ID M3YZB1_MUSPF Unreviewed; 2572 AA.
AC M3YZB1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Stabilin 1 {ECO:0000313|Ensembl:ENSMPUP00000016671.1};
DE SubName: Full=Stabilin-1 isoform X2 {ECO:0000313|RefSeq:XP_004738201.1};
GN Name=STAB1 {ECO:0000313|Ensembl:ENSMPUP00000016671.1,
GN ECO:0000313|RefSeq:XP_004738201.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000016671.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000016671.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004738201.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004738201.1};
RG RefSeq;
RL Submitted (NOV-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; AEYP01001934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01001935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004738201.1; XM_004738144.3.
DR STRING; 9669.ENSMPUP00000016671; -.
DR Ensembl; ENSMPUT00000016920.1; ENSMPUP00000016671.1; ENSMPUG00000016776.1.
DR GeneID; 101681183; -.
DR CTD; 23166; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000157928; -.
DR HOGENOM; CLU_001035_0_0_1; -.
DR OMA; VHAECIP; -.
DR OrthoDB; 2970631at2759; -.
DR Proteomes; UP000000715; 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 CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.30.180.10; FAS1 domain; 7.
DR Gene3D; 2.10.25.10; Laminin; 11.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.90.20.10; Plasmodium vivax P25 domain; 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; 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; 24.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00180; EGF_Lam; 5.
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; 10.
DR PROSITE; PS50026; EGF_3; 16.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2572
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041158539"
FT TRANSMEM 2477..2500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..149
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 157..194
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 233..272
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 357..495
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 507..642
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 729..769
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 862..904
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 905..947
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 948..987
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 989..1119
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1129..1254
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1331..1369
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1376..1413
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1417..1455
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1456..1497
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1498..1540
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1583..1709
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1725..1865
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1970..2008
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2015..2052
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2092..2132
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2133..2175
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2209..2302
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 2323..2460
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DISULFID 139..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 165..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 184..193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 759..768
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1359..1368
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1384..1401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1403..1412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1421..1431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1998..2007
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2042..2051
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2231..2300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 2255..2276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 2572 AA; 274694 MW; 971CA5F6F1EF6458 CRC64;
MAGPRGCLLL CLLAFCLAGS SFTRGQKVQS RRCDVKTKFV TRIPCTMCPA IKRRMCPPGW
LRALPEKIAQ DCRYEVQLGD SLMSMSGCSL ECWKDVVEKA CCPGYWGSQC YECPGGAETP
CHGRGTCLDG IDGNGTCVCK ENFGGSACQE CRDPNRFGPN CQSECSCVHG VCNHGPLGDG
SCLCFAGYTG PRCDQELPVC RALNCPQNSQ CSAEAPSCRC LPGHIQQGRE CRAPNPCQPS
PCSPLAQCSV SPTGQAQCRC PKDYHGDGTV CLPQDPCTIN YGGCPSNSTM CLYQRPGKAS
CLCKPGLVSA NHNASAGCFA YCFPHSCDRS ATCQVTPDGK ISCVCKEGEV GDGRACYGHL
LHEIQKAGQL GVVFLRLRVS LAMLDQGCRE ILTTSGPFTV LVPSLSAVTS KIMNASLARR
LCKQHIIAGQ HVLEEPGTQQ TRRWWTLAGQ EIIVTFNRFT KYTYKYKEQP QQTFAIHKTN
YPAANGVFHL VTALQWQPPP ELPEDPKRTI GQILASTEAF SRFETILENC GLPSILDGPG
PFTVFAPSNE AVDNLRDGRL IYLFTAGLSK LQELVKYHIY SHGQLTVEKL ISKSRVLTMA
NQVLAVNISE EGRILLGPEG VPLRRVDVLA SNGVIHMLEG VLLPPTILPI LPKLCSEEQH
QIVAGSCVDC QALNTSTCPP NSVKVDSFPK ECVYTHDPTG LNVLRKGCAH SCNQTVLKPG
CCKGFFGPDC AQCPGGFSNP CYGKGNCSDG VRGNGACLCF PDYKGIACHI CSNPNKHGDQ
CQEDCGCVHG LCDNRPGSGG GCQQGTCAPG FSGRFCNESE GSCGPSEQAQ NCHQHARCIR
QGGVPRCVCL DGFEGDGFSC TPSNPCSNPD RGGCSENAEC VPGARGTHHC TCHKGWSGDG
RVCVAIDECE LDARGGCHAD ALCSYVGPGQ SRCTCKLGFA GDGYECSPID PCRAGNGGCH
DLATCRAVGG GQRVCTCPTG YGGDGFSCYG DIFRELEANA HFSVFYQWIK SAGITLPTDS
RVTALVPSES AIRRLSPEDQ AFWLQPRALP QLVRAHFLQG AFSEEELARL GGRDVATLSP
NTRWEIHNIS GRVWVHNASV DIADLLATNG VLHVLSQVLL PARGDVLPAT GVLQQLDLVP
AFRLFRKLLQ HHKLVPQIEA ATAYTIFVPT NRSLEASGNS SSMDADTVRH HVILGEALSV
ETLQRGGHRN SLLGPAHWLV FYNHSGQPEV NHVLLEGPVL EAPGCSLFGL AGVLTVGSSR
CLHSHAESLR EKCVNCSRRF RCTQGFQLED TPKKSCVYKS GSSFSRGCSY TCAKRIQVPD
CCPGFFGTLC EPCPGGQGGV CSGHGQCQDR LLGSGECRCH EGFHGTACEM CELGRYGPNC
AGVCDCAHGL CQEGLQGDGS CVCNVGWQGP RCDQKITGPQ CPKKCDPNAN CIQDSAAAPA
CVCAAGYSGN GSYCSEVDPC ANNHGGCSPH ANCTKVAPGQ RTCTCHDGYT GDGELCQEAN
GCLIRHGGCH VHADCIPTGP QQVSCSCREG YSGDGIRTCV LLDPCSQNNG GCSPYAVCKG
AGDGQRTCTC DAAHTVGDGF TCRARVGLEL LRDRHASFFS LHLLEYKELK GDGPFTIFVP
RADLMTNLSQ DELARIRANR QLVFRYHVVG CRRLSSQELL EEGYVTTLSG HPLRIHEREG
SIYVNDFARV VSSDQEAVNG VLHFIDRVLL PPDVLHWEPD AAPALRRNVT AAAEGFGYKI
FSSLVKEAGL LPLLQDASHR PLTMLWPTDS ALRALPADRQ AWLHHEDHRD KLAAILRGHV
IRNIEALASD LPNLGPLRTM HGTPISFSCS RARPGELTVG EEDARIVQRH LPFEGGLAYG
IDQLLEPPGL GARCDRFETR PLRLKICSIC GLEPPCPEGS QEQGSPETCW RYYSKFWTSP
PLHSLALRSI WARSSLWGQP QGLGRGCHRN CVTTTWKPSC CPGHYGSECR ACPGGAGSPC
SGRGVCMDGM SGSGQCQCHA RFTGTACELC APGAFGPQCQ ACHCSSHGRC DEGLGGSGSC
FCDEGWTGPS CEVQLKLQPV CTPPCAPQAA CRADNSCECG LGYEGDGHTC TVVDLCQEGR
GGCSEHANCS QVGTAVTCTC LPAYEGDGWS CRARDPCADG RRGGCHEHAD CLNTGPNTRR
CVCHAGYVGD GLQCLEEPEP PVDRCLGQPP PCHVDAVCTD FHFQEKQAGV FHLQAPSGPY
GLNFSEAEAA CGAQGAVLAS LPQLSAAQKL GFHLCLVGWL ANGSAAHPVV FPAADCGGGQ
VGVVSLGARE NRSECWDAYC YRELDVACRC RRGFVGDGTS MCNGKLLDVL AATANFSTFY
GMLLGYANAT PRGLDFLDFL DDELTYKTLF VPVNEGFLDN MTLSGPDLEL HASNATFLST
NASQHTVLPA HSGLSLVFSA VGPDNSSGAP VAPGAVVVSH VVMWDIMAFN GIIHALARPL
LAPLQPRAVV APEAPPVAAG VGAVVAAGAL LGVVAGAFYL RARGKATGFG FSAFQAEEDA
EEDFTPWQEG TSPTLVSVPN PVFGSHDAFC EPFDDSLLED DFPDTQRILA VK
//