ITIH1_MOUSE
ID ITIH1_MOUSE Reviewed; 907 AA.
AC Q61702; Q3UEI9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H1;
DE Short=ITI heavy chain H1;
DE Short=ITI-HC1;
DE Short=Inter-alpha-inhibitor heavy chain 1;
DE Flags: Precursor;
GN Name=Itih1;
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].
RC STRAIN=C57BL/6N; TISSUE=Liver;
RX PubMed=7534067; DOI=10.1042/bj3060505;
RA Chan P., Risler J.-L., Raguenez G., Salier J.-P.;
RT "The three heavy-chain precursors for the inter-alpha-inhibitor family in
RT mouse: new members of the multicopper oxidase protein group with
RT differential transcription in liver and brain.";
RL Biochem. J. 306:505-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-585.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-585.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: 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. {ECO:0000250}.
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 Interacts with TNFAIP6 (via Link and CUB domains).
CC {ECO:0000250|UniProtKB:P19827}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Liver specific.
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: The S-linked glycan is composed of two 6-carbon sugars, possibly
CC Glc or Gal. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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DR EMBL; X70391; CAA49841.1; -; mRNA.
DR EMBL; AK149500; BAE28922.1; -; mRNA.
DR EMBL; CH466573; EDL24774.1; -; Genomic_DNA.
DR CCDS; CCDS49435.1; -.
DR PIR; S54353; S54353.
DR RefSeq; NP_001293007.1; NM_001306078.1.
DR RefSeq; NP_032432.2; NM_008406.3.
DR AlphaFoldDB; Q61702; -.
DR SMR; Q61702; -.
DR BioGRID; 200836; 6.
DR IntAct; Q61702; 1.
DR STRING; 10090.ENSMUSP00000126449; -.
DR GlyGen; Q61702; 5 sites.
DR iPTMnet; Q61702; -.
DR PhosphoSitePlus; Q61702; -.
DR SwissPalm; Q61702; -.
DR CPTAC; non-CPTAC-3534; -.
DR CPTAC; non-CPTAC-3832; -.
DR MaxQB; Q61702; -.
DR PaxDb; Q61702; -.
DR PRIDE; Q61702; -.
DR ProteomicsDB; 269409; -.
DR Antibodypedia; 31337; 280 antibodies from 24 providers.
DR DNASU; 16424; -.
DR Ensembl; ENSMUST00000163118; ENSMUSP00000126449; ENSMUSG00000006529.
DR GeneID; 16424; -.
DR KEGG; mmu:16424; -.
DR UCSC; uc007svz.1; mouse.
DR CTD; 3697; -.
DR MGI; MGI:96618; Itih1.
DR VEuPathDB; HostDB:ENSMUSG00000006529; -.
DR eggNOG; ENOG502RXR2; Eukaryota.
DR GeneTree; ENSGT00940000162180; -.
DR HOGENOM; CLU_008101_0_0_1; -.
DR InParanoid; Q61702; -.
DR OMA; FNFLEAM; -.
DR OrthoDB; 955432at2759; -.
DR PhylomeDB; Q61702; -.
DR TreeFam; TF328982; -.
DR BioGRID-ORCS; 16424; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q61702; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q61702; protein.
DR Bgee; ENSMUSG00000006529; Expressed in left lobe of liver and 29 other tissues.
DR ExpressionAtlas; Q61702; baseline and differential.
DR Genevisible; Q61702; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005540; F:hyaluronic acid binding; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
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 Glycoprotein; Phosphoprotein; Protease inhibitor; Proteoglycan;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..31
FT /evidence="ECO:0000250"
FT /id="PRO_0000016509"
FT CHAIN 32..668
FT /note="Inter-alpha-trypsin inhibitor heavy chain H1"
FT /id="PRO_0000016510"
FT PROPEP 669..907
FT /evidence="ECO:0000250"
FT /id="PRO_0000016511"
FT DOMAIN 34..163
FT /note="VIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT DOMAIN 287..447
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19827"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19827"
FT MOD_RES 668
FT /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="S-linked (Hex...) cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 650
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q0VCM5"
FT CONFLICT 344
FT /note="A -> V (in Ref. 1; CAA49841)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="I -> T (in Ref. 1; CAA49841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 907 AA; 101067 MW; AF430E611C1755CD CRC64;
MEGATGLRVL LCLLPLLTLQ ARPALGLATG RPRGSEKRHA VDTSVNGVSI KSLKVNCKVT
SRFAHYVITS QVVNNADKAR EVAFDVEIPK TAFISDFAIT SDGKAFIGDI KDKVTAWKQY
RKAAVLGESA GLVRASGRNM EQFTIHITVG AQSKATFRLT YEEVLKRRLM QYDITIKVRP
KQLVQHFEID VDIFEPQGIS KLDAQASFLS EELAAQTIKK SFSGKKGHVL FRPTVSQQQS
CPTCSTSLLN GEFKVTYDVN RDKLCDLLVA NNYFTHFFAP KNLTNMSKNL VFVIDISGSM
EGQKVRQTKE ALLKILEDMR PVDNFDLVLF GSKVQSWKGS LVPASNANLQ AAQDFVRRFS
LAGATNLNGG LLRGIEILNK AQGSHPELSS PASILIMLTD GEPTEGETDR SQILKNVRNA
IRGRFPLYNL GFGHDLDFSF LEVMSTENNG WAQRIYEDHD ATQQLQGFYN QVANPLLTDV
ELQYPQDAVL ALTQHRHKQY YDGSEIVVAG RIANHKLNTF KADVRARGEK QEFRATCLVD
EEEMKKLLRE RGHVLENHVE RLWAYLTIQE LLAKRMKTEG EERANLSSQV LKMSLDYHFV
TPLTSLTIRG LTDEDGLEPT IDKPLEDSQP LEMVGPRRTF VLSAIQPSPT AHPIDSKLPL
RVTGVDTDPH FIIYVPSKED SLCFNINEEP GVILNLVQDP DTGFTVNGQL IGNKASSPGQ
HESTYFGRLG ISSPTSDFQL EVTPQNITLN PSSSGSMFSW RDQAVLQKDG VVVTINKKRN
LVVSVDDGAT FEIVLHRTWK GSAVHQDFLG FYVLDSFRMS ARTKGLLGQF FSPLDFEVFD
LHPGSDPTKT DATMVVKNRQ LTVTRGLQKD YSKDPRHGAE VPCWFVHDNG AGLIDGVHTD
YVVSDIF
