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Database: UniProt
Entry: A0A3B4U9U8_SERDU
LinkDB: A0A3B4U9U8_SERDU
Original site: A0A3B4U9U8_SERDU 
ID   A0A3B4U9U8_SERDU        Unreviewed;       694 AA.
AC   A0A3B4U9U8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Vasorin {ECO:0000313|Ensembl:ENSSDUP00000014928.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000014928.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000014928.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A3B4U9U8; -.
DR   STRING; 41447.ENSSDUP00000014928; -.
DR   Ensembl; ENSSDUT00000015212.1; ENSSDUP00000014928.1; ENSSDUG00000010909.1.
DR   GeneTree; ENSGT00940000159318; -.
DR   OMA; HRYIEMR; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR24369; ANTIGEN BSP, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR24369:SF160; VASORIN; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00364; LRR_BAC; 6.
DR   SMART; SM00365; LRR_SD22; 4.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51450; LRR; 3.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..694
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017212650"
FT   TRANSMEM        594..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          425..462
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          484..577
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          376..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        452..461
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   694 AA;  76035 MW;  FC40E10453793100 CRC64;
     MERERVCTMK VFLTPLMPFL LLLIFPDGIL SSACPNDCTC STPESILCFL RRSSTIPKGV
     PSYTKSLYLF ANGIEGLTAE DFDGMENLEM LDLSQNKLTE LPDRVFEPLT SLRNLDLSSN
     QITHISEECF QGMALLERLY LYSNLIKTIH PAAFNGLGHL LELKIQGNQL TSLPALSMPR
     LLLLDLRFNV LPTLGPSDLQ TPNLESLKLG GVGLTSLNKE LIGSLKNLHE LDISGNQLES
     FPSVLKETKG LIHLSLAGNP MGPLKVQDLQ NLGELQDLDI SSLSLQGLPE EFSQLFPHLR
     KLTVAENPFN CLCTLAWFPR WLRAQSIILE RTEETRCHFP PINAGKVLER LEHRDFGCPT
     TTTITTSTVK TTTTLPVPVT TLPSTTEAIP APRASDNPTD KDDDSPLLPV PASPSSSSSI
     DLGEDQHFCP SHTCLNGGTC RLDQHGQVEC TCPHGTSGTY CEVQNHHPPS PPEAAIPMAT
     VTADATDISS HEVTATSILV DLHRYTEMRP YIRGIRLTYR NLSGPDRRPI QLSLPASFPE
     YRLRGLKPNS TYTVCVSPLG APSDIDSVCT EAHTAPESIS GPDARVTDPR LTTMLAPAVA
     ILLVLVLIAI AVGVVCYLRR KRAKGHLDLD CEPSQLELDG VKAGLDNGAL PQKQPQIMIP
     EPAVQNGNLE YEVLLLQDHC TSNNNMSSHK PSYF
//
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