STAB2_MOUSE
ID STAB2_MOUSE Reviewed; 2559 AA.
AC Q8R4U0; Q8BM87;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 Contains:
DE RecName: Full=Short form stabilin-2;
DE Flags: Precursor;
GN Name=Stab2 {ECO:0000312|MGI:MGI:2178743}; Synonyms=Feel2, Hare;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAL91684.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAL91684.2};
RC TISSUE=Liver {ECO:0000312|EMBL:AAL91684.2};
RX PubMed=11829752; DOI=10.1042/0264-6021:3620155;
RA Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P.,
RA Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J.,
RA Longati P., Velten F.W., Johansson S., Goerdt S.;
RT "Stabilin-1 and -2 constitute a novel family of fasciclin-like hyaluronan
RT receptor homologues.";
RL Biochem. J. 362:155-164(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1666-2559.
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12473645; DOI=10.1074/jbc.m210211200;
RA Tamura Y., Adachi H., Osuga J., Ohashi K., Yahagi N., Sekiya M.,
RA Okazaki H., Tomita S., Iizuka Y., Shimano H., Nagai R., Kimura S.,
RA Tsujimoto M., Ishibashi S.;
RT "FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end
RT products.";
RL J. Biol. Chem. 278:12613-12617(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=14598175; DOI=10.1007/s00418-003-0585-5;
RA Falkowski M., Schledzewski K., Hansen B., Goerdt S.;
RT "Expression of stabilin-2, a novel fasciclin-like hyaluronan receptor
RT protein, in murine sinusoidal endothelia, avascular tissues, and at
RT solid/liquid interfaces.";
RL Histochem. Cell Biol. 120:361-369(2003).
RN [5]
RP FUNCTION, INTERACTION WITH CLATHRIN AND AP2, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH GULP1.
RX PubMed=18230608; DOI=10.1074/jbc.m709105200;
RA Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S.;
RT "Requirement of adaptor protein GULP during stabilin-2-mediated cell corpse
RT engulfment.";
RL J. Biol. Chem. 283:10593-10600(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 short form
CC also functions as an endocytosis receptor for heparin internalization
CC as well as HA and CS. {ECO:0000269|PubMed:15572036,
CC ECO:0000269|PubMed:18230608}.
CC -!- SUBUNIT: Interacts with heparin, alpha-M/beta-2 integrin (ITGAM and
CC ITGB2), and thymosin beta 4 (TMSB4X) (By similarity). Interacts with
CC GULP1. Associates with clathrin and adapter protein AP-2; in liver
CC sinusoidal endothelial cells (LSECs). {ECO:0000250,
CC ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:18230608}.
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: Expressed in endothelial sinuses of liver, lymph
CC nodes, bone marrow, spleen and in specialised structures of eye, heart,
CC brain and kidney. Expression is detected in corneal and lens
CC epithelium, in mesenchymal cells of the heart valves, in the ependymal
CC cells lining the ventricles in the brain, and in the prismatic
CC epithelial cells covering the renal papillae.
CC {ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:14598175}.
CC -!- DOMAIN: Recognizes phosphatidyl serine via its epidermal growth factor-
CC like domains.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Proteolytically processed to yield a smaller protein.
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DR EMBL; AF364951; AAL91684.2; -; mRNA.
DR EMBL; AK034522; BAC28741.1; -; mRNA.
DR CCDS; CCDS36021.1; -.
DR RefSeq; NP_619614.1; NM_138673.2.
DR AlphaFoldDB; Q8R4U0; -.
DR SMR; Q8R4U0; -.
DR BioGRID; 228666; 2.
DR STRING; 10090.ENSMUSP00000048309; -.
DR GlyGen; Q8R4U0; 29 sites.
DR iPTMnet; Q8R4U0; -.
DR PhosphoSitePlus; Q8R4U0; -.
DR SwissPalm; Q8R4U0; -.
DR CPTAC; non-CPTAC-3499; -.
DR jPOST; Q8R4U0; -.
DR MaxQB; Q8R4U0; -.
DR PaxDb; Q8R4U0; -.
DR PRIDE; Q8R4U0; -.
DR ProteomicsDB; 257446; -.
DR Antibodypedia; 18052; 152 antibodies from 22 providers.
DR DNASU; 192188; -.
DR Ensembl; ENSMUST00000035288; ENSMUSP00000048309; ENSMUSG00000035459.
DR GeneID; 192188; -.
DR KEGG; mmu:192188; -.
DR UCSC; uc007gqo.1; mouse.
DR CTD; 55576; -.
DR MGI; MGI:2178743; Stab2.
DR VEuPathDB; HostDB:ENSMUSG00000035459; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000156566; -.
DR HOGENOM; CLU_001035_0_0_1; -.
DR InParanoid; Q8R4U0; -.
DR OMA; ENISNPM; -.
DR OrthoDB; 6428at2759; -.
DR PhylomeDB; Q8R4U0; -.
DR TreeFam; TF331489; -.
DR Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-MMU-3000497; Scavenging by Class H Receptors.
DR BioGRID-ORCS; 192188; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Stab2; mouse.
DR PRO; PR:Q8R4U0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R4U0; protein.
DR Bgee; ENSMUSG00000035459; Expressed in mesenteric lymph node and 103 other tissues.
DR ExpressionAtlas; Q8R4U0; baseline and differential.
DR Genevisible; Q8R4U0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0038024; F:cargo receptor activity; IMP:MGI.
DR GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0030214; P:hyaluronan catabolic process; IMP:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.30.180.10; -; 7.
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; IPR002049; LE_dom.
DR InterPro; IPR000538; Link_dom.
DR Pfam; PF12947; EGF_3; 8.
DR Pfam; PF02469; Fasciclin; 6.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 21.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00180; EGF_Lam; 5.
DR SMART; SM00554; FAS1; 7.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF82153; SSF82153; 7.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 16.
DR PROSITE; PS50026; EGF_3; 21.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50213; FAS1; 7.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Disulfide bond; EGF-like domain; Endocytosis;
KW Glycoprotein; Hyaluronic acid; Laminin EGF-like domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..2559
FT /note="Stabilin-2"
FT /id="PRO_0000007714"
FT CHAIN 1136..2551
FT /note="Short form stabilin-2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007715"
FT TOPO_DOM 29..2464
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2465..2485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2486..2559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 116..156
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 164..201
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 203..244
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 245..284
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 330..370
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 379..512
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 522..659
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 743..783
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 833..873
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 874..917
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 918..960
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 961..1002
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1002..1135
FT /note="FAS1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 1145..1273
FT /note="FAS1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 1350..1415
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 1439..1477
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1478..1519
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1520..1561
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1562..1603
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1603..1731
FT /note="FAS1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 1747..1888
FT /note="FAS1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 1965..2030
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 2055..2089
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2090..2130
FT /note="EGF-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2131..2173
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2206..2298
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 2318..2452
FT /note="FAS1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 2510..2520
FT /note="Interaction with TMSB4X"
FT /evidence="ECO:0000250"
FT REGION 2514..2559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2515..2529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2001
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2072
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..134
FT /evidence="ECO:0000250"
FT DISULFID 128..144
FT /evidence="ECO:0000250"
FT DISULFID 146..155
FT /evidence="ECO:0000250"
FT DISULFID 168..179
FT /evidence="ECO:0000250"
FT DISULFID 172..189
FT /evidence="ECO:0000250"
FT DISULFID 191..200
FT /evidence="ECO:0000250"
FT DISULFID 207..218
FT /evidence="ECO:0000250"
FT DISULFID 212..230
FT /evidence="ECO:0000250"
FT DISULFID 232..243
FT /evidence="ECO:0000250"
FT DISULFID 249..260
FT /evidence="ECO:0000250"
FT DISULFID 254..270
FT /evidence="ECO:0000250"
FT DISULFID 272..283
FT /evidence="ECO:0000250"
FT DISULFID 334..346
FT /evidence="ECO:0000250"
FT DISULFID 340..356
FT /evidence="ECO:0000250"
FT DISULFID 358..369
FT /evidence="ECO:0000250"
FT DISULFID 747..761
FT /evidence="ECO:0000250"
FT DISULFID 755..771
FT /evidence="ECO:0000250"
FT DISULFID 773..782
FT /evidence="ECO:0000250"
FT DISULFID 837..850
FT /evidence="ECO:0000250"
FT DISULFID 844..859
FT /evidence="ECO:0000250"
FT DISULFID 861..872
FT /evidence="ECO:0000250"
FT DISULFID 878..893
FT /evidence="ECO:0000250"
FT DISULFID 887..903
FT /evidence="ECO:0000250"
FT DISULFID 905..916
FT /evidence="ECO:0000250"
FT DISULFID 922..936
FT /evidence="ECO:0000250"
FT DISULFID 930..946
FT /evidence="ECO:0000250"
FT DISULFID 948..959
FT /evidence="ECO:0000250"
FT DISULFID 965..978
FT /evidence="ECO:0000250"
FT DISULFID 972..988
FT /evidence="ECO:0000250"
FT DISULFID 990..1001
FT /evidence="ECO:0000250"
FT DISULFID 1355..1369
FT /evidence="ECO:0000250"
FT DISULFID 1363..1379
FT /evidence="ECO:0000250"
FT DISULFID 1381..1390
FT /evidence="ECO:0000250"
FT DISULFID 1402..1413
FT /evidence="ECO:0000250"
FT DISULFID 1406..1423
FT /evidence="ECO:0000250"
FT DISULFID 1425..1434
FT /evidence="ECO:0000250"
FT DISULFID 1443..1453
FT /evidence="ECO:0000250"
FT DISULFID 1447..1463
FT /evidence="ECO:0000250"
FT DISULFID 1465..1476
FT /evidence="ECO:0000250"
FT DISULFID 1482..1495
FT /evidence="ECO:0000250"
FT DISULFID 1489..1505
FT /evidence="ECO:0000250"
FT DISULFID 1507..1518
FT /evidence="ECO:0000250"
FT DISULFID 1524..1537
FT /evidence="ECO:0000250"
FT DISULFID 1531..1547
FT /evidence="ECO:0000250"
FT DISULFID 1549..1560
FT /evidence="ECO:0000250"
FT DISULFID 1566..1579
FT /evidence="ECO:0000250"
FT DISULFID 1573..1589
FT /evidence="ECO:0000250"
FT DISULFID 1591..1602
FT /evidence="ECO:0000250"
FT DISULFID 1970..1984
FT /evidence="ECO:0000250"
FT DISULFID 1978..1994
FT /evidence="ECO:0000250"
FT DISULFID 1996..2005
FT /evidence="ECO:0000250"
FT DISULFID 2017..2028
FT /evidence="ECO:0000250"
FT DISULFID 2022..2038
FT /evidence="ECO:0000250"
FT DISULFID 2040..2049
FT /evidence="ECO:0000250"
FT DISULFID 2059..2069
FT /evidence="ECO:0000250"
FT DISULFID 2063..2075
FT /evidence="ECO:0000250"
FT DISULFID 2077..2088
FT /evidence="ECO:0000250"
FT DISULFID 2094..2107
FT /evidence="ECO:0000250"
FT DISULFID 2101..2116
FT /evidence="ECO:0000250"
FT DISULFID 2118..2129
FT /evidence="ECO:0000250"
FT DISULFID 2135..2149
FT /evidence="ECO:0000250"
FT DISULFID 2143..2159
FT /evidence="ECO:0000250"
FT DISULFID 2161..2172
FT /evidence="ECO:0000250"
FT DISULFID 2228..2296
FT /evidence="ECO:0000250"
FT DISULFID 2252..2273
FT /evidence="ECO:0000250"
FT CONFLICT 1666
FT /note="L -> G (in Ref. 2; BAC28741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2559 AA; 277532 MW; 1C9855AD61EFF015 CRC64;
MARSKLLLGK LLPLILIFLG LLVQNACSPT EAPELTKRCD KKSTLTIKTE CQSCSVNIAV
KCPDGYIKIT NGTVGVRDCR YSLKIQSYVL DIPGCRHICR KDYLQPQCCP GHWGPDCMEC
PGGARAPCGG RGVCDEGMEG TGSCSCRAGF RGTACENCAA EDVFGPNCSA VCSCVHGVCN
SGISGDGTCE CLSAYRGPRC DKPIPECAAL LCPENSRCSP SSKDETKLQC KCLPSYKGDG
QTCKPINPCL KNVCHPHASC SYLGPNRHSC VCQKGYQGDG QVCLPVDPCQ TSYGNCPTKS
TVCRYDGPGQ SHCECKEHYR NFVPGVGCSM TDICESKNPC HKNANCSTVS PGQTQCTCQK
GYVGDGLNCY GNIMQRLREL NTEPRGMWQG QLTSFISILD RTYAWPLSNL GPFTVLLPSD
KGLKGVDVKE LLMDKEAARY FVKLHIIAGQ MSTEQMYNLD TFYTLTGKSG EIINKDKDNQ
LKLKLYGSKI VQIIQGNIVA SNGLVHILDR AMDKIEPTLE SNPQQTIMTM LQPRYGKFRS
LLEKTNVGQA LEKGGIDEPY TIFVPSNEAL SNMTAGVLDY LLSPEGSRKL LELVRYHIVA
FTQLEVATLV STLHIRSMAN QIITFNISSK GQILANNVAV DETEVAAKNG RIYTLTGVLI
PPSILPILPH RCNETKREMK LGTCVRCFMK NWSKCPTNSE PTAIFTNKCF YGSRAWNLKI
GCARYCDVTV EIPRCCKGFF GPDCNPCPGG FMNPCSGNGQ CIDGLGGNGT CICEDGFQGS
RCQFCSKPNR YGPQCNRTCQ CVHGICDNRL DSDGSCLPGT CREGTAGRFC DKQTSACGPY
MQFCHIHATC EYSNETASCV CNDGYEGDGT LCSKKDPCLG STSRGGCSPN AECIQASTGT
YSCVCQRGWT GNGRDCVEIN SCLLPSSGGC HDNATCLYVG PGQNECECKK GFRGNGIDCE
PIISCLEQIE KCHPLATCQY TLSGVWSCVC QEGYEGNGVL CYGNVLMELS FLSEAAVFYQ
WINNASLQSM LSATSNLTVL VPSLQAIKDM DQNEKSFWLS RNNIPALIKY HTLLGTYRVA
DLQTLPSSHM LATSLQGSFL RLDKADGNIT IEGASFVDGD NAATNGVVHI INKVLIPQRG
LTGSLPSLLT RLEQMPDYSI FRGYIIHYNL ASAIEAADAY TVFVPNNEAI ESYIREKKAT
SLKEDILQYH VVLGEKLLRN DLHNGMHRET MLGFSYLLAF FLHNDQLYVN EAPINYTNVA
TDKGVIHGLE KVLEIKKNRC DNNDTIIVRG KCGKCSQQTL CPLETKPLSE TRKCIYSVYF
MGKRSIFIGC QLQCVRTIIT SACCAGFFGP QCQACPGKGQ NVCSGNGFCL DGVNGTGTCE
CEQGFNGTAC ETCTEGKYGI HCDQACSCVH GRCNQGPSGD GSCDCDVGWR GVKCDSEITT
DNCNGTCHTS ANCLLDPDGK ASCKCAAGFQ GNGTVCTAIN ACEISNGGCS AKADCKRTIP
GSRVCVCKAG YTGDGIVCLE INPCLENHGG CDRHAECTQT GPNQAVCNCL PKYTGDGKVC
TLINVCLTNN GGCSPFAFCN HTEQDQRTCT CKPDYTGDGI VCRGSIHSEL PKNPSTSQYF
FQLQEHAVQE LAGPGPFTVF VPSSDSFNSE SKLKVWDKQG LMSQILRYHV VACQQLLLEN
LKVITSATTL QGEPISISVS QDTVLINKKA KVLSSDIIST NGVIHVIDTL LSPQNLLITP
KGASGRVLLN LTTVAANHGY TKFSKLIQDS GLLKVITDPM HTPVTLFWPT DKALQALPQE
QQDFLFNEDN KDKLKAYLKF HVIRDTMALA SDLPRSASWK TLQGSELSVR CGTGSDVGEL
FLNGQMCRII QRRLLFDGGV AYGIDCLLMD PTEGGRCDTF TTFNIPGECG SCFSTPRCPL
QSKPKGVRKK CIYNPLPFRR DVEGCQNLCT LVVHVPRCCS GYFMPDCQAC PGGPDTPCNN
RGMCYDQYKP TGQCQCHTGF NGTACELCLP GRFGPDCQPC GCSEHGQCDE GITGSGQCLC
EAGWTGRFCD APTVVIPVCI PACSMHATCM ENNTCVCNLN YEGDGITCTV VDFCKQNNGG
CAKVAKCSQK GTQVSCSCQK GYKGDGHSCT EIDPCANGVN GGCHEHATCR MTGPGKQKCE
CKSHYVGDGR DCEPEQLPLD RCLQDNGQCH PDANCVDLHF QDTTVGVFHL RSPLGQYKLT
FDKAKEACAK EAASIATYNQ LSYAQKAKYH LCSAGWLESG RVAYPTIYAS KKCANIVGIV
DYGTRTNKSE MWDVFCYRMK DVNCTCKAGY VGDGFSCNGN LLQVLMSFPS LTNFLTEVLV
FSRSSAQGRA FLKHLTDLSI SGTLFVPQNS GLPKNKSLSG RDIEHHLTNV NVSFYDDLVN
GTVLKTRLGS QLLITSSQDQ LHQEARFVDG RAILQWDIIA SNGVLHIISE PLKAPPTAAT
AAHSGLGTGI FCAVVLVTGA IALAAYSYFR LNQRTTGFRR FESEDDIDAL AFGKQQPESI
TNPLYETSTP AAPEPSCDPF TDSGERELEN SDPLGALRS
