENGFAIGPGG WGAANRLDYS YDDFLDTVQE TATSIGNAKS
     SRIKRSAPLS DYKIKLIFNI TASVPLPDER NDTLEWENQQ RLLQTLETIT NKLKRTLNKD
     PMYSFQLASE ILIADSNSLE TKKASPFCRP GSVLRGRMCV NCPLGTYYNL EHFTCESCRI
     GSYQDEEGQL ECKLCPSGMY TEYIHSRNIS DCKAQCKQGT YSYSGLETCE SCPLGTYQPK
     FGSRSCLSCP ENTSTVKRGA VNISACGVPC PEGKFSRSGL MPCHPCPRDY YQPNAGKAFC
     LACPFYGTTP FAGSRSITEC SSFSSTFSAA EESVVPPASL GHIKKRHEIS SQVFHECFFN
     PCHNSGTCQQ LGRGYVCLCP LGYTGLKCET DIDECSPLPC LNNGVCKDLV GEFICECPSG
     YTGQRCEENI NECSSSPCLN KGICVDGVAG YRCTCVKGFV GLHCETEVNE CQSNPCLNNA
     VCEDQVGGFL CKCPPGFLGT RCGKNVDECL SQPCKNGATC KDGANSFRCL CAAGFTGSHC
     ELNINECQSN PCRNQATCVD ELNSYSCKCQ PGFSGKRCET EQSTGFNLDF EVSGIYGYVM
     LDGMLPSLHA LTCTFWMKSS DDMNYGTPIS YAVDNGSDNT LLLTDYNGWV LYVNGREKIT
     NCPSVNDGRW HHIAITWTSA NGIWKVYIDG KLSDGGAGLS VGLPIPGGGA LVLGQEQDKK
     GEGFSPAESF VGSISQLNLW DYVLSPQQVK SLATSCPEEL SKGNVLAWPD FLSGIVGKVK
     IDSKSIFCSD CPRLGGSVPH LRTASEDLKP GSKVNLFCDP GFQLVGNPVQ YCLNQGQWTQ
     PLPHCERISC GVPPPLENGF HSADDFYAGS TVTYQCNNGY YLLGDSRMFC TDNGSWNGVS
     PSCLDVDECA VGSDCSEHAS CLNVDGSYIC SCVPPYTGDG KNCAEPIKCK APGNPENGHS
     SGEIYTVGAE VTFSCQEGYQ LMGVTKITCL ESGEWNHLIP YCKAVSCGKP AIPENGCIEE
     LAFTFGSKVT YRCNKGYTLA GDKESSCLAN SSWSHSPPVC EPVKCSSPEN INNGKYILSG
     LTYLSTASYS CDTGYSLQGP SIIECTASGI WDRAPPACHL VFCGEPPAIK DAVITGNNFT
     FRNTVTYTCK EGYTLAGLDT IECLADGKWS RSDQQCLAVS CDEPPIVDHA SPETAHRLFG
     DIAFYYCSDG YSLADNSQLL CNAQGKWVPP EGQDMPRCIA HFCEKPPSVS YSILESVSKA
     KFAAGSVVSF KCMEGFVLNT SAKIECMRGG QWNPSPMSIQ CIPVRCGEPP SIMNGYASGS
     NYSFGAMVAY SCNKGFYIKG EKKSTCEATG QWSSPIPTCH PVSCGEPPKV ENGFLEHTTG
     RIFESEVRYQ CNPGYKSVGS PVFVCQANRH WHSESPLMCV PLDCGKPPPI QNGFMKGENF
     EVGSKVQFFC NEGYELVGDS SWTCQKSGKW NKKSNPKCMP AKCPEPPLLE NQLVLKELTT
     EVGVVTFSCK EGHVLQGPSV LKCLPSQQWN DSFPVCKIVL CTPPPLISFG VPIPSSALHF
     GSTVKYSCVG GFFLRGNSTT LCQPDGTWSS PLPECVPVEC PQPEEIPNGI IDVQGLAYLS
     TALYTCKPGF ELVGNTTTLC GENGHWLGGK PTCKAIECLK PKEILNGKFS YTDLHYGQTV
     TYSCNRGFRL EGPSALTCLE TGDWDVDAPS CNAIHCDSPQ PIENGFVEGA DYSYGAIIIY
     SCFPGFQVAG HAMQTCEESG WSSSIPTCMP IDCGLPPHID FGDCTKLKDD QGYFEQEDDM
     MEVPYVTPHP PYHLGAVAKT WENTKESPAT HSSNFLYGTM VSYTCNPGYE LLGNPVLICQ
     EDGTWNGSAP SCISIECDLP TAPENGFLRF TETSMGSAVQ YSCKPGHILA GSDLRLCLEN
     RKWSGASPRC EAISCKKPNP VMNGSIKGSN YTYLSTLYYE CDPGYVLNGT ERRTCQDDKN
     WDEDEPICIP VDCSSPPVSA NGQVRGDEYT FQKEIEYTCN EGFLLEGARS RVCLANGSWS
     GATPDCVPVR CATPPQLANG VTEGLDYGFM KEVTFHCHEG YILHGAPKLT CQSDGNWDAE
     IPLCKPVNCG PPEDLAHGFP NGFSFIHGGH IQYQCFPGYK LHGNSSRRCL SNGSWSGSSP
     SCLPCRCSTP VIEYGTVNGT DFDCGKAARI QCFKGFKLLG LSEITCEADG QWSSGFPHCE
     HTSCGSLPMI PNAFISETSS WKENVITYSC RSGYVIQGSS DLICTEKGVW SQPYPVCEPL
     SCGSPPSVAN AVATGEAHTY ESEVKLRCLE GYTMDTDTDT FTCQKDGRWF PERISCSPKK
     CPLPENITHI LVHGDDFSVN RQVSVSCAEG YTFEGVNISV CQLDGTWEPP FSDESCSPVS
     CGKPESPEHG FVVGSKYTFE STIIYQCEPG YELEGNRERV CQENRQWSGG VAICKETRCE
     TPLEFLNGKA DIENRTTGPN VVYSCNRGYS LEGPSEAHCT ENGTWSHPVP LCKPNPCPVP
     FVIPENALLS EKEFYVDQNV SIKCREGFLL QGHGIITCNP DETWTQTSAK CEKISCGPPA
     HVENAIARGV HYQYGDMITY SCYSGYMLEG FLRSVCLENG TWTSPPICRA VCRFPCQNGG
     ICQRPNACSC PEGWMGRLCE EPICILPCLN GGRCVAPYQC DCPPGWTGSR CHTAVCQSPC
     LNGGKCVRPN RCHCLSSWTG HNCSRKRRTG F
//