Q8WWQ8 (STAB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Stabilin-2

Alternative name(s):
FAS1 EGF-like and X-link domain-containing adhesion molecule 2
Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2
Short name=FEEL-2
Hyaluronan receptor for endocytosis

Cleaved into the following chain:

1. 190 kDa form stabilin-2
   Alternative name(s):
   190 kDa hyaluronan receptor for endocytosis

Gene names

Name:	STAB2
Synonyms:	FEEL2, FELL, FEX2, HARE

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2551 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalisation as well as HA and CS. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19
Subunit structure	Interacts with GULP1 and heparin. Also interacts with alpha-M/beta-2 integrin (ITGAM and ITGB2) and thymosin beta 4 (TMSB4X and/or TMSB4Y). Ref.12 Ref.15 Ref.16
Subcellular location	Cell membrane; Single-pass type I membrane protein. Cytoplasm. Note: Only a small amount appears to be present at the cell surface. Ref.8 Ref.12
Tissue specificity	Highly expressed in sinusoidal endothelial cells of liver, spleen and lymph nodes. Also expressed in non SEC-cells such as HMDMs (monocyte-derivedmacrophages), HAMs (T-cell leukemia virus type 1-associated myelopathy), and several macrophage cell line. Ref.1 Ref.2 Ref.6 Ref.9 Ref.12 Ref.14
Domain	Recognizes phosphatidyl serine via its epidermal growth factor-like domains.
Post-translational modification	Glycosylated. Ref.8 Proteolytically processed to yield a 190 kDa protein. Ref.6
Sequence similarities	Contains 17 EGF-like domains. Contains 7 FAS1 domains. Contains 2 laminin EGF-like domains. Contains 1 Link domain.
Sequence caution	The sequence AAF82398.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAD18723.1 differs from that shown. Reason: Frameshift at positions 240, 253, 588 and 1586.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Laminin EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Hyaluronic acid
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Non-traceable author statement Ref.2. Source: UniProtKB carbohydrate metabolic process Traceable author statement. Source: Reactome cell adhesion Non-traceable author statement Ref.2. Source: UniProtKB defense response to bacterium Inferred from direct assay Ref.2. Source: UniProtKB hyaluronan catabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA external side of plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to plasma membrane Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	Gram-negative bacterial cell surface binding Inferred from direct assay Ref.1. Source: UniProtKB hyaluronic acid binding Inferred from sequence or structural similarity. Source: UniProtKB low-density lipoprotein particle binding Inferred from direct assay Ref.2. Source: UniProtKB low-density lipoprotein receptor activity Inferred from direct assay Ref.2. Source: UniProtKB protein disulfide oxidoreductase activity Non-traceable author statement Ref.2. Source: UniProtKB scavenger receptor activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 2551	2532	Stabilin-2		PRO_0000007712
	Chain	1136 – 2551	1416	190 kDa form stabilin-2 Ref.6		PRO_0000007713
Regions
	Topological domain	20 – 2458	2439	Extracellular Potential
	Transmembrane	2459 – 2479	21	Helical; Potential
	Topological domain	2480 – 2551	72	Cytoplasmic Potential
	Domain	108 – 148	41	EGF-like 1
	Domain	156 – 193	38	EGF-like 2
	Domain	195 – 236	42	EGF-like 3
	Domain	237 – 276	40	EGF-like 4
	Domain	322 – 362	41	EGF-like 5
	Domain	371 – 505	135	FAS1 1
	Domain	515 – 652	138	FAS1 2
	Domain	736 – 776	41	EGF-like 6
	Domain	826 – 866	41	EGF-like 7
	Domain	867 – 909	43	EGF-like 8
	Domain	910 – 952	43	EGF-like 9
	Domain	953 – 992	40	EGF-like 10
	Domain	994 – 1127	134	FAS1 3
	Domain	1137 – 1265	129	FAS1 4
	Domain	1343 – 1408	66	Laminin EGF-like 1
	Domain	1432 – 1470	39	EGF-like 11
	Domain	1471 – 1512	42	EGF-like 12
	Domain	1513 – 1554	42	EGF-like 13
	Domain	1555 – 1594	40	EGF-like 14
	Domain	1596 – 1724	129	FAS1 5
	Domain	1740 – 1881	142	FAS1 6
	Domain	1957 – 2022	66	Laminin EGF-like 2
	Domain	2047 – 2081	35	EGF-like 15
	Domain	2082 – 2122	41	EGF-like 16
	Domain	2123 – 2165	43	EGF-like 17
	Domain	2198 – 2291	94	Link
	Domain	2311 – 2446	136	FAS1 7
	Region	2504 – 2514	11	Interaction with TMSB4X
Amino acid modifications
	Modified residue	2497	1	Phosphoserine By similarity
	Glycosylation	133	1	N-linked (GlcNAc...) Potential
	Glycosylation	337	1	N-linked (GlcNAc...) Potential
	Glycosylation	449	1	N-linked (GlcNAc...) Potential
	Glycosylation	619	1	N-linked (GlcNAc...) Potential
	Glycosylation	720	1	N-linked (GlcNAc...) Potential
	Glycosylation	761	1	N-linked (GlcNAc...) Potential
	Glycosylation	847	1	N-linked (GlcNAc...) Potential
	Glycosylation	925	1	N-linked (GlcNAc...) Potential
	Glycosylation	1016	1	N-linked (GlcNAc...) Potential
	Glycosylation	1028	1	N-linked (GlcNAc...) Potential
	Glycosylation	1100	1	N-linked (GlcNAc...) Potential
	Glycosylation	1247	1	N-linked (GlcNAc...) Potential
	Glycosylation	1275	1	N-linked (GlcNAc...) Potential
	Glycosylation	1367	1	N-linked (GlcNAc...) Potential
	Glycosylation	1429	1	N-linked (GlcNAc...) Potential
	Glycosylation	1437	1	N-linked (GlcNAc...) Potential
	Glycosylation	1465	1	N-linked (GlcNAc...) Potential
	Glycosylation	1573	1	N-linked (GlcNAc...) Potential
	Glycosylation	1679	1	N-linked (GlcNAc...) Potential
	Glycosylation	1743	1	N-linked (GlcNAc...) Ref.20
	Glycosylation	1993	1	N-linked (GlcNAc...) Potential
	Glycosylation	2064	1	N-linked (GlcNAc...) Potential
	Glycosylation	2280	1	N-linked (GlcNAc...) Potential
	Glycosylation	2296	1	N-linked (GlcNAc...) Potential
	Glycosylation	2336	1	N-linked (GlcNAc...) Potential
	Glycosylation	2368	1	N-linked (GlcNAc...) Potential
	Glycosylation	2382	1	N-linked (GlcNAc...) Potential
	Glycosylation	2393	1	N-linked (GlcNAc...) Potential
	Disulfide bond	112 ↔ 126		By similarity
	Disulfide bond	120 ↔ 136		By similarity
	Disulfide bond	138 ↔ 147		By similarity
	Disulfide bond	160 ↔ 171		By similarity
	Disulfide bond	164 ↔ 181		By similarity
	Disulfide bond	183 ↔ 192		By similarity
	Disulfide bond	199 ↔ 210		By similarity
	Disulfide bond	204 ↔ 222		By similarity
	Disulfide bond	224 ↔ 235		By similarity
	Disulfide bond	241 ↔ 252		By similarity
	Disulfide bond	246 ↔ 262		By similarity
	Disulfide bond	264 ↔ 275		By similarity
	Disulfide bond	326 ↔ 338		By similarity
	Disulfide bond	332 ↔ 348		By similarity
	Disulfide bond	350 ↔ 361		By similarity
	Disulfide bond	740 ↔ 754		By similarity
	Disulfide bond	748 ↔ 764		By similarity
	Disulfide bond	766 ↔ 775		By similarity
	Disulfide bond	830 ↔ 843		By similarity
	Disulfide bond	837 ↔ 852		By similarity
	Disulfide bond	854 ↔ 865		By similarity
	Disulfide bond	871 ↔ 885		By similarity
	Disulfide bond	879 ↔ 895		By similarity
	Disulfide bond	897 ↔ 908		By similarity
	Disulfide bond	914 ↔ 928		By similarity
	Disulfide bond	922 ↔ 938		By similarity
	Disulfide bond	940 ↔ 951		By similarity
	Disulfide bond	957 ↔ 970		By similarity
	Disulfide bond	964 ↔ 980		By similarity
	Disulfide bond	1348 ↔ 1362		By similarity
	Disulfide bond	1356 ↔ 1372		By similarity
	Disulfide bond	1374 ↔ 1383		By similarity
	Disulfide bond	1395 ↔ 1406		By similarity
	Disulfide bond	1399 ↔ 1416		By similarity
	Disulfide bond	1418 ↔ 1427		By similarity
	Disulfide bond	1436 ↔ 1446		By similarity
	Disulfide bond	1440 ↔ 1456		By similarity
	Disulfide bond	1458 ↔ 1469		By similarity
	Disulfide bond	1475 ↔ 1488		By similarity
	Disulfide bond	1482 ↔ 1498		By similarity
	Disulfide bond	1500 ↔ 1511		By similarity
	Disulfide bond	1517 ↔ 1530		By similarity
	Disulfide bond	1524 ↔ 1540		By similarity
	Disulfide bond	1542 ↔ 1553		By similarity
	Disulfide bond	1559 ↔ 1572		By similarity
	Disulfide bond	1566 ↔ 1582		By similarity
	Disulfide bond	1962 ↔ 1976		By similarity
	Disulfide bond	1970 ↔ 1986		By similarity
	Disulfide bond	1988 ↔ 1997		By similarity
	Disulfide bond	2009 ↔ 2020		By similarity
	Disulfide bond	2014 ↔ 2030		By similarity
	Disulfide bond	2032 ↔ 2041		By similarity
	Disulfide bond	2051 ↔ 2061		By similarity
	Disulfide bond	2055 ↔ 2067		By similarity
	Disulfide bond	2069 ↔ 2080		By similarity
	Disulfide bond	2086 ↔ 2099		By similarity
	Disulfide bond	2093 ↔ 2108		By similarity
	Disulfide bond	2110 ↔ 2121		By similarity
	Disulfide bond	2127 ↔ 2141		By similarity
	Disulfide bond	2135 ↔ 2151		By similarity
	Disulfide bond	2153 ↔ 2164		By similarity
	Disulfide bond	2220 ↔ 2289		By similarity
	Disulfide bond	2244 ↔ 2265		By similarity
Natural variations
	Natural variant	110	1	I → V. Corresponds to variant rs17034186 [ dbSNP | Ensembl ].		VAR_048995
	Natural variant	306	1	E → K. Corresponds to variant rs12319476 [ dbSNP | Ensembl ].		VAR_048996
	Natural variant	510	1	P → H. Ref.1 Ref.2 Corresponds to variant rs1609860 [ dbSNP | Ensembl ].		VAR_019541
	Natural variant	787	1	R → Q. Corresponds to variant rs17034336 [ dbSNP | Ensembl ].		VAR_048997
	Natural variant	881	1	R → H. Corresponds to variant rs7973658 [ dbSNP | Ensembl ].		VAR_048998
	Natural variant	1736	1	N → T. Corresponds to variant rs17034433 [ dbSNP | Ensembl ].		VAR_048999
	Natural variant	2039	1	P → T. Ref.4 Ref.5 Corresponds to variant rs7306642 [ dbSNP | Ensembl ].		VAR_049000
	Natural variant	2401	1	L → V. Ref.5 Ref.7 Corresponds to variant rs2271637 [ dbSNP | Ensembl ].		VAR_049001
	Natural variant	2519	1	Y → S. Corresponds to variant rs3751197 [ dbSNP | Ensembl ].		VAR_049002
Experimental info
	Sequence conflict	67	1	G → R in BAD18723. Ref.5
	Sequence conflict	152	1	D → A in BAD18723. Ref.5
	Sequence conflict	887	1	K → N in BAD18723. Ref.5
	Sequence conflict	1136	1	S → L AA sequence Ref.8
	Sequence conflict	1151	1	S → P in CAC82105. Ref.1
	Sequence conflict	1276	1	D → A in CAC82105. Ref.1
	Sequence conflict	1522	1	G → C in BAD18723. Ref.5
	Sequence conflict	1557	1	N → Y in AAO39681. Ref.6
	Sequence conflict	1599 – 1600	2	IY → HE in AAF82398. Ref.7
	Sequence conflict	1854	1	F → S in BAD18723. Ref.5
	Sequence conflict	2249	1	L → V in BAD18723. Ref.5
	Sequence conflict	2253	1	R → G in BAD18723. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8WWQ8 [UniParc]. Last modified April 17, 2007. Version 3. Checksum: 3ACB6A6C3CB80044	FASTA	2,551	276,988
	10 20 30 40 50 60 MMLQHLVIFC LGLVVQNFCS PAETTGQARR CDRKSLLTIR TECRSCALNL GVKCPDGYTM 70 80 90 100 110 120 ITSGSVGVRD CRYTFEVRTY SLSLPGCRHI CRKDYLQPRC CPGRWGPDCI ECPGGAGSPC 130 140 150 160 170 180 NGRGSCAEGM EGNGTCSCQE GFGGTACETC ADDNLFGPSC SSVCNCVHGV CNSGLDGDGT 190 200 210 220 230 240 CECYSAYTGP KCDKPIPECA ALLCPENSRC SPSTEDENKL ECKCLPNYRG DGKYCDPINP 250 260 270 280 290 300 CLRKICHPHA HCTYLGPNRH SCTCQEGYRG DGQVCLPVDP CQINFGNCPT KSTVCKYDGP 310 320 330 340 350 360 GQSHCECKEH YQNFVPGVGC SMTDICKSDN PCHRNANCTT VAPGRTECIC QKGYVGDGLT 370 380 390 400 410 420 CYGNIMERLR ELNTEPRGKW QGRLTSFISL LDKAYAWPLS KLGPFTVLLP TDKGLKGFNV 430 440 450 460 470 480 NELLVDNKAA QYFVKLHIIA GQMNIEYMNN TDMFYTLTGK SGEIFNSDKD NQIKLKLHGG 490 500 510 520 530 540 KKKVKIIQGD IIASNGLLHI LDRAMDKLEP TFESNNEQTI MTMLQPRYSK FRSLLEETNL 550 560 570 580 590 600 GHALDEDGVG GPYTIFVPNN EALNNMKDGT LDYLLSPEGS RKLLELVRYH IVPFTQLEVA 610 620 630 640 650 660 TLISTPHIRS MANQLIQFNT TDNGQILAND VAMEEIEITA KNGRIYTLTG VLIPPSIVPI 670 680 690 700 710 720 LPHRCDETKR EMKLGTCVSC SLVYWSRCPA NSEPTALFTH RCVYSGRFGS LKSGCARYCN 730 740 750 760 770 780 ATVKIPKCCK GFYGPDCNQC PGGFSNPCSG NGQCADSLGG NGTCICEEGF QGSQCQFCSD 790 800 810 820 830 840 PNKYGPRCNK KCLCVHGTCN NRIDSDGACL TGTCRDGSAG RLCDKQTSAC GPYVQFCHIH 850 860 870 880 890 900 ATCEYSNGTA SCICKAGYEG DGTLCSEMDP CTGLTPGGCS RNAECIKTGT GTHTCVCQQG 910 920 930 940 950 960 WTGNGRDCSE INNCLLPSAG GCHDNASCLY VGPGQNECEC KKGFRGNGID CEPITSCLEQ 970 980 990 1000 1010 1020 TGKCHPLASC QSTSSGVWSC VCQEGYEGDG FLCYGNAAVE LSFLSEAAIF NRWINNASLQ 1030 1040 1050 1060 1070 1080 PTLSATSNLT VLVPSQQATE DMDQDEKSFW LSQSNIPALI KYHMLLGTYR VADLQTLSSS 1090 1100 1110 1120 1130 1140 DMLATSLQGN FLHLAKVDGN ITIEGASIVD GDNAATNGVI HIINKVLVPQ RRLTGSLPNL 1150 1160 1170 1180 1190 1200 LMRLEQMPDY SIFRGYIIQY NLANAIEAAD AYTVFAPNNN AIENYIREKK VLSLEEDVLR 1210 1220 1230 1240 1250 1260 YHVVLEEKLL KNDLHNGMHR ETMLGFSYFL SFFLHNDQLY VNEAPINYTN VATDKGVIHG 1270 1280 1290 1300 1310 1320 LGKVLEIQKN RCDNNDTTII RGRCRTCSSE LTCPFGTKSL GNEKRRCIYT SYFMGRRTLF 1330 1340 1350 1360 1370 1380 IGCQPKCVRT VITRECCAGF FGPQCQPCPG NAQNVCFGNG ICLDGVNGTG VCECGEGFSG 1390 1400 1410 1420 1430 1440 TACETCTEGK YGIHCDQACS CVHGRCNQGP LGDGSCDCDV GWRGVHCDNA TTEDNCNGTC 1450 1460 1470 1480 1490 1500 HTSANCLTNS DGTASCKCAA GFQGNGTICT AINACEISNG GCSAKADCKR TTPGRRVCTC 1510 1520 1530 1540 1550 1560 KAGYTGDGIV CLEINPCLEN HGGCDKNAEC TQTGPNQAAC NCLPAYTGDG KVCTLINVCL 1570 1580 1590 1600 1610 1620 TKNGGCSEFA ICNHTGQVER TCTCKPNYIG DGFTCRGSIY QELPKNPKTS QYFFQLQEHF 1630 1640 1650 1660 1670 1680 VKDLVGPGPF TVFAPLSAAF DEEARVKDWD KYGLMPQVLR YHVVACHQLL LENLKLISNA 1690 1700 1710 1720 1730 1740 TSLQGEPIVI SVSQSTVYIN NKAKIISSDI ISTNGIVHII DKLLSPKNLL ITPKDNSGRI 1750 1760 1770 1780 1790 1800 LQNLTTLATN NGYIKFSNLI QDSGLLSVIT DPIHTPVTLF WPTDQALHAL PAEQQDFLFN 1810 1820 1830 1840 1850 1860 QDNKDKLKEY LKFHVIRDAK VLAVDLPTST AWKTLQGSEL SVKCGAGRDI GDLFLNGQTC 1870 1880 1890 1900 1910 1920 RIVQRELLFD LGVAYGIDCL LIDPTLGGRC DTFTTFDASG ECGSCVNTPS CPRWSKPKGV 1930 1940 1950 1960 1970 1980 KQKCLYNLPF KRNLEGCRER CSLVIQIPRC CKGYFGRDCQ ACPGGPDAPC NNRGVCLDQY 1990 2000 2010 2020 2030 2040 SATGECKCNT GFNGTACEMC WPGRFGPDCL PCGCSDHGQC DDGITGSGQC LCETGWTGPS 2050 2060 2070 2080 2090 2100 CDTQAVLPAV CTPPCSAHAT CKENNTCECN LDYEGDGITC TVVDFCKQDN GGCAKVARCS 2110 2120 2130 2140 2150 2160 QKGTKVSCSC QKGYKGDGHS CTEIDPCADG LNGGCHEHAT CKMTGPGKHK CECKSHYVGD 2170 2180 2190 2200 2210 2220 GLNCEPEQLP IDRCLQDNGQ CHADAKCVDL HFQDTTVGVF HLRSPLGQYK LTFDKAREAC 2230 2240 2250 2260 2270 2280 ANEAATMATY NQLSYAQKAK YHLCSAGWLE TGRVAYPTAF ASQNCGSGVV GIVDYGPRPN 2290 2300 2310 2320 2330 2340 KSEMWDVFCY RMKDVNCTCK VGYVGDGFSC SGNLLQVLMS FPSLTNFLTE VLAYSNSSAR 2350 2360 2370 2380 2390 2400 GRAFLEHLTD LSIRGTLFVP QNSGLGENET LSGRDIEHHL ANVSMFFYND LVNGTTLQTR 2410 2420 2430 2440 2450 2460 LGSKLLITAS QDPLQPTETR FVDGRAILQW DIFASNGIIH VISRPLKAPP APVTLTHTGL 2470 2480 2490 2500 2510 2520 GAGIFFAIIL VTGAVALAAY SYFRINRRTI GFQHFESEED INVAALGKQQ PENISNPLYE 2530 2540 2550 STTSAPPEPS YDPFTDSEER QLEGNDPLRT L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Stabilin-1 and -2 constitute a novel family of fasciclin-like hyaluronan receptor homologues." Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P., Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J., Longati P., Velten F.W., Johansson S., Goerdt S. Biochem. J. 362:155-164(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT HIS-510.
[2]	"FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and angiogenesis-modulating activities." Adachi H., Tsujimoto M. J. Biol. Chem. 277:34264-34270(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT HIS-510.
[3]	"FEX2, a novel cell adhesion molecule of Fas-1 superfamily mediates cell-cell interaction." Park S.-Y., Kim I.-S. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-2551, VARIANT THR-2039. Tissue: Spleen.
[5]	"The nucleotide sequence of a long cDNA clone isolated from human spleen." Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O. Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-2551, VARIANTS THR-2039 AND VAL-2401. Tissue: Spleen.
[6]	"Purification and molecular identification of the human hyaluronan receptor for endocytosis." Zhou B., McGary C.T., Weigel J.A., Saxena A., Weigel P.H. Glycobiology 13:339-349(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1136-2551, PROTEIN SEQUENCE OF 1136-1144; 1257-1269; 1597-1605; 1623-1645; 1652-1660; 1813-1817; 1834-1843; 1914-1918; 1953-1957; 2204-2217; 2211-2215 AND 2355-2367, TISSUE SPECIFICITY.
[7]	"Molecular cloning and characterization of human FELL sharing homology with CD44." Tao Q., Zhang W., Cao X. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1599-2551, VARIANT VAL-2401.
[8]	"Expression, processing, and glycosaminoglycan binding activity of the recombinant human 315-kDa hyaluronic acid receptor for endocytosis (HARE)." Harris E.N., Kyosseva S.V., Weigel J.A., Weigel P.H. J. Biol. Chem. 282:2785-2797(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1136-1144, GLYCOSYLATION, SUBCELLULAR LOCATION, FUNCTION.
[9]	"FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end products." Tamura Y., Adachi H., Osuga J., Ohashi K., Yahagi N., Sekiya M., Okazaki H., Tomita S., Iizuka Y., Shimano H., Nagai R., Kimura S., Tsujimoto M., Ishibashi S. J. Biol. Chem. 278:12613-12617(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[10]	"Endocytic function, glycosaminoglycan specificity, and antibody sensitivity of the recombinant human 190-kDa hyaluronan receptor for endocytosis (HARE)." Harris E.N., Weigel J.A., Weigel P.H. J. Biol. Chem. 279:36201-36209(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Stabilin-1 and stabilin-2 are both directed into the early endocytic pathway in hepatic sinusoidal endothelium via interactions with clathrin/AP-2, independent of ligand binding." Hansen B., Longati P., Elvevold K., Nedredal G.-I., Schledzewski K., Olsen R., Falkowski M., Kzhyshkowska J., Carlsson F., Johansson S., Smedsroed B., Goerdt S., Johansson S., McCourt P. Exp. Cell Res. 303:160-173(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Stabilin-2 is involved in lymphocyte adhesion to the hepatic sinusoidal endothelium via the interaction with alphaMbeta2 integrin." Jung M.Y., Park S.Y., Kim I.S. J. Leukoc. Biol. 82:1156-1165(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ALPHA-M/BETA-2 [ITGAM/ITGB2] INTEGRIN.
[13]	Erratum Jung M.Y., Park S.Y., Kim I.S. J. Leukoc. Biol. 83:438-438(2008)
[14]	"Rapid cell corpse clearance by stabilin-2, a membrane phosphatidylserine receptor." Park S.Y., Jung M.Y., Kim H.J., Lee S.J., Kim S.Y., Lee B.H., Kwon T.H., Park R.W., Kim I.S. Cell Death Differ. 15:192-201(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[15]	"Thymosin beta4 is involved in stabilin-2-mediated apoptotic cell engulfment." Lee S.J., So I.S., Park S.Y., Kim I.S. FEBS Lett. 582:2161-2166(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TMSB4X.
[16]	"Requirement of adaptor protein GULP during stabilin-2-mediated cell corpse engulfment." Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S. J. Biol. Chem. 283:10593-10600(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GULP1.
[17]	"The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a systemic clearance receptor for heparin." Harris E.N., Weigel J.A., Weigel P.H. J. Biol. Chem. 283:17341-17350(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"Epidermal growth factor-like domain repeat of stabilin-2 recognizes phosphatidylserine during cell corpse clearance." Park S.-Y., Kim S.-Y., Jung M.-Y., Bae D.-J., Kim I.-S. Mol. Cell. Biol. 28:5288-5298(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Rat and human HARE/stabilin-2 are clearance receptors for high- and low-molecular-weight heparins." Harris E.N., Baggenstoss B.A., Weigel P.H. Am. J. Physiol. 296:G1191-G1199(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1743, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ295695 mRNA. Translation: CAC82105.1. AB052958 mRNA. Translation: BAC15608.1. AY311388 mRNA. Translation: AAP74958.1. AK024503 mRNA. Translation: BAB15793.1. AK074051 mRNA. Translation: BAB84877.1. AK160380 mRNA. Translation: BAD18723.1. Frameshift. AY227444 mRNA. Translation: AAO39681.1. AF160476 mRNA. Translation: AAF82398.1. Different initiation.
IPI	IPI00292579.
RefSeq	NP_060034.9. NM_017564.9.
UniGene	Hs.408249.
3D structure databases
ProteinModelPortal	Q8WWQ8.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-6542238.
STRING	9606.ENSP00000373539.
PTM databases
PhosphoSite	Q8WWQ8.
Polymorphism databases
DMDM	145559531.
Proteomic databases
PaxDb	Q8WWQ8.
PRIDE	Q8WWQ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000388887; ENSP00000373539; ENSG00000136011.
GeneID	55576.
KEGG	hsa:55576.
UCSC	uc001tjw.3. human.
Organism-specific databases
CTD	55576.
GeneCards	GC12P103981.
HGNC	HGNC:18629. STAB2.
HPA	HPA026871.
MIM	608561. gene.
neXtProt	NX_Q8WWQ8.
PharmGKB	PA38611.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2335.
HOVERGEN	HBG079218.
InParanoid	Q8WWQ8.
OMA	IPKCCKG.
OrthoDB	EOG4QNMV8.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	Q8WWQ8.
Bgee	Q8WWQ8.
CleanEx	HS_STAB2.
Genevestigator	Q8WWQ8.
GermOnline	ENSG00000136011. Homo sapiens.
Family and domain databases
Gene3D	2.30.180.10. 7 hits. 2.40.155.10. 8 hits. 3.10.100.10. 1 hit.
InterPro	IPR016186. C-type_lectin-like. IPR016187. C-type_lectin_fold. IPR000742. EG-like_dom. IPR013032. EGF-like_CS. IPR024731. EGF_dom_MSP1-like. IPR002049. EGF_laminin. IPR000782. FAS1_domain. IPR023413. GFP_like. IPR009030. Growth_fac_rcpt. IPR000538. Link. [Graphical view]
Pfam	PF12947. EGF_3. 7 hits. PF02469. Fasciclin. 7 hits. PF00193. Xlink. 1 hit. [Graphical view]
SMART	SM00181. EGF. 20 hits. SM00554. FAS1. 7 hits. SM00445. LINK. 1 hit. [Graphical view]
SUPFAM	SSF82153. BIgH3_FAS1. 7 hits. SSF56436. C-type_lectin_fold. 1 hit. SSF57184. Grow_fac_recept. 1 hit.
PROSITE	PS00022. EGF_1. 7 hits. PS01186. EGF_2. 16 hits. PS50026. EGF_3. 21 hits. PS01248. EGF_LAM_1. 2 hits. PS50027. EGF_LAM_2. False negative. PS50213. FAS1. 7 hits. PS01241. LINK_1. 1 hit. PS50963. LINK_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55576.
NextBio	60076.
SOURCE	Search...

Entry information

Entry name

STAB2_HUMAN

Accession

Primary (citable) accession number: Q8WWQ8
Secondary accession number(s): Q6ZMK2 , Q7Z5N9, Q86UR4, Q8IUG9, Q8TES1, Q9H7H7, Q9NRY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	April 17, 2007
Last modified:	May 1, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.