ID A0A2K6M329_RHIBE Unreviewed; 2537 AA.
AC A0A2K6M329;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Stabilin 1 {ECO:0000313|Ensembl:ENSRBIP00000030175.1};
GN Name=STAB1 {ECO:0000313|Ensembl:ENSRBIP00000030175.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000030175.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000030175.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000030175.1}
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; 61621.ENSRBIP00000030175; -.
DR Ensembl; ENSRBIT00000054134.1; ENSRBIP00000030175.1; ENSRBIG00000038956.1.
DR GeneTree; ENSGT00940000157928; -.
DR OMA; VHAECIP; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:Ensembl.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR Gene3D; 2.30.180.10; FAS1 domain; 7.
DR Gene3D; 2.10.25.10; Laminin; 13.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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; 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; 23.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00554; FAS1; 7.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF82153; FAS1 domain; 7.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 9.
DR PROSITE; PS50026; EGF_3; 18.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50213; FAS1; 7.
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:UP000233180};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014427227"
FT TRANSMEM 2443..2466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..146
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 223..262
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 347..485
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 497..630
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 717..757
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 807..847
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 850..892
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 893..935
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 936..975
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 977..1110
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1121..1246
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1323..1361
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1368..1405
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1409..1447
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1448..1489
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1490..1532
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1533..1575
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1575..1701
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1717..1845
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1950..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 2072..2112
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 2175..2268
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 2289..2426
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DISULFID 136..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 747..756
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1351..1360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1376..1393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1395..1404
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1413..1423
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 2197..2266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 2221..2242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 2537 AA; 272193 MW; 38433487DE093ACF CRC64;
MAGPQGLLPL CFLAFCLAVF IRGQVLFKGC DVKTTFVTHV PCTSCAAIKK QTCPSGWLRE
LPDQITQDCR YEVQLGGSMV SMSGCRRKCR KQVVQKACCP GYWGSRCYEC PGGAETPCNG
HGTCLDGMDR NGTCVCQENF RGSACQECQD PNRFGPDCQS GECLQGKRAG SVLDLGSSVL
FPLCSELPIC QELRCPQNTQ CSAEAPSCRC LPGYTQQGSE CRAPNPCWPS PCSPLAQCSV
SPKGQAQCHC PENYHGDGMV CLPKDPCTDN LGGCPSNSTL CVYQKPGQAF CTCRPGLISI
NNNASAGCFP FCSPFSCDRS ATCKATADGK TSCVCRESEV GDGRACYGHL LHEVQKATQT
GRVFLQLRVA VAMMDQGCRE ILTTAGPFTV LVPSISSFSS RTMNASLAQQ LCRQHIIAGQ
HILEDTRTQQ TRRWWTLAGQ EITVTFNQFT KYSYKYKDQP QQTFNIYKAN NIAANGVFHV
VTGLRWQPPS GTPGDPKRTI GQILASTEAF SRFETILENC GLPSILDGPG PFTVFAPSNE
AVDSLRDGRL IYLFTAGLSK LQELVRYHIY NHGQVQEAHS PKVGSTMANQ VLAVNISEEG
RILLGPEGVP LQRVDVLAAN GVIHMLDGIL LPPTILPILP KHCSEEQHKI VAGSCVDCQA
LNTSMCPHNS VKLDIFPKEC VYIHDPTGLN VLKKGCASYC NQTVTEQGCC KGFFGPDCTQ
CPGGFSNPCY GKGNCSDGIQ GNGACLCFPD YKGIACHICS NPNKHGDQCQ EDCGCVHGLC
DNRPGSGGVC QQGTCAPGFS GRFCNESMGD CGPTGLAQHC HLHARCVSQE GVARCRCLDG
FEGDGFSCTP SNPCSHPDRG GCSENAECVP GSLGTHHCTC HKGWSGDGRV CVAIDECELD
VRGGCHADAL CSYVGPGQSR CTCKLGFAGD GYQCSPIDPC RAGNGGCHGL ATCRAVGGGQ
RVCTCPPGFG GDGFSCYGDI FWELEANAHF SVFYQWFKSA GITLPADRQV TALVPSEAAV
RQLNPEERAF WLQPRMLPSL VRAHFLQGAL FEEELARLGG QEVATLNPTT RWEIRNISGV
WSGGRMSSVD VLGPPLGHRM VSLHIPSQVL TAPPRDDAQW GRGLLQQLDL VPAFSLFREL
LQRHRLVSQI EAATAYTIFV PTNRSLEAQG NSSHLDADTV RHHVVLGEAL SMETLRKGGH
RNSLLGPAHW IVFYNHSGQP EVNHVPLEGP MLEAPGRSLI GLSGVLTVGS SRCLHSHAEA
LREKCVNCTR KFRCTQGFQL QDTPRKSCVY RSGFSFSRGC SYTCAKKIQV PDCCPGFFGT
LCEPCPGGLG GVCSGHGQCQ DRFLGSGECH CHEGFHGTAC EMCELGRYGP NCTGVCDCAH
GLCQEGLQGD GSCVCNVGWQ GLRCDQKITS PQCPRKCDPN ANCVQDSAGA STCACAAGYS
GNGVFCSEVD PCAHGHGGCS PHANCTKVAP GQRTCTCQDG YMGDGELCQE INSCLIHHGG
CHIHAECIPT GPQQVSCSCR QGYSGDGIRT CELLDPCSKN NGGCSPYATC KSTGDGQRTC
TCDTANTVGD GLTCRARVGL ELLRDKHASF FSLRLLEYKE LKGDGPFTIF VPHADLMSNL
SQDELARIRA HRQLVFRYHV VGCRRLRSED LLEQGYATAL SGHPLRFSER EGSIYLNDFA
RVVSSDHEAV NGILHFIDRV LLPPDALHWE PDDEPIPRRN VTAAAQGFGY KIFSSLLKVL
LPSVPHQTPA AFRALPPDRQ AWLYHEDHRD KLAAILRGHM IRNVEALASD LPNLGPLRTM
HGTPVSFSCS RTRPGELMVG EDDARIVQRH LPFEGGLAYG IDQLLEPPGL GARCDHFETR
PLRLNTCSIC GLEPPCPEGS QEQGSPEACW RFYPKFWTSP PLRSLGLRSV WVQHSLWARP
QGLGRGCHRN CVTTTWKPSC CPGHYGSECQ ACPGGPSSPC SDRGMCMDGM SGSGQCLCHS
GFAGTACELC APGAFGPHCQ ACRCTVHGRC DEGLGGSGSC FCDEGWTGSH CEVQLELQPV
CTPPCAPKAV CRAGNSCECS LGYEGDGRVC TVADLCQDGH GGCSEHANCS QVGTAVTCTC
LPDYEGDGWS CRARNPCTDG HRGGCSEHAD CLSTGLNTRR CECHAGYVGD GLQCLEELEP
PVDRCLGQPP PCHSDARPLW SELFGGSRPC FIPSALCCPA GVWGPEVGHP LLFLQLGFHL
CLMGWLANGS AAHPVVFPVA DCGNGRVGIV SLGARKNLSE RWDAYCFRVQ DVACRCRDGF
VGDGISTCNG KLLDVLAATA NFSTFYGMLL GYANATQRGL DFLDFLDDEL TYKTLFVPVN
EGFVDNMTLS GPDLELHASN ATLLSANASQ GKLLPAHSGL SLIISDAGPD NSSWAPVAPG
TVVVSHVIVW DIMAFNGIIH VLASPLLAPP QPQAVLAPEA PPVAAGVGAV LAAGALLGLV
AGALYLRARV KPTGFGFSAF QAEEDAADDF SPWQEGTNPT LVSVPNPVFG SDTFCEPFND
SLLEEDFPDT QRILTVK
//
