PRG4_MOUSE
ID PRG4_MOUSE Reviewed; 1054 AA.
AC Q9JM99; Q3UEL1; Q3V198;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Proteoglycan 4;
DE AltName: Full=Lubricin;
DE AltName: Full=Megakaryocyte-stimulating factor;
DE AltName: Full=Superficial zone proteoglycan;
DE Contains:
DE RecName: Full=Proteoglycan 4 C-terminal part;
DE Flags: Precursor;
GN Name=Prg4; Synonyms=Msf, Szp;
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 [MRNA] (ISOFORM A), TISSUE SPECIFICITY, AND
RP IDENTIFICATION OF ISOFORMS B; C AND D.
RX PubMed=11124536; DOI=10.1159/000056791;
RA Ikegawa S., Sano M., Koshizuka Y., Nakamura Y.;
RT "Isolation, characterization and mapping of the mouse and human PRG4
RT (proteoglycan 4) genes.";
RL Cytogenet. Cell Genet. 90:291-297(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 572-1054.
RC STRAIN=C57BL/6J; TISSUE=Head, and Liver;
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 FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15719068; DOI=10.1172/jci200522263;
RA Rhee D.K., Marcelino J., Baker M., Gong Y., Smits P., Lefebvre V.,
RA Jay G.D., Stewart M., Wang H., Warman M.L., Carpten J.D.;
RT "The secreted glycoprotein lubricin protects cartilage surfaces and
RT inhibits synovial cell overgrowth.";
RL J. Clin. Invest. 115:622-631(2005).
RN [4]
RP PROTEOLYTIC PROCESSING, DISULFIDE BOND, AND MUTAGENESIS OF
RP 949-ARG--ARG-955; 949-ARG--ARG-951; CYS-795; 851-CYS--CYS-853; CYS-930 AND
RP CYS-1053.
RX PubMed=16000300; DOI=10.1074/jbc.m505401200;
RA Rhee D.K., Marcelino J., Al-Mayouf S., Schelling D.K., Bartels C.F.,
RA Cui Y., Laxer R., Goldbach-Mansky R., Warman M.L.;
RT "Consequences of disease-causing mutations on lubricin protein synthesis,
RT secretion, and post-translational processing.";
RL J. Biol. Chem. 280:31325-31332(2005).
CC -!- FUNCTION: Plays a role in boundary lubrication within articulating
CC joints. Prevents protein deposition onto cartilage from synovial fluid
CC by controlling adhesion-dependent synovial growth and inhibiting the
CC adhesion of synovial cells to the cartilage surface.
CC {ECO:0000269|PubMed:15719068}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:16000300}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q92954}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=A;
CC IsoId=Q9JM99-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9JM99-2; Sequence=VSP_016471;
CC Name=C;
CC IsoId=Q9JM99-3; Sequence=VSP_016472;
CC Name=D;
CC IsoId=Q9JM99-4; Sequence=VSP_016471, VSP_016472;
CC Name=E;
CC IsoId=Q9JM99-5; Sequence=VSP_016472, VSP_016473;
CC -!- TISSUE SPECIFICITY: Highly expressed in cartilage, bone and liver and
CC weakly expressed in heart, brain and muscle. Expressed in the surface
CC chondrocytes and in synovial intimal cells. Isoform B is expressed in
CC bone, small intestine, muscle, testis, heart, liver and lung. Isoform C
CC and isoform D are widely expressed. {ECO:0000269|PubMed:11124536,
CC ECO:0000269|PubMed:15719068}.
CC -!- DEVELOPMENTAL STAGE: First detected at the forming joint surface from
CC 15.5 dpc, after cavitation has begun. At later stages of morphogenesis,
CC strong expression is observed in cartilage surface cells (superficial
CC zone chondocytes) and in the newly forming synovium.
CC {ECO:0000269|PubMed:15719068}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92954}.
CC -!- PTM: O-glycosylated; contains glycosaminoglycan chondroitin sulfate and
CC keratan sulfate. O-glycosylated with sialylated oligosaccharides which
CC are predominantly represented by the monosialylated core type I
CC structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of
CC disialylated O-glycans. {ECO:0000250|UniProtKB:Q92954}.
CC -!- PTM: The disulfide bond between Cys-795 and Cys-1053 is essential for
CC protein cleavage. {ECO:0000269|PubMed:16000300}.
CC -!- PTM: Proteolytically cleaved by cathepsin CTSG.
CC {ECO:0000250|UniProtKB:Q92954}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile. In the newborn
CC period, their joints appear normal. The aged mice exhibit abnormal
CC protein deposits on the cartilage surface and disappearance of
CC underlying superficial zone chondrocytes. In addition to cartilage
CC surface changes and subsequent cartilage deterioration, intimal cells
CC in the synovium surrounding the joint space become hyperplastic, which
CC further contribute to joint failure. {ECO:0000269|PubMed:15719068}.
CC -!- MISCELLANEOUS: Different forms varying in molecular weight have been
CC observed. Such forms are possibly due to different levels of
CC glycosylation and protein cleavage.
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DR EMBL; AB034730; BAA92310.1; -; mRNA.
DR EMBL; AK132597; BAE21253.1; -; mRNA.
DR EMBL; AK149469; BAE28900.1; -; mRNA.
DR CCDS; CCDS48391.1; -. [Q9JM99-5]
DR RefSeq; NP_001103616.1; NM_001110146.1.
DR AlphaFoldDB; Q9JM99; -.
DR SMR; Q9JM99; -.
DR BioGRID; 220515; 4.
DR GlyGen; Q9JM99; 60 sites.
DR iPTMnet; Q9JM99; -.
DR PhosphoSitePlus; Q9JM99; -.
DR CPTAC; non-CPTAC-3938; -.
DR MaxQB; Q9JM99; -.
DR PaxDb; Q9JM99; -.
DR PeptideAtlas; Q9JM99; -.
DR PRIDE; Q9JM99; -.
DR ProteomicsDB; 291868; -. [Q9JM99-1]
DR ProteomicsDB; 291869; -. [Q9JM99-2]
DR ProteomicsDB; 291870; -. [Q9JM99-3]
DR ProteomicsDB; 291871; -. [Q9JM99-4]
DR ProteomicsDB; 291872; -. [Q9JM99-5]
DR DNASU; 96875; -.
DR GeneID; 96875; -.
DR KEGG; mmu:96875; -.
DR CTD; 10216; -.
DR MGI; MGI:1891344; Prg4.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; Q9JM99; -.
DR BioGRID-ORCS; 96875; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Prg4; mouse.
DR PRO; PR:Q9JM99; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JM99; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR CDD; cd00094; HX; 1.
DR Gene3D; 2.110.10.10; -; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR Pfam; PF00045; Hemopexin; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00120; HX; 2.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF50923; SSF50923; 1.
DR SUPFAM; SSF90188; SSF90188; 2.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1054
FT /note="Proteoglycan 4"
FT /id="PRO_0000043234"
FT CHAIN 956..1054
FT /note="Proteoglycan 4 C-terminal part"
FT /id="PRO_0000043235"
FT DOMAIN 26..69
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 66..108
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REPEAT 317..324
FT /note="1; approximate"
FT REPEAT 325..332
FT /note="2; approximate"
FT REPEAT 333..340
FT /note="3; approximate"
FT REPEAT 349..356
FT /note="4; approximate"
FT REPEAT 357..364
FT /note="5"
FT REPEAT 365..371
FT /note="6; approximate"
FT REPEAT 372..379
FT /note="7"
FT REPEAT 380..387
FT /note="8"
FT REPEAT 388..395
FT /note="9"
FT REPEAT 396..403
FT /note="10"
FT REPEAT 404..411
FT /note="11"
FT REPEAT 412..418
FT /note="12; approximate"
FT REPEAT 419..426
FT /note="13"
FT REPEAT 427..434
FT /note="14"
FT REPEAT 435..442
FT /note="15"
FT REPEAT 443..450
FT /note="16; approximate"
FT REPEAT 451..458
FT /note="17"
FT REPEAT 459..466
FT /note="18"
FT REPEAT 467..474
FT /note="19"
FT REPEAT 475..482
FT /note="20"
FT REPEAT 483..490
FT /note="21"
FT REPEAT 491..498
FT /note="22"
FT REPEAT 499..506
FT /note="23"
FT REPEAT 507..514
FT /note="24"
FT REPEAT 515..522
FT /note="25"
FT REPEAT 523..530
FT /note="26"
FT REPEAT 531..538
FT /note="27"
FT REPEAT 539..546
FT /note="28"
FT REPEAT 547..554
FT /note="29"
FT REPEAT 555..562
FT /note="30"
FT REPEAT 563..570
FT /note="31"
FT REPEAT 571..578
FT /note="32"
FT REPEAT 579..586
FT /note="33"
FT REPEAT 587..594
FT /note="34"
FT REPEAT 595..602
FT /note="35"
FT REPEAT 603..610
FT /note="36"
FT REPEAT 611..618
FT /note="37"
FT REPEAT 797..840
FT /note="Hemopexin 1"
FT REPEAT 841..888
FT /note="Hemopexin 2"
FT REGION 110..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..618
FT /note="37 X 8 AA repeats of K-X-P-X-P-T-T-X"
FT COMPBIAS 110..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..696
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 955..956
FT /note="Cleavage; by subtilisin-like proprotein convertase
FT 4"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 237
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 250
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 301
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 302
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 306
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 313
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 327
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 330
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 338
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 354
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 362
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 369
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 377
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 378
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 385
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 386
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 393
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 394
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 416
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 417
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 424
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 432
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 433
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 440
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 441
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 448
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 472
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 480
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 481
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 488
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 489
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 496
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 497
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 504
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 505
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 512
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 520
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 521
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 528
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 529
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 553
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 560
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 561
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 568
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 569
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 576
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 577
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 592
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 600
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 601
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 622
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 624
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 628
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 629
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 692
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 810
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q92954"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..46
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 30..34
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 34..64
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 44..57
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 44..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 50..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 57..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 70..86
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 70..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 74..104
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 84..97
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 84..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 90..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 97..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 795..1053
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:16000300"
FT VAR_SEQ 26..66
FT /note="Missing (in isoform B and isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_016471"
FT VAR_SEQ 107..194
FT /note="Missing (in isoform C, isoform D and isoform E)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016472"
FT VAR_SEQ 224..766
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016473"
FT MUTAGEN 795
FT /note="C->A: Not cleaved by subtilisin-like proprotein
FT convertase. Not cleaved by subtilisin-like proprotein
FT convertase; when associated with A-1053."
FT /evidence="ECO:0000269|PubMed:16000300"
FT MUTAGEN 851..853
FT /note="CNC->ANA: Cleaved by subtilisin-like proprotein
FT convertase."
FT /evidence="ECO:0000269|PubMed:16000300"
FT MUTAGEN 851
FT /note="C->A: Cleaved by subtilisin-like proprotein
FT convertase."
FT MUTAGEN 930
FT /note="C->A: Cleaved by subtilisin-like proprotein
FT convertase."
FT /evidence="ECO:0000269|PubMed:16000300"
FT MUTAGEN 949..955
FT /note="RRRRFER->ARARFEA: Not cleaved by subtilisin-like
FT proprotein convertase 4."
FT /evidence="ECO:0000269|PubMed:16000300"
FT MUTAGEN 949..951
FT /note="RRR->ARA: Cleaved by subtilisin-like proprotein
FT convertase 4."
FT /evidence="ECO:0000269|PubMed:16000300"
FT MUTAGEN 955
FT /note="R->A: Not cleaved by subtilisin-like proprotein
FT convertase 4."
FT MUTAGEN 1053
FT /note="C->A: Not cleaved by subtilisin-like proprotein
FT convertase 4. Not cleaved by subtilisin-like proprotein
FT convertase; when associated with A-795."
FT /evidence="ECO:0000269|PubMed:16000300"
FT CONFLICT 65..66
FT /note="SP -> TT (in Ref. 2; BAE28900)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="S -> A (in Ref. 1; BAA92310)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="Q -> R (in Ref. 1; BAA92310)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="L -> P (in Ref. 1; BAA92310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1054 AA; 115996 MW; 13312FB7070DF2A4 CRC64;
MGWKILPVCL SLLLPVVLIQ QVSSQDLSSC AGRCGEGYSR DATCNCDYNC QHYMECCPDF
KRVCSPELSC KGRCFESFAR GRECDCDSQC KQYGKCCADY DSFCEEVHNS TSPSSKTAPT
PAGASDTIKS TTKRSPKSPT TRTIKVVESE ELTEEHSDSE NQESSSSSSS SSSTIRKIKS
SKNSANRELQ KNPNVKDNKK NTPKKKPNPE PPAVDEAGSG LDNGEFKLTP PPPDPPTTPH
SKVATSPKTT AAKPVTPKPS LAPNSETSKE ASLASNKETT VETKETTATN KQSSASKKKT
TSVKETRSAE KTSDKDVEPT STTPKNSAPT TTKKPVTTTK ESKFLPLPQE PEPTTAKEPP
PTTKKPEPTT RKEPEPTTPK EPEPTTPKEP EPTTPKEPEP TTPKEPPPTT KKPEPTTPKE
PGPTTPKEPE PTTTKEPEPT TTKEPESTTR KEPEPTTPKE PEPTTPKEPE PTTLKEPEPT
TPKEPEPTTP KEPEPTTPKE PEPTTPKEPE PTTPKEPEPT TPKEPEPTTP KEPEPTTPKE
PEPTTPKKPE PTTPKEPVPT TPKEPEPTTP KEPEPTTPKE PEPTTRKEPE PTTPKEPEPT
TPKEPEPTTP KKPEPTTTSP KTTTLKATTL APKVTAPAEE IQNKPEETTP ASEDSDDSKT
TLKPQKPTKA PKPTKKPTKA PKKPTSTKKP KTPKTRKPKT TPSPLKTTSA TPELNTTPLE
VMLPTTTIPK QTPNPETAEV NPDHEDADGG EGEKPLIPGP PVLFPTAIPG TDLLAGRLNQ
GININPMLSD ETNLCNGKPV DGLTTLRNGT LVAFRGHYFW MLNPFRPPSP PRRITEVWGI
PSPIDTVFTR CNCEGKTFFF KDSQYWRFTN DVVDPGYPKQ IVKGFGGLTG KIVAALSIAK
YKDRPESVYF FKRGGNIQQY TYKQEPMKKC TGRRPAINYS VYGEAAQVRR RRFERAVGPF
QTHTFRIHYS VPMRVSYQDK GFLHNEVKVS TMWRGFPNVV TSAITLPNIR KPDGYDYYAF
SKDQYYNIDV PTRTARAITT RSGQTLSKIW YNCP
