ID F6P8Y7_DANRE Unreviewed; 2543 AA.
AC F6P8Y7; A0A8M6YX27;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Stabilin 2 {ECO:0000313|Ensembl:ENSDARP00000116540};
DE SubName: Full=Stabilin-2 isoform X1 {ECO:0000313|RefSeq:XP_017210540.1};
GN Name=stab2 {ECO:0000313|Ensembl:ENSDARP00000116540,
GN ECO:0000313|RefSeq:XP_017210540.1,
GN ECO:0000313|ZFIN:ZDB-GENE-041210-336};
GN Synonyms=si:dkey-207j16.6 {ECO:0000313|RefSeq:XP_017210540.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000116540};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000116540}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116540};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000116540, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116540,
RC ECO:0000313|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_017210540.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_017210540.1};
RG RefSeq;
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 EMBL; CR383662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017210540.1; XM_017355051.2.
DR STRING; 7955.ENSDARP00000116540; -.
DR PaxDb; 7955-ENSDARP00000116540; -.
DR Ensembl; ENSDART00000136000; ENSDARP00000116540; ENSDARG00000045748.
DR Ensembl; ENSDART00000136000.4; ENSDARP00000116540.2; ENSDARG00000045748.7.
DR GeneID; 565194; -.
DR AGR; ZFIN:ZDB-GENE-041210-336; -.
DR CTD; 55576; -.
DR ZFIN; ZDB-GENE-041210-336; stab2.
DR eggNOG; KOG1218; Eukaryota.
DR HOGENOM; CLU_001035_0_0_1; -.
DR OMA; RCHGSAN; -.
DR OrthoDB; 2970631at2759; -.
DR TreeFam; TF331489; -.
DR Reactome; R-DRE-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-DRE-3000497; Scavenging by Class H Receptors.
DR Proteomes; UP000000437; Chromosome 4.
DR Bgee; ENSDARG00000045748; Expressed in mature ovarian follicle and 20 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IMP:ZFIN.
DR GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR GO; GO:0060837; P:blood vessel endothelial cell differentiation; IMP:ZFIN.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0042632; P:cholesterol homeostasis; IGI:ZFIN.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IGI:ZFIN.
DR GO; GO:0150024; P:oxidised low-density lipoprotein particle clearance; IGI:ZFIN.
DR GO; GO:1901492; P:positive regulation of lymphangiogenesis; IMP:ZFIN.
DR GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IMP:ZFIN.
DR CDD; cd00053; EGF; 1.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.30.180.10; FAS1 domain; 7.
DR Gene3D; 2.10.25.10; Laminin; 16.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR24038; STABILIN; 1.
DR PANTHER; PTHR24038:SF0; STABILIN-2; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF12947; EGF_3; 8.
DR Pfam; PF02469; Fasciclin; 6.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 23.
DR SMART; SM00179; EGF_CA; 9.
DR SMART; SM00180; EGF_Lam; 5.
DR SMART; SM00554; FAS1; 7.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF82153; FAS1 domain; 7.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 15.
DR PROSITE; PS50026; EGF_3; 19.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50213; FAS1; 7.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
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}; Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..2543
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041157263"
FT TRANSMEM 2454..2478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 103..143
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 150..187
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 189..229
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 230..269
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 315..354
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 354..495
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 507..641
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 727..767
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 817..856
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 857..899
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 900..942
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 984..1117
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1124..1252
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1333..1373
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1380..1417
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1421..1460
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1461..1502
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1503..1545
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1546..1587
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1587..1714
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1730..1871
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1948..1988
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1995..2032
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2037..2071
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2113..2155
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2188..2281
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 2301..2438
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT REGION 2496..2532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 133..142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 158..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 177..186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 198..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 757..766
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1363..1372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1388..1405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1407..1416
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1425..1435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1429..1446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1978..1987
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2022..2031
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2041..2051
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2210..2279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 2234..2255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 2543 AA; 275454 MW; 512FCA9BEFC90A64 CRC64;
MPFLLDVVCG GLILLLGTEI LWVAGAQKRC DKDITMVTKS KCHSCSLSHL AKCPNGYAKM
PPGTSDRDCR YYVTPVFSIS GCSFNCFKEV VEPQCCRGYW GNDCMECPGS ASTPCSNNGV
CSDGIAGNGT CTCASGFTGA ACEECKTDLY GPTCSNVCRC KNGLCSSGLK GTGECTCFSG
YTGLDCAQEL PACAALQCGP DSRCIEEMLT GQLVCKCKPG YQGDGVQCTS INPCLRSVCH
ANAVCAHTGP NKHVCTCTEG YSGDGRVCMP IDPCQTNLGN CTSGSTRCVY DGPGKAHCEC
LEGFEKFVEG QGCSIIDLCK PDSCHKYATC ATAEPGTVEC NCREGFIGNG KICFGDIIQQ
LNEMNSKPGG KWTGQLSSAI TLFNQVTGWF LTARGPFTVF VPVNKAFKGT SVKSLLADEM
KARYLAKLHV VAGEVNSESL KKGILFHTLT GMGAESMIDA EQVKIRLHGS RKKGALVESD
IFASNGMIHL IDKLMDAVPS TVISEKEESL LEILSKNGKF SQFKSLLEKT NLATVLEEDG
PYTLFAPTNV AFALMKPDYL AYLKSEEGKT KLLELMRNHI VSTTPLSAYV IVSNPRAVTM
AEQILTFNVT TAGQILVNGE SVIELDVEAK NGRLHSLEGL LIPPSIEPIL PHRCDIIKPI
KYMAPCVSCT LISKSTCPTG ESLKAYRRGC VFNKKQLGLS LPSIGCSHIC NDTKTTPQCC
KGFFGPDCSP CPGGFTTPCS SHGTCSEGID GNGTCQCEPK FKGSRCQYCA DSNKYGPNCD
KTCWCIHGTC DNHPEASGKC KQGSCKDGYT GEYCELQTQP CGPNQPCHAH ANCVSNKGAF
TCVCKPGFQG DGYMCMESDP CALPHRGGCS KNAICIKTGP GTHKCKCLSG WREDGDECQA
INNCLDPSRG GCHPNATCIY VGPGQIDCAC KSGYHGNGRE CEPVNQCVEQ KGGCHFLATC
QFLNPDGWHC VCEDGYAGDG KICYGTLLQE VSTNPDLLGF NQWISKAELS QLLSERENLT
LFVPSAQAIE KMSKEDKDIW MTPSNLPSLV KNHILSGSFT LSDLNTSPSP PPRLVSLLKR
TLPVYSTNDT TIVAGGKITF GDMAAKNGVI HLIDTVLIPE QQMSEGLLQV LKKRSDLSLF
YGSLLNHNLT NEMEESLGFT VFAPTDNAIQ DYLKRTGKES LDLNVTMYHI ILTEILKDVD
LVDGLYKDTM LGFQYQLGFF RQDKRLLVNE AEVNVTDLET SKGVIHIISA VLNIPSNRCD
KATSILFSGR CMDCFQTIIN PCPSGTKKVM SRKRRCMYSR VLHGDTLLTI GCKFSCEKMT
IERICCSGHY GINCEKCPGS EDQSCFGNGI CKDGINGTGV CLCNQGFNGT ACESCQPGKY
GIHCDQECKC VHGRCKDGID GDGSCACDLG WRGVNCDIAI KSDMCGGKCH SSANCLVNVV
DSSYYCSCAA GFQGNGTYCE AIDACAERNG GCSAHAVCKR TLPGRRICMC HPGYAGDGNV
CTSINPCLDG VNGGCHADSN CIHTGPNKTA CHCKEGFYKD GKNCELINLC KEKNGGCHRA
AICTMTGPLQ RNCTCHAGYV GDGEICKYTL QRELSIETAR TAFVKAMFKN RIYELDTRGP
FTVFAFRSEN YKNQSIDLVK RTPENTRIMR YHIVCCRTLL PQDLMQPRNL TTLSGDILSI
TYSENTIYIN NKAKVLFSDI ESSNGILHEI DSVLVPPGLE IREDKKQDII PRNFSEVASA
NGFKTFFKLL EDTDTLKLVM DPIHQPVTLF MPTDDAMSAL SQEQKDFLYA MHNRDKLSEY
LRYHILRDTK LMASELIYAS SLKTQQGSDL SVACMGEEQI GELYVNHKGC RIVKRYLDFN
GGMIYGIECL LNPPSLGGRC DHRQTIDFTL ACRSCGSSIM DCPLGSKPVG EQECVLPDSV
ISRGSKCQST CKVVVWKPKC CSGYYGRDCL ACPGGPQSPC SNHGKCDEDH LGNGTCTCDT
GFTGVACESC LDGHFGPDCN ACNCTEHGSC DEGLQGTGSC FCEEGWTGPQ CENKLADGPV
CNPACHEKGV CMENNTCVCK PFYEGDGITC TVANMCKYWN GGCSKDAKCS QKGEKVSCAC
LQGFSGDGFV CTPIDPCVDG ENGGCHEHAT CTMTGPGKRK CECKDSYVGD GIDCEAKVLP
VNRCLVDNGQ CHSDAQCTDL HHEDKTLGVF HYRSTNGTYK LNYTMAQEAC KEAGSTIATY
MQLSYAQQAG YSLCTAGWLD KARVAYPMSF SSPRCGSGHV GIVDYGVRNN LSETWDTFCY
RVKDVQCKCK TGYIGDGFSC TGNLMQVLSA TPTLSNFLSQ ILNFSTSASG KAFVNRLRNI
TIQSTLFVPD NDGLYSNQTL SGRDIEHHLL DGRALILQAL INVTHVRTRL GSSLTITGVP
DLQNPQKMTS SGYINDRYVI DSNIFASNGV IHVLQGPLKA PPPPTPSFHP AHQAGLGIGV
LGLIILIVVA GFVGYNFYTH KTKPFQFHYF KEDEGEDVTP TESSPNISNP VYDAAPATKE
QPPTEEDKHQ VISSGVFDLL QDS
//
