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Database: UniProt
Entry: A0A3B4X699_SERLL
LinkDB: A0A3B4X699_SERLL
Original site: A0A3B4X699_SERLL 
ID   A0A3B4X699_SERLL        Unreviewed;      2392 AA.
AC   A0A3B4X699;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Stabilin 1 {ECO:0000313|Ensembl:ENSSLDP00000008208.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000008208.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000008208.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   STRING; 1841481.ENSSLDP00000008208; -.
DR   Ensembl; ENSSLDT00000008475.1; ENSSLDP00000008208.1; ENSSLDG00000006358.1.
DR   GeneTree; ENSGT00940000157928; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:Ensembl.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR   GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0150024; P:oxidised low-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:1901492; P:positive regulation of lymphangiogenesis; IEA:Ensembl.
DR   GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
DR   Gene3D; 2.30.180.10; FAS1 domain; 7.
DR   Gene3D; 2.10.25.10; Laminin; 8.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR036378; FAS1_dom_sf.
DR   InterPro; IPR000782; FAS1_domain.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR000538; Link_dom.
DR   PANTHER; PTHR24038; STABILIN; 1.
DR   PANTHER; PTHR24038:SF8; STABILIN-1; 1.
DR   Pfam; PF12947; EGF_3; 7.
DR   Pfam; PF02469; Fasciclin; 6.
DR   Pfam; PF00193; Xlink; 1.
DR   SMART; SM00181; EGF; 22.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00554; FAS1; 6.
DR   SMART; SM00445; LINK; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF82153; FAS1 domain; 7.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 11.
DR   PROSITE; PS50026; EGF_3; 15.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50213; FAS1; 6.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2310..2334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..93
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          101..138
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          178..216
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          264..303
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          303..436
FT                   /note="FAS1"
FT                   /evidence="ECO:0000259|PROSITE:PS50213"
FT   DOMAIN          447..580
FT                   /note="FAS1"
FT                   /evidence="ECO:0000259|PROSITE:PS50213"
FT   DOMAIN          657..697
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          790..832
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          833..875
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          876..917
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1017..1145
FT                   /note="FAS1"
FT                   /evidence="ECO:0000259|PROSITE:PS50213"
FT   DOMAIN          1238..1270
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1277..1314
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1318..1357
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1358..1399
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1450..1573
FT                   /note="FAS1"
FT                   /evidence="ECO:0000259|PROSITE:PS50213"
FT   DOMAIN          1568..1711
FT                   /note="FAS1"
FT                   /evidence="ECO:0000259|PROSITE:PS50213"
FT   DOMAIN          1803..1843
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1850..1887
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1967..2009
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2043..2136
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          2156..2298
FT                   /note="FAS1"
FT                   /evidence="ECO:0000259|PROSITE:PS50213"
FT   DISULFID        83..92
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        109..126
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        128..137
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        687..696
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1260..1269
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1285..1302
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1304..1313
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1322..1332
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1326..1343
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1833..1842
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1877..1886
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2065..2134
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        2089..2110
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ   SEQUENCE   2392 AA;  260615 MW;  3C5BBB13A9A2498F CRC64;
     MHGGCIHTVC RSLNRSWNDT HLITCLSIFP CTLSVCLSVC LSVCLSVCLS VCLSAACPSW
     SGKTCNFHGA CLDGDLGNGT CVCDDGFSGF ACQECKNQNA FGEKCDKECD CVHGVCNKGP
     EGDGQCLCQP PYTGKRCDQV SARCSNCSPY SFCKGEGDTA DCECLPGYRK MAQGKCSLFS
     ICSPKDCDVN AQCSSQGSKV SCVCKPDYQG DGRICVPRNP CSDNNGGCPI NSTICVFKGP
     NKSSCECMSG MSPIGGSPEF GCQLVSACSA DTCDPTAVCQ TELDGQPRCV CEAGQIGDGR
     RCYGNLMEQL IELGRTGSQR ENLTEAVALF EKGCLLLLSH NGPFTAFIPL ILLIYSLTLS
     LQGVNEELVC KNHLILGQHL YKDLEGRDFN MYGGAKMRSK DNKKFILMDN PRKLYTVLQE
     DLPAANGIIH IIDQQITNMI SMRPFSDKTI GEILTKSGQY NRFLSLVDNC GAPPPLKGPG
     PLTVFIPTNQ AVDRARDGSI LYMLNDAKYK LQELLRHHVF SQAVLTVDDL ARLPRILTMA
     NQIITISVSD GILLGEKGVR LVTTNIVASN GIIHMIDGLL YPPSILPVLP HRCDVIESKI
     TGPCVHCSYL YETECPDGST EMVNTSLLLP CEWMINCAVA QPLRAVAECC DGFYGPDCKP
     CIGGFQHPCY DKGRCSDGIN GNGSCSCQSG FKGVACHICS DPATHGDNCD QECRCVHGVC
     DNRPGSGGVC RRGSCFEGYS GESCDRTATP CNSDGLQEHC HIHAYCTHTG LHTTCVCRDG
     YEGDGHSCSP INPCLQSNRG GCDTNADCVY AGPGNASCVC VEGWTGDGKV CVEINNCQLE
     SRGGCSLNAD CNHKGPGQSE CVCKTGYMGN GIKCDLVNPC RNNNGGCHGM AKCELKEGGT
     HTCTCPDGYA GDGIICYGSL LDKYNHFPED LSGNLTMLVP SREALRNMSV DLDLFWTSRH
     RLPHFLRAHI LPGMYSIEDL DRLVGSRLPT LNPPTSWEIN NSSGVLAPSR SDLPPEPPKL
     MAFLNSSSDF TLFRQYALMY NLSQDLSMFE FTLLLPTDDA IRQHLSRTNS SLLDSDVFKY
     HVILNELLFP DHLSDGMLKS TLLGSDHQVH FHFNDNNQTL VNDVPLDGSF IETQNGVIIV
     LTQVLKVRRN RCSKQVTLQV NGRCSDCDGP PRCLLNYKPV RKPQFPTNMR SNCRYRKRVG
     SRRKSVQGCI IKCLRVTMDH SCCPGYFGHE CFKCPGEVGS WCSNHGECQD GNHGDGECRC
     YEGFHGTACE DCEPGRYGVN CSSKCVCDHG KCEDGLAGSG RCVCYKGWKG VSCSVEIKDD
     ACGGVCDENA NCITGPKGAA AACVCVAGYE GNGTYCKELD LCSRSNGGCS EFAVCMKVSA
     GERTCTCQEG YTGDGVVCLE RLMTQVMTNI INDFIKNENG CRAGNNNGGC SKYARCEYMG
     QGQRNCSCFR GQIGDGFECR GNTNNVSHLP FDLPLTSDLA MPRLPPSQDV VLSMCLSYRN
     AGRLDELVRY HVVSCETLTL SDLKTTERAV SLSGNMLHFS LQQGSVWINN RSRIVKSDYT
     TTNGVIHHID TVSSLSPSLS LSPSVRFYNL VEDAGLLPVL QELIHQPYTM FWPTDQAFNS
     LPAERRRWLS SPDHQEELVA TLKAHIIRSY RVMGISHPDK YSSFRTMHGS TIKYMCDKTL
     GAVLINDNAA RVVERYLNFK EGMAYGIDQL LEPPGLGAHC DSLENKTGRC GSCIYPPSCP
     LRHHDTVRSG KTERCLNLRH RYAIGYRRWY PDLDDHFTRT GCKRICQFPS WVQKCCTNHY
     GRDCQVCPGG VEAPCGNHGS CDDGVRGSGR CRCSMGFRGV ACELCNTGYY GPNCTACSCG
     QQGRCDDGIE GSGQCVCKPG WLGDRCQTEI ASIPEECRQC HAQADCVPGA GCQCKSGFEG
     NGTFCTPDLC SEYNGGCHQN ADCNQTGLVV NCTCHSDYQG DGYSCEPINR CVEEQNGGCS
     DFASCKFTGP NERECECLAG YVGNGVQCLE KVVPPVDRCL EDNGGCDPVA SCKDLHYHAN
     TAGVFHLRSP EGKYKMNFSE ADAGCQAEGA TLANFKQMGD AQQMGMHLCV AGWMEGGKVG
     YPTRFPSVKC GDNHVGLVIY KDPVDQSSKY DAYCYRVKDV ECTCPAGYVG NGDFCNGVLT
     SVLATYSNFS TFYKLLLDYS GSTSGGKQLV EFLSHRKSEV TLFVPHNAGF APNQTLSGRD
     LEYHISANNS VRPFMDLRHE EVITSWLGFN LTVTHVIVVD KYNNKLLLRS YKLVNKRLLL
     EWDIPAVNGI IHVIEAPLTA PPPQVSKDGL TLTAAILVSL LLVCVLAALG YYVFKHKTDA
     FRFHYFRNED EDGAAGGRTK PALVSIPNPL YSGSRAFTEP FGVISTVLSV SQ
//
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