ID A0A0L8HVY6_OCTBM Unreviewed; 1183 AA.
AC A0A0L8HVY6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=OCBIM_22004589mg {ECO:0000313|EMBL:KOF93393.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF93393.1};
RN [1] {ECO:0000313|EMBL:KOF93393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF93393.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF93393.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KQ417182; KOF93393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8HVY6; -.
DR STRING; 37653.A0A0L8HVY6; -.
DR EnsemblMetazoa; Ocbimv22004590m; Ocbimv22004590m.p; Ocbimv22004589m.g.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProt.
DR CDD; cd00033; CCP; 7.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 7.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR19325:SF573; SUSHI DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF02494; HYR; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 6.
DR SMART; SM00032; CCP; 7.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 7.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50825; HYR; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 7.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..119
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 157..272
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 388..492
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 491..558
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 559..616
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 617..677
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 678..737
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 737..776
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 842..901
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 969..1032
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1033..1096
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1087..1176
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DISULFID 123..135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 130..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 142..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 619..662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 648..675
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 741..751
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 872..899
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1183 AA; 131636 MW; 04EFDDE5574CC4CB CRC64;
MCYHIVEKQM PWDLADDSCK SLHSNLVTID DYWTNMDISA AVKKKGHDEY WIGFNRLGVI
HSNETAYWGK DSPSNTQTGF WNNYQPNVDK GKCSAVSQSG QNYKWSFTKC DLAKVFVCEM
TACSKDTFRC NNGRCIGKQG LCDGTDNCWD LTDEVSCDQQ CQYYESGLNG LIKTKNFPND
YDNDTFCMWR IEADVGNFVK LTFNEFLTEN CTDVVEIFVG GDSETDSILL AKLSGNMPTN
TEYLSYNNKM LLKFTSDFEN TMKGFSANWI AVPTGYSHSM LTATENEQIL SFNDNKNLLH
NTWTITTKHR REIVSLIKQG MVLHDKDEVI VYDGDSVESP IIGQYKLTDF GTDGPDIIMS
TGPKLHILLK TRGIDSKVNV KFLYKQGCNT ITNNALSGEI VSPGFYAGIN FPNSVSCQWT
IASEASRGLI LKFIYKSDDD TLLVKYNNGS QIVEVNAVNV ADIEVPDGQV NVSFTTNSIK
NKKGFKAKYS VDCPALHLNQ FTTAQPPLNI WHQDSQVTIS CVNGYGFRDE KFVGNNSILL
ECQEGGKWSV QKIPKCLKNY CGPAKYIKNG FVFNATGAMV GDTVTYSCYP GYVISENKTI
MCTSNGTWET SPSCISSGCS DRSNITNGQV VIENGNGTTV GSVLRYSCDP GYHIEGNPLQ
LCLKSTFWTD EEPTCNKFNC TIIGLSDKIP EVNITQIEDV PYNETINISC NEGYNLTGPY
TIRCTENQTF SLSSCQDINE CNSHHKCEQI CINTPGSYKC QCAKGYTLKA DNSSCEDIDE
CQKSNGNCQH SCTNVNGSYT CNCDDGYVLY KENNTMSYAI PAAEDGTQFG DVFYLNHSCV
RVMCSNLLPL VNGFIQPQRK ISRYGDIFHY SCKIGYQLVG EKTSVCQYNG SWSQTQPRCE
EMKCQLDLLH TFVNKPTLLT NESIPYLGYL NFSCTILGKG TEYRQRQCLY DPATKTTKLL
GDSYECGFID CGPPMPIGGS NITTLKDTTY GSEFEMACSD MYTLKGNSSQ GNNIVRCESD
GKWDYGDLRC LGVMCEDPFF PVNGDVTVNT YALGGNASYK CNEDGYQPFP NSIRTCVANN
SKNGLIWSGE IPKCLDVKKP ILVAGTCTDS VTVKLYSLFN LTQPEFTDNS GKVRITVQPD
YISQNFVINN NFTVEYTATD DAGNNETCST SVIVEESPTL RPQ
//
