ID A0A3M7SL94_BRAPC Unreviewed; 2903 AA.
AC A0A3M7SL94;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=SCO-spondin {ECO:0000313|EMBL:RNA36465.1};
DE Flags: Fragment;
GN ORFNames=BpHYR1_045060 {ECO:0000313|EMBL:RNA36465.1};
OS Brachionus plicatilis (Marine rotifer) (Brachionus muelleri).
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Monogononta; Pseudotrocha; Ploima; Brachionidae; Brachionus.
OX NCBI_TaxID=10195 {ECO:0000313|EMBL:RNA36465.1, ECO:0000313|Proteomes:UP000276133};
RN [1] {ECO:0000313|EMBL:RNA36465.1, ECO:0000313|Proteomes:UP000276133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYR1 {ECO:0000313|EMBL:RNA36465.1};
RX PubMed=30375419; DOI=10.1038/s41598-018-34188-y;
RA Franch-Gras L., Hahn C., Garcia-Roger E.M., Carmona M.J., Serra M.,
RA Gomez A.;
RT "Genomic signatures of local adaptation to the degree of environmental
RT predictability in rotifers.";
RL Sci. Rep. 8:16051-16051(2018).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RNA36465.1}.
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; REGN01001180; RNA36465.1; -; Genomic_DNA.
DR STRING; 10195.A0A3M7SL94; -.
DR Proteomes; UP000276133; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 6.
DR CDD; cd19941; TIL; 4.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1.
DR PANTHER; PTHR11339:SF373; HEMOLECTIN, ISOFORM A; 1.
DR Pfam; PF08742; C8; 3.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF01826; TIL; 2.
DR Pfam; PF00094; VWD; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00832; C8; 3.
DR SMART; SM00192; LDLa; 5.
DR SMART; SM00214; VWC; 2.
DR SMART; SM00215; VWC_out; 3.
DR SMART; SM00216; VWD; 3.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 5.
DR SUPFAM; SSF57567; Serine protease inhibitors; 4.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 5.
DR PROSITE; PS51233; VWFD; 3.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000276133};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 247..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1479..1646
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1841..2010
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 2309..2479
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DISULFID 2703..2718
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2729..2747
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2741..2756
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2766..2784
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2824..2839
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2862..2877
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 2903
FT /evidence="ECO:0000313|EMBL:RNA36465.1"
SQ SEQUENCE 2903 AA; 333031 MW; 49A911B098C4DF1B CRC64;
MKSFSKNNTS DVSNRMNTNC ANFVSQHQTI DNSNKFSGSN NYESVDYFNH VNPKFKFDPT
VVRQQPQFSF RPDQPITSYD SNTADIYSYR ELNEIYNEND ESKPIAEKVP VNQNSVKASA
NLNLTYIEVK PMNIIEEDKN NIYNASSSVY SVKYLIDIND LKTHLASTNS QATMDTIKTK
NSQSNLIKSS TNDELRDEKT INNFNKHVTK KIHINSNPFF CCKIFSLFSC CFQFFCGMCF
KPCCSTAGFL GVVGMLIGLM TGGALMGLSG IITLPYEITK NICNTTQDNN YYYYQNNHTF
YVEKNNSIDS NINFTKFCSE FYIRPNFAII DNFKKNKTIE KKKEFFTLEL KSNLSKKFDE
ITKNKNSISK LIPLSYEVVL QPKINSNENA PSIKQKTKSL NLNLIMKIKV SIKLICNYTT
DFIFVHSKEF STIDLSLEHN NKPHIEIKRW NHDSNTNILE IELTDKCSLQ SIYTLNIFVS
YKNYGNSLKF VENSKIFFIS NFNEQFDSAF PIVVPYFYHT KRQQIQIYFS GPASFSVSLE
KPVSSSQLIF NTGRNKRELK DGIEYTSYDQ SPFFSAQTLG FILGDFACKE SYDLEKFNLN
FRICSTKSSD LYSETFDLLS NNVKHLVQFY HNYTKQPYAV NKIDLIVVPL TEIDLIEINH
VGILYLPALF IDSKLYSNDY LTKLKRKLSL VNILSKQLAK HWFYESMDFH CMKKKLEENE
ISKETLSLMK LCTNGSCSIN ETNMILDKYF ELNEKCFLFR GVMNWISYLA FKSINPDFFD
LVNLEWSLIK HIDETYFLTN KNLKHIYQYY DFPRLVDGNT FLKIKTELRS LISAKTLHTI
LGNERFQSVI NEWSNMVKQI SIGDSFKYHE KLNNLRNNEI YILRVFEKYF GQYNLIPIGY
FSLKSILRSW NTIDNDLVIK VERNYNKKDA LVQIESSNIL KFYYPFNWFK GTLKSVSSFD
LYEVDSYNNL NQLANLVWIN DSSTLIKYMP GADKWIVGNY MKTFSFFRIN YDTQNWIMLT
QQLLFDFKSF NINERIQIVD DVFYLINNQF LSIRYGLDIL DYLKRENRFL PWKFAIDQIK
KIFSYIEDDS QVYSKFREFI INLVKPLYER LQWGENIMDS LDEKFIRVQV VDLMCSLDYE
DCVQNSVKQL TDMIKINVNN IPLYLRKSVY CTAIRHTGIN EWFYLWKMYL IQRQEDNFSL
KDSFLYSLSC SSQNWILNLF LRRLVYENSI LLEDLPVAVS YISQNPVGKY VTWNHISQNY
QNFYNKIGND PELFVKILQV STSEFKFKYE IKQIYDFIEE IGLKNYSIYY EDSNDRIYND
ENNLFTNIEN RMSHFTKWKQ ANVKELDDWL TMANVSIITK LFVCLMAIHY TLCQDSHFCD
MKQKKNAECP EELDILYEYS KNDSEWKIDF EQFRLEKISH TTDLIREITN RKLSGKLCPY
TRIHKQCCEG YSGADCKIAN SAVPIPMKNL TRPAYLPFST CLLWGKDHYR TFDGSFFQLS
GNCDYKLSGA SSWQVNVKTE GCQNYNTCKK TLLMSFGSIK INADGGKISI DQEILGDEEN
YVKDALTIER KEEFVHLRFS DGVRLKWTTD SLTIFLTVDD QYVNKVSGLC GDYNDEKEND
FLLPTGEYTK EASIFANSWR LDSSCSEVPP ITYPCNTPEL KIEAKEACKL IIDPNDAFNL
CDKVLNGSKY FEECEKDFCV AKRSSDPKSV EIAVCNAFAL FGSQCSDHFI SVEWRTASRC
PKQCPGRKVY SECGTSCPKT CQNRNIDLSG VQCIQACSPG CVCPAGLYID AGQNNTCVES
QECTCFYRGN YYRPNEKVTI DCNECICQSG LWSCTKRKCP RTCSLYGLGH FKTFDGKNYD
FRGSCEYTLL EQINTTLDPN LLITYKSVNA LNKENPIELN IHAMKTIVSF RQNLIYVNSQ
LVSSLPFVNP DVFVKKTSEF FYSIQGKGFW VLFDGIRVYI TVDPLYLENI RGLCGTYNFK
SSDDFMPPNG FIESDITSFV DSYKLDGSCQ TPKQMVPCDT YPSAVSDANS MCDVLKSALF
KPCESLVDVA TYIEACKFDI CSDENSNHRD MYRCRAVAAY AHECASKGVV IDWLENDDLR
ELKAACYNSK YGKCYGGSQY SECTKLANST CKELFIRDKF VGQNEFCVAG CSCPDGQFLD
KINGQYTCVV KESCSCYDFV QNKYYQPGEK IKRACSTCTC SNGSWSCDNT DCRDIIKCPQ
NQVFSNKASS CPKTCANKDH YRDCNIEIEG CICPNGTIPD FNNVCVPEIR CSCHHGGKNY
NHMETIRMGC NTCECRGGHW TCSTEKCDGV CIAAGDPHYS TYDGFRFSYQ GNCKYILTQT
SDQSFRVIAE NIPCGTTGVT CTKNIFIQYN EISISLMRGR NIEVNGIEIV DLDEGARVFG
SVRIMTAGLY HIINSTDFMI KWDEATRLYI VIHSHWKNKM QGICGNFDMD SSNDMQTTSG
ILGTLEEFVD SWKVEKSCPL RPSPIIDESD PCSGHLHRKE WAIKECSLVN TPGAENPFSP
CLEKLDPADI QKSHIECLFD ACSCDKGGDC ECLCSSLASF SELCLKVGVA VKWRTQHRCP
IQCEYGKEYL PCGPLCQQTC MDLSTGNNPQ CPDAGCVEGC FCPEGYVIDY NGKCVLPTNC
DCYANANRYP PGSQIAKDCE ICVCINGTFK CDEKILDCKT ECNNETEFSC KVDKTCIPLE
WLCDKTADCS DSSDEADCKC ELNNSTFVCD NGQCINSINV CDGIVNCRDQ SDEKDCFNPI
CEEFLCQNKK CIPQKWVCDG YIDCGIQDES DEMNCNNTNI CEDEVREFYC ESKNPKCHPI
AELCDGHDDC GDGSDEKNCT CICKNGFTCK NKCECIDPKK VCDSVRDCSD GTDEINCGCQ
EDEYRCIGGK CINSTKLCDG IED
//
