HMCN2_MOUSE
ID HMCN2_MOUSE Reviewed; 5100 AA.
AC A2AJ76; Q8BNH3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Hemicentin-2;
DE Flags: Precursor;
GN Name=Hmcn2;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17015624; DOI=10.1369/jhc.6a6975.2006;
RA Xu X., Dong C., Vogel B.E.;
RT "Hemicentins assemble on diverse epithelia in the mouse.";
RL J. Histochem. Cytochem. 55:119-126(2007).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=21215633; DOI=10.1016/j.cub.2010.12.006;
RA Xu X., Vogel B.E.;
RT "A secreted protein promotes cleavage furrow maturation during
RT cytokinesis.";
RL Curr. Biol. 21:114-119(2011).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-909; ARG-914 AND ARG-915, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=32035013; DOI=10.1002/dvdy.159;
RA Lin M.H., Pope B.D. III, Sasaki T., Keeley D.P., Sherwood D.R., Miner J.H.;
RT "Mammalian hemicentin 1 is assembled into tracks in the extracellular
RT matrix of multiple tissues.";
RL Dev. Dyn. 249:775-788(2020).
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=34504132; DOI=10.1038/s41598-021-96824-4;
RA Welcker D., Stein C., Feitosa N.M., Armistead J., Zhang J.L., Luetke S.,
RA Kleinridders A., Bruening J.C., Eming S.A., Sengle G., Niehoff A.,
RA Bloch W., Hammerschmidt M.;
RT "Hemicentin-1 is an essential extracellular matrix component of the dermal-
RT epidermal and myotendinous junctions.";
RL Sci. Rep. 11:17926-17926(2021).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:17015624}. Cleavage furrow
CC {ECO:0000269|PubMed:21215633}. Note=The antibody used in
CC PubMed:17015624 and PubMed:21215633 to determine subcellular location
CC does not distinguish between HMCN1 and HMCN2.
CC {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:21215633}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AJ76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AJ76-2; Sequence=VSP_039372;
CC -!- TISSUE SPECIFICITY: In neonatal skin, localized in the pericellular
CC space of basal epidermal keratinocytes (at protein level)
CC (PubMed:34504132). In adult skin, restricted to basal keratinocytes of
CC hair follicles and the interfollicular epidermis (PubMed:34504132).
CC Absent from the myotendinous junction but present in skeletal muscle
CC (at protein level) (PubMed:34504132). Expressed in the pericellular
CC extracellular matrix of epithelial cells in a number of tissues
CC including embryonic trophectoderm and adult skin and tongue
CC (PubMed:17015624). Also present in the extracellular matrix of some,
CC but not all, blood vessels (PubMed:17015624). Expressed primarily in
CC epithelial cells in the embryonic epidermis, lung, intestine, skeletal
CC hindlimb muscle, tongue and the muscular layers of the esophagus
CC (PubMed:34504132). {ECO:0000269|PubMed:17015624,
CC ECO:0000269|PubMed:34504132}.
CC -!- INDUCTION: Following wounding, up-regulated in the basal keratinocytes
CC within the epidermal tongues of closing wounds.
CC {ECO:0000269|PubMed:34504132}.
CC -!- PTM: Reported to be phosphorylated; however as this position is
CC extracellular, the in vivo relevance is unsure.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable and fertile with no gross
CC phenotypes (PubMed:32035013). Double knockout of Hmcn1 and Hmcn2
CC results in no overt phenotypes with mice being viable and fertile
CC (PubMed:32035013). {ECO:0000269|PubMed:32035013}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38997.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK083701; BAC38997.1; ALT_FRAME; mRNA.
DR EMBL; AL732564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 10090.ENSMUSP00000109160; -.
DR GlyGen; A2AJ76; 40 sites.
DR iPTMnet; A2AJ76; -.
DR PhosphoSitePlus; A2AJ76; -.
DR MaxQB; A2AJ76; -.
DR PaxDb; A2AJ76; -.
DR PeptideAtlas; A2AJ76; -.
DR PRIDE; A2AJ76; -.
DR ProteomicsDB; 273183; -. [A2AJ76-1]
DR ProteomicsDB; 273184; -. [A2AJ76-2]
DR Antibodypedia; 65468; 13 antibodies from 6 providers.
DR Ensembl; ENSMUST00000113532; ENSMUSP00000109160; ENSMUSG00000055632. [A2AJ76-1]
DR UCSC; uc008jds.3; mouse. [A2AJ76-2]
DR MGI; MGI:2677838; Hmcn2.
DR VEuPathDB; HostDB:ENSMUSG00000055632; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000162328; -.
DR HOGENOM; CLU_000087_0_0_1; -.
DR InParanoid; A2AJ76; -.
DR OMA; QLHWRRE; -.
DR PhylomeDB; A2AJ76; -.
DR ChiTaRS; Hmcn2; mouse.
DR PRO; PR:A2AJ76; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AJ76; protein.
DR Bgee; ENSMUSG00000055632; Expressed in esophagus and 51 other tissues.
DR ExpressionAtlas; A2AJ76; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR Gene3D; 2.40.155.10; -; 1.
DR Gene3D; 2.60.40.10; -; 43.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR006605; G2_nidogen/fibulin_G2F.
DR InterPro; IPR009017; GFP.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR032984; Hemicentin-2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23278:SF29; PTHR23278:SF29; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 4.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF07679; I-set; 32.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00409; IG; 43.
DR SMART; SM00408; IGc2; 43.
DR SMART; SM00406; IGv; 12.
DR SUPFAM; SSF48726; SSF48726; 42.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF54511; SSF54511; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 5.
DR PROSITE; PS50835; IG_LIKE; 43.
DR PROSITE; PS50993; NIDOGEN_G2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Immunoglobulin domain; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Sensory transduction;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..5100
FT /note="Hemicentin-2"
FT /id="PRO_0000395109"
FT DOMAIN 37..211
FT /note="VWFA"
FT DOMAIN 426..515
FT /note="Ig-like C2-type 1"
FT DOMAIN 517..601
FT /note="Ig-like C2-type 2"
FT DOMAIN 609..692
FT /note="Ig-like C2-type 3"
FT DOMAIN 699..782
FT /note="Ig-like C2-type 4"
FT DOMAIN 787..877
FT /note="Ig-like C2-type 5"
FT DOMAIN 882..968
FT /note="Ig-like C2-type 6"
FT DOMAIN 973..1058
FT /note="Ig-like C2-type 7"
FT DOMAIN 1063..1156
FT /note="Ig-like C2-type 8"
FT DOMAIN 1161..1239
FT /note="Ig-like C2-type 9"
FT DOMAIN 1246..1335
FT /note="Ig-like C2-type 10"
FT DOMAIN 1340..1437
FT /note="Ig-like C2-type 11"
FT DOMAIN 1442..1531
FT /note="Ig-like C2-type 12"
FT DOMAIN 1536..1624
FT /note="Ig-like C2-type 13"
FT DOMAIN 1629..1717
FT /note="Ig-like C2-type 14"
FT DOMAIN 1722..1810
FT /note="Ig-like C2-type 15"
FT DOMAIN 1825..1913
FT /note="Ig-like C2-type 16"
FT DOMAIN 1920..2008
FT /note="Ig-like C2-type 17"
FT DOMAIN 2011..2100
FT /note="Ig-like C2-type 18"
FT DOMAIN 2105..2189
FT /note="Ig-like C2-type 19"
FT DOMAIN 2196..2285
FT /note="Ig-like C2-type 20"
FT DOMAIN 2290..2379
FT /note="Ig-like C2-type 21"
FT DOMAIN 2384..2473
FT /note="Ig-like C2-type 22"
FT DOMAIN 2478..2566
FT /note="Ig-like C2-type 23"
FT DOMAIN 2571..2662
FT /note="Ig-like C2-type 24"
FT DOMAIN 2667..2758
FT /note="Ig-like C2-type 25"
FT DOMAIN 2781..2871
FT /note="Ig-like C2-type 26"
FT DOMAIN 2875..2964
FT /note="Ig-like C2-type 27"
FT DOMAIN 2971..3058
FT /note="Ig-like C2-type 28"
FT DOMAIN 3063..3153
FT /note="Ig-like C2-type 29"
FT DOMAIN 3157..3245
FT /note="Ig-like C2-type 30"
FT DOMAIN 3250..3340
FT /note="Ig-like C2-type 31"
FT DOMAIN 3345..3432
FT /note="Ig-like C2-type 32"
FT DOMAIN 3438..3523
FT /note="Ig-like C2-type 33"
FT DOMAIN 3528..3609
FT /note="Ig-like C2-type 34"
FT DOMAIN 3614..3702
FT /note="Ig-like C2-type 35"
FT DOMAIN 3707..3793
FT /note="Ig-like C2-type 36"
FT DOMAIN 3798..3886
FT /note="Ig-like C2-type 37"
FT DOMAIN 3891..3977
FT /note="Ig-like C2-type 38"
FT DOMAIN 3982..4067
FT /note="Ig-like C2-type 39"
FT DOMAIN 4071..4158
FT /note="Ig-like C2-type 40"
FT DOMAIN 4163..4244
FT /note="Ig-like C2-type 41"
FT DOMAIN 4252..4336
FT /note="Ig-like C2-type 42"
FT DOMAIN 4343..4428
FT /note="Ig-like C2-type 43"
FT DOMAIN 4432..4654
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT DOMAIN 4668..4708
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4709..4753
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4754..4789
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4797..4837
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4904..4943
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1265..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 909
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 914
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 915
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
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 1068
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2034
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5035
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 449..497
FT /evidence="ECO:0000250"
FT DISULFID 539..588
FT /evidence="ECO:0000250"
FT DISULFID 630..678
FT /evidence="ECO:0000250"
FT DISULFID 720..766
FT /evidence="ECO:0000250"
FT DISULFID 808..859
FT /evidence="ECO:0000250"
FT DISULFID 903..952
FT /evidence="ECO:0000250"
FT DISULFID 994..1042
FT /evidence="ECO:0000250"
FT DISULFID 1091..1140
FT /evidence="ECO:0000250"
FT DISULFID 1182..1225
FT /evidence="ECO:0000250"
FT DISULFID 1269..1319
FT /evidence="ECO:0000250"
FT DISULFID 1363..1421
FT /evidence="ECO:0000250"
FT DISULFID 1465..1515
FT /evidence="ECO:0000250"
FT DISULFID 1559..1608
FT /evidence="ECO:0000250"
FT DISULFID 1653..1701
FT /evidence="ECO:0000250"
FT DISULFID 1745..1794
FT /evidence="ECO:0000250"
FT DISULFID 1846..1899
FT /evidence="ECO:0000250"
FT DISULFID 1941..1990
FT /evidence="ECO:0000250"
FT DISULFID 2033..2084
FT /evidence="ECO:0000250"
FT DISULFID 2126..2175
FT /evidence="ECO:0000250"
FT DISULFID 2218..2269
FT /evidence="ECO:0000250"
FT DISULFID 2314..2363
FT /evidence="ECO:0000250"
FT DISULFID 2408..2457
FT /evidence="ECO:0000250"
FT DISULFID 2501..2550
FT /evidence="ECO:0000250"
FT DISULFID 2597..2646
FT /evidence="ECO:0000250"
FT DISULFID 2695..2744
FT /evidence="ECO:0000250"
FT DISULFID 2806..2855
FT /evidence="ECO:0000250"
FT DISULFID 2901..2950
FT /evidence="ECO:0000250"
FT DISULFID 2993..3042
FT /evidence="ECO:0000250"
FT DISULFID 3088..3137
FT /evidence="ECO:0000250"
FT DISULFID 3180..3229
FT /evidence="ECO:0000250"
FT DISULFID 3273..3324
FT /evidence="ECO:0000250"
FT DISULFID 3369..3418
FT /evidence="ECO:0000250"
FT DISULFID 3462..3507
FT /evidence="ECO:0000250"
FT DISULFID 3551..3593
FT /evidence="ECO:0000250"
FT DISULFID 3637..3686
FT /evidence="ECO:0000250"
FT DISULFID 3728..3777
FT /evidence="ECO:0000250"
FT DISULFID 3819..3870
FT /evidence="ECO:0000250"
FT DISULFID 3912..3961
FT /evidence="ECO:0000250"
FT DISULFID 4003..4051
FT /evidence="ECO:0000250"
FT DISULFID 4093..4142
FT /evidence="ECO:0000250"
FT DISULFID 4184..4231
FT /evidence="ECO:0000250"
FT DISULFID 4274..4322
FT /evidence="ECO:0000250"
FT DISULFID 4364..4412
FT /evidence="ECO:0000250"
FT DISULFID 4672..4683
FT /evidence="ECO:0000250"
FT DISULFID 4679..4692
FT /evidence="ECO:0000250"
FT DISULFID 4694..4707
FT /evidence="ECO:0000250"
FT DISULFID 4713..4726
FT /evidence="ECO:0000250"
FT DISULFID 4720..4735
FT /evidence="ECO:0000250"
FT DISULFID 4739..4752
FT /evidence="ECO:0000250"
FT DISULFID 4758..4771
FT /evidence="ECO:0000250"
FT DISULFID 4765..4780
FT /evidence="ECO:0000250"
FT DISULFID 4801..4812
FT /evidence="ECO:0000250"
FT DISULFID 4808..4821
FT /evidence="ECO:0000250"
FT DISULFID 4823..4836
FT /evidence="ECO:0000250"
FT DISULFID 4908..4918
FT /evidence="ECO:0000250"
FT DISULFID 4914..4927
FT /evidence="ECO:0000250"
FT DISULFID 4929..4942
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..4439
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039372"
FT CONFLICT 5026
FT /note="A -> V (in Ref. 1; BAC38997)"
FT /evidence="ECO:0000305"
FT CONFLICT 5068
FT /note="L -> V (in Ref. 1; BAC38997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5100 AA; 547198 MW; 74EAFA906677B3DF CRC64;
MTPGAQLLPL LVAISTAVAA VVTSDAPTKT LSPATGDATL AFVFDVTGSM WDDLMQVIDG
ASRILERSLS SRSRVIANYA LVPFHDPDIG PVTLTADPVV FQRELRELYV QGGGDCPEMS
VGAIKAAVEV ANPGSFIYVF SDARAKDYHK KKELLQLLQL KQSQVVFVLT GDCGDRTHPG
YLVFEEIAST SSGQVFQLDK QQVSEVLKWV ESAIQASKVH LLSADHEEEG EHTWRIPFDP
SLKEVTIALS GPGPEIEVRD PLGRVLQTDE GLNVLLNIPD SAKVVAFKPE HPGLWAIKVY
SSGRHSVRIS GISNINFRAG FSMQPSLDLN HTIEWPLQGV PISLVINSTG LQAPGHLESV
ELSHSSGRSL LTLPTQLLSN GSTHQLWAGP PFHVPKERFY LKVKGKDHEG NPLLRVSGVS
YSAVAPGVPL VSMAPKIHGY LQQPLLVSCS VYSTLPFQLQ LQRDGERLGE ERYFQESGNS
SWEIPRASKA EEGTYQCIAV SRAGSGRASA QIVITDPPPQ LVPGPNVTVS PGETAILSCQ
VLGETPYNLT WVRDWRALPA TTGRISQLSD LSLEVRSIIP TDGGQYQCVA SNPNGVTRAT
TWLLVREAPQ VSINARSQRF SQGVEVRVSC SASGYPTPHI SWSREGLALP EDSRIHVDAQ
GTLIIQGLAP EDAGNYSCQA TNEVGTDEET VTLYYTDPPS VSAVNAVVLT AVGEEAVLLC
AASGVPPPRV IWYRGGLEVI LAPGDSRSGT LRIPEAQERD AGLYTCKAVN ELGDASAEIQ
LVVGNAPRLT DPPQDVTVEL GKSVFLTCRA TGRPPPIVTW RRGDGQALEP GRGSRTGQRD
SGVLVFERVS LEDQAPYVCE ARNVFGKAQA EARLVVTGHA PPQIANSASV VRVLEGQPVS
LTCVILAGRP LPERRWLKAG SPLPPGNRHA VRADGSLHLD RALQEDAGRY SCVATNVAGS
QHRDVELVVQ VPPRIHPTST HHVTNEGVPA SLPCIASGVP TPKITWTKET NALTTSGHYS
VSRNGTLVIV QPSPQDAGAY VCTATNSVGF SSQEMWLSVN TKPMIKMNGS QAVDVPLRVT
VKAGEEVTLD CEAQGSPTPL LTWTKDANPL LPVTNRYELL PSGSLRLAQA QVGDNGLYGC
TASNPAGATS RRYVLRVQVP PQVQPGPRVL KVLAGEALDL NCVAEGNPQP QLNWFKDGMA
LMGEGAQGSV HFAAVKTSDA GLYRCEASNS AGTDTWKLEL LVLEPPHWGT DETKSLLERV
AGENASLPCP AQGTPKPRIT WRRGPSSEPL NGRPDVAVLD EGSLFLSSVS LADSGEYECQ
ATNEVGSASR RAKLVVYVPP SIREEGHITN VSGLAGQPLT LECDINGFPA PEVAWLKDGQ
LVGDSGGGWD GEEASGHRLL DGSRSLHFPR IQESHSGLYS CQAENQAGSA QRDFNLAVFI
PPSLLGAGAA QEVLGLAGAD VTLECQTSGV PTPQVEWTKD GQPILPGDPH ILLQEDGQVL
RIISSHLGDE GQYQCVAFSP AGQQAKDFQL SIHSPPTIWG SNETGEVTVL EGHTAQLLCE
ARGMPSPAIT WYKDGTLLAP SSEVVYSKGG RQLQLVKAQP SDAGLYTCQA SNPAGITKKS
TSLEVYVPPT IEGADGGPYL VQAVAGRPVA LECVARGHPP PTISWQHEGL PVVDSNGTWL
EAGGALQLEN PGEASGGLYS CVASSPAGEA VLQYSVEMQV PPQLLVAEGM GQVTATVGQS
LDLPCQASGS PVPTIQWLQN GRPAEELAGV QLASQGTILH ISHVELNHSG LFACQATNEA
GTAGAEVEVS VHGKQVSVNL GASFSAHHWW GEPHSPFPAT CNPPVCRHWS AYPKPSLVER
WRGRGNLRGQ PSGTVREPGL TLLSQIEKAD LRDEGVYTCS ATNLAGESKK DVTLKVLVPP
NIEPGPVNKV VLENASVTLE CLASGVPPPD VSWFKGRQPI STQRRVIVSA DGRVLHIERV
QLSDAGSYRC VATNVAGSAG LKYGLRVNVP PRITLPPNLP GPVLLGTPFR LTCNATGTPR
PTLIWLKDGN PVSPEGIPGL KVFPGGQVLT VASARASDSG SYSCVAVSAV GEDRRDVILQ
VHMPPSILGE ELNMSVVVNE SVTLECQSHA VPPPVLRWQK DGRPLEPHPG IRLSADKALL
EVDRAAVWDA GHYTCEAINQ AGRSEKHFNL HVWVPPAFPS KEPYTLTVTE GQTARLSCDC
QGIPFPKISW RKDGQPLPGE GDSLEQVLAV GRLLYLGQAQ SAQEGTYTCE CSNAAGTSSQ
EQSLEVLVPP QVTGLWEPLT TVSVIQDGNT TLACNATGKP LPVVTWQRDG QPVSVEPGLR
LQNQNHSLHV ERAQASHAGG YSCVAENTAG RAERRFALSV LAPPHLTGDS DSLTNVTATL
HGSFTLLCEA AGVPAPTVQW FQEGQPISPR EGTYLLAGGW MLKMTQAQEQ DRGLYSCLAS
NEAGEARRNF SVEVLVPPSI ENEDLEEVIK VPEGQTAQLE CNATGHPPPK VTWFKDGQSL
TVEDPYEMSP DGAFLWIPQA NLSNAGHYSC IASNAVGEKT KHTQLSVLVV PTILGVPEKN
ANEEVTVTIN NPISLICEAL AFPSPNITWM KDGSPFEASK NIQLLPGTHG LQILNAQKED
AGQYTCVVTN ELGEATKNYH VEVLIPPSIS KDDPLGEVSV KEVKTKVNSS LTLECECWAT
PPPSISWYKD GRPVTPSHRL SVLGEGRLLQ IQPTQVSDSG RYLCVATNVA GEDDQDFNVL
IQVPPMFQKM GDVDAGFEPL PHEEEAQGRV TEYREIVENN PAYLYCDTNA IPPPELTWYR
EGQPLSAADG VSVLQGGRIL QLPLVQAEDA GRYSCKAANE VGEDWLHYEL LVLTPPVIPG
DTQELVEEVT VNASSAVSLE CPALGNPAPA VSWFQNGLPV SPSPRLQVLE EGQVLKVATA
EVADAASYMC VAENQAGSAE KLFTLKVQVP PQISDWTTSQ LTATLNSSVS LPCEVYAHPN
PEVTWYKDGQ PLSLGQEAFL LPGTHTLRLA RAQPADSGTY LCEALNAAGR DQKMVQLNVL
VPPSFKQAPG GPQEAIQVRA GDKAILSCET DSLPEPAVTW FKDQQPLALG QRIQGLQGGQ
TLEILDSQAS DKGVYSCKVS NTAGEAIRTF VLAIQVPPTF EKPERETVNQ VAGRTLVLAC
DVSGIPAPTV TWLKDRLPVE SSVVHGVVSR GGRLQLSHLQ PAQAGTYTCV AENAQAEARK
DFVVSVLVPP QIQDSGMAQE HNVLEKQEIR LHCEAEGQPP PDITWLKDGG LLDQHVGPHL
RFYLDGSTLV LKGLRTADSG AYTCVAHNPA GEDARLHTVN VLVPPTIKQQ AGDTGTLVSR
TGELVTMVCP VQGSPPIHVS WLKDGLPLPL SQRTLLHSSG RTLRISQVQL ADSGVFTCVA
ASPAGVADRN FTLLVLVPPI LEPVEFQNNV MAAQGSEVVL PCEARGSPLP LVSWMKDGEP
LLPQSLEQGP GLKLESVSVG DAGTYSCTAA SEAGEARRHF QLTVMDPPHI EESGETSELS
LTPGAHLELL CEARGIPPPN ITWHKDGQAL RRTENDSQAG RVLRVDNAGL YTCLAESPAG
EVEKSFRVRV QAPPNVVGPR GPRSVVGLAP GQLILECSVE AEPAPEIEWH RGGVLLQADA
HTHFPEQGRF LKLQALSTAD GGDYSCTARN RAGSTSVAFR VEIHTAPTIQ SGPNTVNVSV
NRTTLLPCQT HGVPTPLVSW RKDGIPLHPG SPRLEFLPEG SLRIHPVLAQ DAGHYLCLAS
NSAGSDRKGL DLRVFEPPAI APGPSNLTLT AYSPASLPCE ARGSPKPLVT WWKDGQKLDL
RLQQGAYRLL PSNALFLTAP SPQDSAQFEC VVSNEVGESR RRYQVTVHVP PTIADDQTHF
TVTRMAPVIL TCHSTGSPTP AVSWSKAGTQ LGARGSGYRI LPSGALEIER ALPLHAGRYT
CTARNSAGVA RKHMVLTVQA SPVVKPLPSV VQVVASEEVL LPCEASGIPQ PMVIWQKEGL
SIPEGAHMQV LPSGQLRIMH ASPEDAGNYF CIAQNSVGSA MAKTRLVVQV PPVIENGLPD
LSTIEGSHAL LPCTAKGSPE PAITWEKDGH LVSGAEGKFT LQPSGELLVK NSEGQDAGTY
ICTAENAVGR ARRRVHLTIL TLPVLTTLPG DRSLRLGDRL WLRCVARGSP TPRIGWTIND
QPVTEGVSEQ DGGSTLQRAA VTREDSGTYT CWAENRVGRV QAVSFVHVKE APVLQGEAFS
YLVEPVGGSI QLHCVVRGDP APDIHWTKDG LPLPISRLHF QLQNGSLTIL RTKMDDAGRY
QCLAVNEMGT VKKVVTVVLQ SAPVFQVEPQ DVTVRSGVDV ELRCRATGEP VPTIEWLRAG
RPLQAGRKLR ALPDGSLWLE HVEAGDAGVY ECVAHNHLGS VTAKALLAVR GEPRGSRGSM
TGVINGQEFG MATLNISVLQ QGSSEAPTIW SSISQVPASV GPLMRVLVVT IAPIYWALAR
ESGEALNGYS LTGGSFQQES QMEFSTGELL TMTQVARGLD PDGLLLVDMK INGMIPESLA
DGDLRVQDFQ EHYVQTGPGQ LFAGSTQRFL HDSLPASLRC NHSIQYDETR GLQPQLVQHL
RASSISSAFD PEAEALNFQL TTALQTEENE VGCPEGFEPD VQGAFCVDKD ECSGGPSPCS
HTCRNAPGHF SCSCPTGFSL AWDHRNCRDV DECAGNTHLC QEEQRCVNLL GSYNCLASCR
PGFRVTADGS NCEDVDECLE QLDECHYNQL CENTPGGHHC GCPRGYRQQG HSLPCLDINE
CLQLPTPCVY QCQNLQGSYR CLCPPGQTLL RDGRTCIPLE RNRQNITIVS HRSPFGPWLR
SRVPRPSSSY HTWVSLRPGS GALNSVGRAW CPPGFIRQDG VCADLDECRV RSLCQHACQN
TEGSYYCLCP SGYRLLPSGK NCQDINECEE DGIECGPGQM CFNTRGSFQC VDTPCPTTYR
QGSSPGTCFR RCSQDCSASG PSTLQYRLLP LPLGVRAHHD VARLAAFSEA GIPANRTELT
VLEPDPRSPF ALRQLRAGQG AVYTRRALTR AGLYRLTVRA AAPRHQSVYI LLIAVSPYPY
