ITIH2_HUMAN
ID ITIH2_HUMAN Reviewed; 946 AA.
AC P19823; Q14659; Q15484; Q5T986;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H2;
DE Short=ITI heavy chain H2;
DE Short=ITI-HC2;
DE Short=Inter-alpha-inhibitor heavy chain 2;
DE AltName: Full=Inter-alpha-trypsin inhibitor complex component II;
DE AltName: Full=Serum-derived hyaluronan-associated protein;
DE Short=SHAP;
DE Flags: Precursor;
GN Name=ITIH2; Synonyms=IGHEP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-282 AND GLU-283, AND VARIANT SER-263.
RX PubMed=2450046; DOI=10.1016/0014-5793(88)80798-1;
RA Gebhard W., Schreitmueller T., Hochstrasser K., Wachter E.;
RT "Complementary DNA and derived amino acid sequence of the precursor of one
RT of the three protein components of the inter-alpha-trypsin inhibitor
RT complex.";
RL FEBS Lett. 229:63-67(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 384-865.
RX PubMed=2446322; DOI=10.1073/pnas.84.23.8272;
RA Salier J.-P., Diarra-Mehrpour M., Sesboue R., Bourguignon J., Benarous R.,
RA Ohkubo I., Kurachi S., Kurachi K., Martin J.-P.;
RT "Isolation and characterization of cDNAs encoding the heavy chain of human
RT inter-alpha-trypsin inhibitor (I alpha TI): unambiguous evidence for
RT multipolypeptide chain structure of I alpha TI.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8272-8276(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 384-766, AND VARIANT ALA-674.
RX PubMed=2462430;
RA Salier J.-P., Diarra-Mehrpour M., Sesboue R., Bourguignon J., Martin J.-P.;
RT "Human inter-alpha-trypsin inhibitor. Isolation and characterization of
RT heavy (H) chain cDNA clones coding for a 383 amino-acid sequence of the H
RT chain.";
RL Biol. Chem. Hoppe-Seyler 369:15-18(1988).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3663330; DOI=10.1515/bchm3.1987.368.2.963;
RA Schreitmueller T., Hochstrasser K., Resinger P.W.M., Wachter E.,
RA Gebhard W.;
RT "cDNA cloning of human inter-alpha-trypsin inhibitor discloses three
RT different proteins.";
RL Biol. Chem. Hoppe-Seyler 368:963-970(1987).
RN [6]
RP PROTEIN SEQUENCE OF 55-74; 116-127; 224-246; 295-307 AND 365-385,
RP IDENTIFICATION IN INTER-ALPHA-INHIBITOR COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=2476436; DOI=10.1016/s0021-9258(18)71575-5;
RA Enghild J.J., Thoegersen I.B., Pizzo S.V., Salvesen G.;
RT "Analysis of inter-alpha-trypsin inhibitor and a novel trypsin inhibitor,
RT pre-alpha-trypsin inhibitor, from human plasma. Polypeptide chain
RT stoichiometry and assembly by glycan.";
RL J. Biol. Chem. 264:15975-15981(1989).
RN [7]
RP PROTEIN SEQUENCE OF 55-64.
RC TISSUE=Plasma;
RX PubMed=1384548; DOI=10.1515/bchm3.1992.373.2.1009;
RA Malki N., Balduyck M., Maes P., Capon C., Mizon C., Han K.K., Tartar A.,
RA Fournet B., Mizon J.;
RT "The heavy chains of human plasma inter-alpha-trypsin inhibitor: their
RT isolation, their identification by electrophoresis and partial sequencing.
RT Differential reactivity with concanavalin A.";
RL Biol. Chem. Hoppe-Seyler 373:1009-1018(1992).
RN [8]
RP PROTEIN SEQUENCE OF 55-64 AND 681-702, CROSS-LINK STRUCTURE, AND
RP GLYCOSYLATION AT THR-691.
RX PubMed=7682553; DOI=10.1016/s0021-9258(18)52933-1;
RA Enghild J.J., Salvesen G., Thoegersen I.B., Valnickova Z., Pizzo S.V.,
RA Hefta S.A.;
RT "Presence of the protein-glycosaminoglycan-protein covalent cross-link in
RT the inter-alpha-inhibitor-related proteinase inhibitor heavy chain
RT 2/bikunin.";
RL J. Biol. Chem. 268:8711-8716(1993).
RN [9]
RP PROTEIN SEQUENCE OF 55-64, AND INTERACTION WITH TNFAIP6.
RX PubMed=7516184; DOI=10.1021/bi00189a049;
RA Wisniewski H.-G., Burgess W.H., Oppenheim J.D., Vilcek J.;
RT "TSG-6, an arthritis-associated hyaluronan binding protein, forms a stable
RT complex with the serum protein inter-alpha-inhibitor.";
RL Biochemistry 33:7423-7429(1994).
RN [10]
RP PROTEIN SEQUENCE OF 67-101, AND HYALURONAN BINDING.
RC TISSUE=Serum;
RX PubMed=7504674; DOI=10.1016/s0021-9258(19)74373-7;
RA Huang L., Yoneda M., Kimata K.;
RT "A serum-derived hyaluronan-associated protein (SHAP) is the heavy chain of
RT the inter alpha-trypsin inhibitor.";
RL J. Biol. Chem. 268:26725-26730(1993).
RN [11]
RP PROTEIN SEQUENCE OF 699-702, AND COVALENT LINKAGE WITH CHONDROITIN SULFATE.
RC TISSUE=Plasma;
RX PubMed=7513643; DOI=10.1111/j.1432-1033.1994.tb18803.x;
RA Morelle W., Capon C., Balduyck M., Sautiere P., Kouach M., Michalski C.,
RA Fournet B., Mizon J.;
RT "Chondroitin sulphate covalently cross-links the three polypeptide chains
RT of inter-alpha-trypsin inhibitor.";
RL Eur. J. Biochem. 221:881-888(1994).
RN [12]
RP GLYCOSYLATION AT ASN-118; THR-666; SER-673; THR-675 AND THR-691, AND MASS
RP SPECTROMETRY.
RX PubMed=9677337; DOI=10.1042/bj3330749;
RA Flahaut C., Capon C., Balduyck M., Ricart G., Sautiere P., Mizon J.;
RT "Glycosylation pattern of human inter-alpha-inhibitor heavy chains.";
RL Biochem. J. 333:749-756(1998).
RN [13]
RP GLYCOSYLATION AT ASN-118; THR-666; SER-673; THR-675 AND THR-691, AND
RP DISULFIDE BONDS.
RX PubMed=9425062; DOI=10.1021/bi971137d;
RA Olsen E.H.N., Rahbek-Nielsen H., Thoegersen I.B., Roepstorff P.,
RA Enghild J.J.;
RT "Posttranslational modifications of human inter-alpha-inhibitor:
RT identification of glycans and disulfide bridges in heavy chains 1 and 2.";
RL Biochemistry 37:408-416(1998).
RN [14]
RP GLYCOSYLATION AT ASN-118.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118 AND ASN-445.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP PHOSPHORYLATION AT SER-60; SER-466 AND SER-886.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
CC -!- FUNCTION: May act as a carrier of hyaluronan in serum or as a binding
CC protein between hyaluronan and other matrix protein, including those on
CC cell surfaces in tissues to regulate the localization, synthesis and
CC degradation of hyaluronan which are essential to cells undergoing
CC biological processes.
CC -!- SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or
CC two heavy chains (HC) and one light chain, bikunin. Inter-alpha-
CC inhibitor (I-alpha-I) is composed of ITIH1/HC1, ITIH2/HC2 and bikunin.
CC {ECO:0000269|PubMed:2476436}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate
CC esterified to the alpha-carboxyl of the C-terminal aspartate after
CC propeptide cleavage. {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core
CC 8 glycans. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320,
CC ECO:0000269|PubMed:7682553, ECO:0000269|PubMed:9425062,
CC ECO:0000269|PubMed:9677337}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000269|PubMed:26091039}.
CC -!- MASS SPECTROMETRY: Mass=76508; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9677337};
CC -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30160.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X07173; CAA30160.1; ALT_FRAME; mRNA.
DR EMBL; AL158044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M18193; AAA60558.1; -; mRNA.
DR EMBL; M33033; AAA59195.1; -; mRNA.
DR CCDS; CCDS31141.1; -.
DR PIR; S00346; IYHU2.
DR RefSeq; NP_002207.2; NM_002216.2.
DR AlphaFoldDB; P19823; -.
DR SMR; P19823; -.
DR BioGRID; 109904; 87.
DR IntAct; P19823; 16.
DR STRING; 9606.ENSP00000351190; -.
DR ChEMBL; CHEMBL4295727; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 285; 16 N-Linked glycans (2 sites), 5 O-Linked glycans (4 sites).
DR GlyGen; P19823; 13 sites, 19 N-linked glycans (2 sites), 15 O-linked glycans (10 sites).
DR iPTMnet; P19823; -.
DR PhosphoSitePlus; P19823; -.
DR BioMuta; ITIH2; -.
DR DMDM; 229462889; -.
DR CPTAC; CPTAC-676; -.
DR CPTAC; non-CPTAC-1134; -.
DR EPD; P19823; -.
DR jPOST; P19823; -.
DR MassIVE; P19823; -.
DR MaxQB; P19823; -.
DR PaxDb; P19823; -.
DR PeptideAtlas; P19823; -.
DR PRIDE; P19823; -.
DR ProteomicsDB; 53690; -.
DR Antibodypedia; 24443; 110 antibodies from 23 providers.
DR DNASU; 3698; -.
DR Ensembl; ENST00000358415.9; ENSP00000351190.4; ENSG00000151655.19.
DR GeneID; 3698; -.
DR KEGG; hsa:3698; -.
DR MANE-Select; ENST00000358415.9; ENSP00000351190.4; NM_002216.3; NP_002207.2.
DR UCSC; uc001ijs.4; human.
DR CTD; 3698; -.
DR DisGeNET; 3698; -.
DR GeneCards; ITIH2; -.
DR HGNC; HGNC:6167; ITIH2.
DR HPA; ENSG00000151655; Tissue enriched (liver).
DR MIM; 146640; gene.
DR neXtProt; NX_P19823; -.
DR OpenTargets; ENSG00000151655; -.
DR PharmGKB; PA29965; -.
DR VEuPathDB; HostDB:ENSG00000151655; -.
DR eggNOG; ENOG502QPS2; Eukaryota.
DR GeneTree; ENSGT00940000157945; -.
DR InParanoid; P19823; -.
DR OMA; GEWEDEM; -.
DR OrthoDB; 955432at2759; -.
DR PhylomeDB; P19823; -.
DR TreeFam; TF328982; -.
DR PathwayCommons; P19823; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P19823; -.
DR BioGRID-ORCS; 3698; 12 hits in 1065 CRISPR screens.
DR ChiTaRS; ITIH2; human.
DR GeneWiki; ITIH2; -.
DR GenomeRNAi; 3698; -.
DR Pharos; P19823; Tbio.
DR PRO; PR:P19823; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P19823; protein.
DR Bgee; ENSG00000151655; Expressed in liver and 116 other tissues.
DR ExpressionAtlas; P19823; baseline and differential.
DR Genevisible; P19823; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030212; P:hyaluronan metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR010600; ITI_HC_C.
DR InterPro; IPR013694; VIT.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF06668; ITI_HC_C; 1.
DR Pfam; PF08487; VIT; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00609; VIT; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS51468; VIT; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW Glycoprotein; Phosphoprotein; Protease inhibitor; Proteoglycan;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..54
FT /id="PRO_0000016517"
FT CHAIN 55..702
FT /note="Inter-alpha-trypsin inhibitor heavy chain H2"
FT /id="PRO_0000016518"
FT PROPEP 703..946
FT /id="PRO_0000016519"
FT DOMAIN 56..185
FT /note="VIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT DOMAIN 308..468
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 665..679
FT /note="O-glycosylated at three sites"
FT MOD_RES 60
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 282
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:2450046"
FT MOD_RES 283
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:2450046"
FT MOD_RES 466
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 702
FT /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT MOD_RES 886
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:9425062, ECO:0000269|PubMed:9677337"
FT /id="CAR_000140"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 666
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:9425062,
FT ECO:0000269|PubMed:9677337"
FT /id="CAR_000214"
FT CARBOHYD 673
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:9425062,
FT ECO:0000269|PubMed:9677337"
FT /id="CAR_000215"
FT CARBOHYD 675
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:9425062,
FT ECO:0000269|PubMed:9677337"
FT /id="CAR_000216"
FT CARBOHYD 691
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7682553,
FT ECO:0000269|PubMed:9425062, ECO:0000269|PubMed:9677337"
FT /id="CAR_000217"
FT DISULFID 261..264
FT /evidence="ECO:0000269|PubMed:9425062"
FT DISULFID 650..651
FT /evidence="ECO:0000269|PubMed:9425062"
FT VARIANT 263
FT /note="N -> S (in dbSNP:rs7075296)"
FT /evidence="ECO:0000269|PubMed:2450046"
FT /id="VAR_055248"
FT VARIANT 569
FT /note="L -> V (in dbSNP:rs7084817)"
FT /id="VAR_055249"
FT VARIANT 674
FT /note="P -> A (in dbSNP:rs3740217)"
FT /evidence="ECO:0000269|PubMed:2462430"
FT /id="VAR_055250"
FT CONFLICT 374
FT /note="K -> L (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="F -> S (in Ref. 3; AAA60558 and 4; AAA59195)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="N -> D (in Ref. 3; AAA60558 and 4; AAA59195)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="V -> A (in Ref. 3; AAA60558 and 4; AAA59195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 106463 MW; BA626B146DDC2A5F CRC64;
MKRLTCFFIC FFLSEVSGFE IPINGLSEFV DYEDLVELAP GKFQLVAENR RYQRSLPGES
EEMMEEVDQV TLYSYKVQST ITSRMATTMI QSKVVNNSPQ PQNVVFDVQI PKGAFISNFS
MTVDGKTFRS SIKEKTVGRA LYAQARAKGK TAGLVRSSAL DMENFRTEVN VLPGAKVQFE
LHYQEVKWRK LGSYEHRIYL QPGRLAKHLE VDVWVIEPQG LRFLHVPDTF EGHFDGVPVI
SKGQQKAHVS FKPTVAQQRI CPNCRETAVD GELVVLYDVK REEKAGELEV FNGYFVHFFA
PDNLDPIPKN ILFVIDVSGS MWGVKMKQTV EAMKTILDDL RAEDHFSVID FNQNIRTWRN
DLISATKTQV ADAKRYIEKI QPSGGTNINE ALLRAIFILN EANNLGLLDP NSVSLIILVS
DGDPTVGELK LSKIQKNVKE NIQDNISLFS LGMGFDVDYD FLKRLSNENH GIAQRIYGNQ
DTSSQLKKFY NQVSTPLLRN VQFNYPHTSV TDVTQNNFHN YFGGSEIVVA GKFDPAKLDQ
IESVITATSA NTQLVLETLA QMDDLQDFLS KDKHADPDFT RKLWAYLTIN QLLAERSLAP
TAAAKRRITR SILQMSLDHH IVTPLTSLVI ENEAGDERML ADAPPQDPSC CSGALYYGSK
VVPDSTPSWA NPSPTPVISM LAQGSQVLES TPPPHVMRVE NDPHFIIYLP KSQKNICFNI
DSEPGKILNL VSDPESGIVV NGQLVGAKKP NNGKLSTYFG KLGFYFQSED IKIEISTETI
TLSHGSSTFS LSWSDTAQVT NQRVQISVKK EKVVTITLDK EMSFSVLLHR VWKKHPVNVD
FLGIYIPPTN KFSPKAHGLI GQFMQEPKIH IFNERPGKDP EKPEASMEVK GQKLIITRGL
QKDYRTDLVF GTDVTCWFVH NSGKGFIDGH YKDYFVPQLY SFLKRP
