STAB2_RAT
ID STAB2_RAT Reviewed; 1431 AA.
AC Q8CFM6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Stabilin-2;
DE AltName: Full=Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2;
DE Short=FEEL-2;
DE AltName: Full=Hyaluronan receptor for endocytosis;
DE Contains:
DE RecName: Full=175 kDa stabilin-2;
DE AltName: Full=175 kDa hyaluronan receptor for endocytosis;
DE Flags: Precursor; Fragment;
GN Name=Stab2 {ECO:0000250|UniProtKB:Q8WWQ8};
GN Synonyms=Feel2, Hare {ECO:0000303|PubMed:12181351};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG13634.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-18; 62-73; 103-120;
RP 122-136; 488-509; 604-619; 651-668; 1070-1075 AND 1120-1129, AND FUNCTION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAG13634.1};
RC TISSUE=Endothelial cell;
RX PubMed=12181351; DOI=10.1091/mbc.02-03-0048;
RA Zhou B., Weigel J.A., Saxena A., Weigel P.H.;
RT "Molecular cloning and functional expression of the rat 175-kDa hyaluronan
RT receptor for endocytosis.";
RL Mol. Biol. Cell 13:2853-2868(2002).
RN [2]
RP FUNCTION.
RX PubMed=9061360; DOI=10.1093/glycob/7.1.15;
RA Yannariello-Brown J., Zhou B., Weigel P.H.;
RT "Identification of a 175 kDa protein as the ligand-binding subunit of the
RT rat liver sinusoidal endothelial cell hyaluronan receptor.";
RL Glycobiology 7:15-21(1997).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15572036; DOI=10.1016/j.yexcr.2004.09.017;
RA Hansen B., Longati P., Elvevold K., Nedredal G.-I., Schledzewski K.,
RA Olsen R., Falkowski M., Kzhyshkowska J., Carlsson F., Johansson S.,
RA Smedsroed B., Goerdt S., Johansson S., McCourt P.;
RT "Stabilin-1 and stabilin-2 are both directed into the early endocytic
RT pathway in hepatic sinusoidal endothelium via interactions with
RT clathrin/AP-2, independent of ligand binding.";
RL Exp. Cell Res. 303:160-173(2005).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17450384; DOI=10.1007/s00441-007-0387-5;
RA Yoshida M., Nishikawa Y., Omori Y., Yoshioka T., Tokairin T., McCourt P.,
RA Enomoto K.;
RT "Involvement of signaling of VEGF and TGF-beta in differentiation of
RT sinusoidal endothelial cells during culture of fetal rat liver cells.";
RL Cell Tissue Res. 329:273-282(2007).
RN [5]
RP FUNCTION.
RX PubMed=19359419; DOI=10.1152/ajpgi.90717.2008;
RA Harris E.N., Baggenstoss B.A., Weigel P.H.;
RT "Rat and human HARE/stabilin-2 are clearance receptors for high- and low-
RT molecular-weight heparins.";
RL Am. J. Physiol. 296:G1191-G1199(2009).
CC -!- FUNCTION: Phosphatidylserine receptor that enhances the engulfment of
CC apoptotic cells. Hyaluronan receptor that binds to and mediates
CC endocytosis of hyaluronic acid (HA). Acts also, in different species,
CC as a primary systemic scavenger receptor for heparin (Hep), chondroitin
CC sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG),
CC acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides
CC and advanced glycation end products (AGE). May serve to maintain tissue
CC integrity by supporting extracellular matrix turnover or it may
CC contribute to maintaining fluidity of bodily liquids by resorption of
CC hyaluronan. Counter receptor which plays an important role in
CC lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-
CC positive and Gram-negative bacteria and may play a role in defense
CC against bacterial infection. The proteolytically processed 175 kDa form
CC also functions as an endocytosis receptor for heparin internalization
CC as well as HA and CS. {ECO:0000269|PubMed:12181351,
CC ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:19359419,
CC ECO:0000269|PubMed:9061360}.
CC -!- SUBUNIT: Interacts with GULP1, heparin, alpha-M/beta-2 integrin (ITGAM
CC and ITGB2), and thymosin beta 4 (TMSB4X). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WWQ8}. Cell
CC membrane {ECO:0000269|PubMed:15572036}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:15572036}.
CC -!- TISSUE SPECIFICITY: Initially expressed in all vascular cells,
CC including those of sinusoidal-like structures, vitellin veins, and
CC hepatic veins or sinus venosus, in E13.5 fetal liver. The expression
CC then progressively disappears in the portal and hepatic veins, but the
CC expression in sinusoidals endothelial cells (SECs) is retained and
CC becomes stronger during development. {ECO:0000269|PubMed:17450384}.
CC -!- DOMAIN: Recognizes phosphatidyl serine via its epidermal growth factor-
CC like domains.
CC -!- PTM: Glycosylated.
CC -!- PTM: Proteolytically processed to yield a 175 kDa protein.
CC {ECO:0000269|PubMed:12181351}.
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DR EMBL; AY007370; AAG13634.1; -; mRNA.
DR AlphaFoldDB; Q8CFM6; -.
DR SMR; Q8CFM6; -.
DR STRING; 10116.ENSRNOP00000056294; -.
DR GlyGen; Q8CFM6; 15 sites.
DR PRIDE; Q8CFM6; -.
DR UCSC; RGD:628822; rat.
DR RGD; 628822; Stab2.
DR eggNOG; KOG1218; Eukaryota.
DR InParanoid; Q8CFM6; -.
DR PhylomeDB; Q8CFM6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:RGD.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; ISO:RGD.
DR GO; GO:0005044; F:scavenger receptor activity; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR Gene3D; 2.30.180.10; -; 4.
DR Gene3D; 3.10.100.10; -; 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 Pfam; PF12947; EGF_3; 5.
DR Pfam; PF02469; Fasciclin; 3.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00554; FAS1; 4.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF82153; SSF82153; 4.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 10.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50213; FAS1; 4.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Endocytosis; Glycoprotein; Hyaluronic acid;
KW Laminin EGF-like domain; Membrane; Receptor; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..1431
FT /note="Stabilin-2"
FT /id="PRO_0000007716"
FT CHAIN 1..1431
FT /note="175 kDa stabilin-2"
FT /id="PRO_0000007717"
FT TOPO_DOM <1..1322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1323..1343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1344..1431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 2..130
FT /note="FAS1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 207..272
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 296..334
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 335..376
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 377..418
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 419..460
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 460..588
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 604..745
FT /note="FAS1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 822..887
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 947..987
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 988..1030
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1063..1156
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 1176..1310
FT /note="FAS1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 1368..1378
FT /note="Interaction with TMSB4X"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 212..226
FT /evidence="ECO:0000250"
FT DISULFID 220..236
FT /evidence="ECO:0000250"
FT DISULFID 238..247
FT /evidence="ECO:0000250"
FT DISULFID 259..270
FT /evidence="ECO:0000250"
FT DISULFID 263..280
FT /evidence="ECO:0000250"
FT DISULFID 282..291
FT /evidence="ECO:0000250"
FT DISULFID 300..310
FT /evidence="ECO:0000250"
FT DISULFID 304..320
FT /evidence="ECO:0000250"
FT DISULFID 322..333
FT /evidence="ECO:0000250"
FT DISULFID 339..352
FT /evidence="ECO:0000250"
FT DISULFID 346..362
FT /evidence="ECO:0000250"
FT DISULFID 364..375
FT /evidence="ECO:0000250"
FT DISULFID 381..394
FT /evidence="ECO:0000250"
FT DISULFID 388..404
FT /evidence="ECO:0000250"
FT DISULFID 406..417
FT /evidence="ECO:0000250"
FT DISULFID 423..436
FT /evidence="ECO:0000250"
FT DISULFID 430..446
FT /evidence="ECO:0000250"
FT DISULFID 448..459
FT /evidence="ECO:0000250"
FT DISULFID 827..841
FT /evidence="ECO:0000250"
FT DISULFID 835..851
FT /evidence="ECO:0000250"
FT DISULFID 853..862
FT /evidence="ECO:0000250"
FT DISULFID 874..885
FT /evidence="ECO:0000250"
FT DISULFID 879..895
FT /evidence="ECO:0000250"
FT DISULFID 897..906
FT /evidence="ECO:0000250"
FT DISULFID 951..964
FT /evidence="ECO:0000250"
FT DISULFID 958..973
FT /evidence="ECO:0000250"
FT DISULFID 975..986
FT /evidence="ECO:0000250"
FT DISULFID 992..1006
FT /evidence="ECO:0000250"
FT DISULFID 1000..1016
FT /evidence="ECO:0000250"
FT DISULFID 1018..1029
FT /evidence="ECO:0000250"
FT DISULFID 1085..1154
FT /evidence="ECO:0000250"
FT DISULFID 1109..1130
FT /evidence="ECO:0000250"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAG13634.1"
SQ SEQUENCE 1431 AA; 155914 MW; 3340A8F7AF366722 CRC64;
SLPSLLTRLE QMPDYSIFRG YIIHYNLASA IESADAYTVF VPNNEAIENY IREKKATSLK
EDILRYHVVL GEKLLKNDLH NGMHRETMLG FSYLLAFFLR NDQLYVNEAP INYTNVATDK
GVIHGLEKVL EIQKNRCDNN DTIIVRGECG KCSQQAPCPL ETKPLRETRK CIYSIYFMGK
RSVFIGCQPQ CVRTIITRAC CAGFFGPQCQ ACPGRGQNVC SGNGFCLDGV NGTGTCQCGL
GFNGTACETC TEGKYGIHCD QACSCVHGRC SQGPLGDGSC DCDVGWRGVK CDMEITTDNC
NGTCHTSANC LLDPDGKASC KCAAGFRGNG TVCTAINACE TSNGGCSTKA DCKRTTPGNR
VCVCKAGYTG DGIVCLEINP CLENHGGCDR NAECTQTGPN QAVCNCLPKY TGDGKVCSLI
NVCLTNNGGC SPFAFCNYTE QDQRICTCKP DYTGDGIVCR GSIYGELPKN PSTSQYFFQL
QEHAVRELAG PGPFTVFAPL SSSFNHEPRI KDWDQQGLMS QVLRYHVVGC QQLLLDNLKV
TTSATTLQGE PVSISVSQDT VFINNEAKVL SSDIISTNGV IHVIDKLLSP KNLLITPKDA
LGRVLQNLTT VAANHGYTKF SKLIQDSGLL SVITDSIHTP VTVFWPTDKA LEALPPEQQD
FLFNQDNKDK LKSYLKFHVI RDSKALASDL PRSASWKTLQ GSELSVRCGT GSDIGELFLN
EQMCRFIHRG LLFDVGVAYG IDCLLMNPTL GGRCDTFTTF DIPGECGSCI FTPKCPLKSK
PKGVKKKCIY NPLPFRRNVE GCQNLCTVVI QTPRCCHGYF MPDCQACPGG PDTPCNNRGM
CRDLYTPMGQ CLCHTGFNGT ACELCWHGRF GPDCQPRSCS EHGQCDEGIT GSGECLCETG
WTAASCDTPT AVFAVCTPAC SVHATCTENN TCVCNLNYEG DGITCTVVDF CKQNNGGCAK
VAKCSQKGTQ VSCSCKKGYK GDGYSCIEID PCADGVNGGC HEHATCRMTG PGKHKCECKS
HYVGDGVDCE PEQLPLDRCL QDNGQCHPDA SCADLYFQDT TVGVFHLRSP LGQYKLTFDK
AKEACAKEAA TIATYNQLSY AQKAKYHLCS AGWLESGRVA YPTTYASQKC GANVVGIVDY
GSRANKSEMW DVFCYRMKDV NCTCKAGYVG DGFSCSGNLL QVLMSFPSLT NFLTEVLAFS
KSSARGQAFL KHLTDLSIRG TLFVPQNSGL PGNKSLSGRD IEHHLTNVNV SFYNDLVNGT
FLRTMLGSQL LITFSQDQLH QETRFVDGRS ILQWDIIAAN GILHIISEPL RAPPTAATAA
HSGLGTGIFC AVVLVTGAIA LAAYSYFRLK QRTTGFQRFD QKRTLMSWLL ASSSPRISQT
LCMRPQRRHP QSPPVTPSQT LENRIWRTAT LWGHCGPDMR SQQATTVTVP R
