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}.
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 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
//