ID A0A0V1D201_TRIBR Unreviewed; 2170 AA.
AC A0A0V1D201;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1 {ECO:0000313|EMBL:KRY55530.1};
DE Flags: Fragment;
GN Name=SVEP1 {ECO:0000313|EMBL:KRY55530.1};
GN ORFNames=T03_14624 {ECO:0000313|EMBL:KRY55530.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY55530.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY55530.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY55530.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:KRY55530.1}.
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DR EMBL; JYDI01000054; KRY55530.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1D201; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 3.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 9.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 6.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR InterPro; IPR000859; CUB_dom.
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; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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 InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02494; HYR; 2.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00084; Sushi; 4.
DR SMART; SM00032; CCP; 8.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00179; EGF_CA; 9.
DR SMART; SM01411; Ephrin_rec_like; 3.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 6.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50825; HYR; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 7.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 60..172
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 176..289
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 391..453
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 454..515
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 516..575
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 576..634
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 634..675
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 886..945
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1009..1075
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1125..1279
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1305..1391
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1392..1475
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1476..1541
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1854..1896
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1898..1934
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1936..1974
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1976..2016
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2018..2054
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2056..2091
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2093..2129
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2131..2167
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 24..42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 36..51
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 518..561
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 916..943
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1886..1895
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1924..1933
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1945..1962
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1964..1973
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2006..2015
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2044..2053
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2060..2070
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2081..2090
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2119..2128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY55530.1"
SQ SEQUENCE 2170 AA; 238990 MW; 594C1B8DA91D7893 CRC64;
LALDCLQSSL SVRLSASSLR MMFCHNGKCI SKNGKCDGFD DCGDLSDEMN CRASQGNALC
IRYAKGDSGI VESPNFPAEY KSNLNCQWTI EVAANAKIRL EFESFQTEPY YDIVTLLDGG
PVENTSVVVD HISGNVDPSK LIFLSSTNRM AVKFRSDASV NFKGFKANWR LVTFDCGGRL
KAHPNEQTIN SPNYPQNYPN GAECLWIIEA TGNQLISITV RINDVELENG KDMLIIYDGE
HSTSRALFST SSAIDEPRVV ISTRNRVSVY FFSNYLNSAR GFSISYRLGC DNTMQGTSGF
ITSPGNNAVD YHGDHLCTFT VNPTQQVMPP RPVTLIFDGM DNRGHQLYPK GKESSVLKSG
GTLISETGHF FLLFKETPLD STVNWNITYS LNCPPLTLSK DVLLSSTSTA YGTKVNISCP
YGSEFINGIG SSTELTCLLG GQWSQNFIPK CQPIYCSIMP VPAENGFVAA ATNVTYMGKV
SIKCYRGHAF SSGLDVEEID CNEDGTWSKI PQCKALVCPE LPEFVNGNRT ILRGDGRSYG
TIYKYRCFSG SYMEGADTVL CEMDGWSSPE PVCKKLSCEP ISYTGNVLLK TDALKIYSGD
VTPVECRPGY KMVGKGEIIC QDNQQFTELP VCEDIDECRL DGMFDCSSLT TTCKNLQGGY
ACECLEGYEP KLECNSTSEL IKSMAIPSDS IISESETWKY PAKNIATSGW CGKLPEPGAN
SISIILDEPR IIEAVIIKKI SDNTLAQVMA ISLKYSLHST HPLKQYVDND GSKILLKSNG
GIIMLPEPIE AEAVKITIEE YKSAPCMIME LQGCRRTSCT DINECLIDKG GCEHLCINRP
GKYECSCHPG YELFTKNGQN DMYVHPKESG TRLGDVFGLN KSCIPRTCNS LIPPENGDIV
STATKFSYPI VVEFVCNFGF QLHGSQFLQC MSDGHWNASV PVCSPAKCAN FENDTEIGLH
LYPGSQLINF GENVTITCAQ DTRPNGPTAF SHFRQCLFSP DSDGPDYLVD CGEPEFLPAS
IYKNFDEVQS FKFGSNFLFT CRKPFFVSGS SNAGDHIVRC LADGSWDFGD LHCDGTVCPD
PGILQDGDVI IDSVEEGNIA RFTCRKPGYM PYPISAMQCI IGAKCPKTEE LGISSGVVPD
TAFAANTETP IRGYEPHKAR MSRGGWCGSP DAFMFLSVDL QHVYTITTLR LAGVGGSGAI
RGHVTKFQLF YKSLFNQNFD TYPEVWNSNF AILEFEMPPG NHNKMYVFQL KEFIRARYIL
IGILEFDNNP CLRFDLLGCS MPLFQNPEIH SEFMFGWNDS LPICRDSEPP TFTDCPMEPL
YAPIDANGQM QPIEIPIPNA IDNSGSIAWI KTEPPDMQNF HVLTKDTNVT YTAFDAAGNW
AQCSIELKVP DNRPPVLVCP ESYIVEVPKD VPGMQMIFNR SSVDLMIDDA SDTVKLTFSP
GEIFLKLKQH VTVKVTAEDD FGNEASCRFQ VLLDTPRCDE SNLLLPPGVE KTCSSYKSGI
KCTISCIDGY QFLESDAGKK LYSCEADEKW TPGIIAPACV PIADEPAKYQ LKVSVSYPIA
TTIPESCLND YKSSLTSVSQ QIDTVLSQRC SASVQAFVRI VEVDFFAEVK RVVGNYTIQV
LPTVLDEVFY NLCGMTLATM FDLHFPSATE AVLPLLEIKG ENGCPVLKAT NTTIDKGFSC
SPGEILQKTE NALPGCYPCP MGTWLYNGTC RPCENGTYQD LNGQINCKRC PAGTYTLHEG
ATMVEHCQPV CDNGMFSESG IVPCQQCPKD TYSSPNKEGG YRKCEPCPKN TFTNDVGASD
ISMCKESCPG GYFSFSGLQP CSPCPKNFYQ PERGQSACIE CPKDRYTENS GAVLENECLE
ANYTDLVYCR NGAVSEVVEH VAVCQCLPGY TGIHCEQLID PCLAQPCFNN GRCVTNGVRY
ECECPEKYSG ERCEFSENEC QDVVCDNGGI CQDLPGIGTT KCLCRTGFYG ERCEFMVNLC
EKQGSELCLN GATCLPLQLN RYMCICAAGW TGRNCDINID DCAGQPCAVN ATCHDEINDF
RCDCPPGFSG KRCHIKQDLC SDNPCVNGRC IDRNFYYQCV CESGWTGKNC EQEIDNCASN
PCLNGATCTK QFNSYECECA DGYEGSRCQH QVDHCAKEPC LNGALCVNKG ANYSCICKNG
FEGFTFYYQI
//
