ID W5NSH2_SHEEP Unreviewed; 891 AA.
AC W5NSH2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
GN Name=ITIH3 {ECO:0000313|Ensembl:ENSOARP00000001112.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000001112.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000001112.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000001112.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000001112.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037051}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the ITIH family.
CC {ECO:0000256|ARBA:ARBA00010158}.
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DR EMBL; AMGL01045508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004018441.1; XM_004018392.3.
DR AlphaFoldDB; W5NSH2; -.
DR SMR; W5NSH2; -.
DR STRING; 9940.ENSOARP00000001112; -.
DR PaxDb; 9940-ENSOARP00000001112; -.
DR Ensembl; ENSOART00000001146.1; ENSOARP00000001112.1; ENSOARG00000001064.1.
DR GeneID; 101109217; -.
DR KEGG; oas:101109217; -.
DR CTD; 3699; -.
DR eggNOG; ENOG502QPS2; Eukaryota.
DR HOGENOM; CLU_008101_0_0_1; -.
DR OMA; FNVIRFD; -.
DR OrthoDB; 608326at2759; -.
DR Proteomes; UP000002356; Chromosome 19.
DR Bgee; ENSOARG00000001064; Expressed in liver and 17 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030212; P:hyaluronan metabolic process; IEA:InterPro.
DR CDD; cd01461; vWA_interalpha_trypsin_inhibitor; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR010600; ITI_HC_C.
DR InterPro; IPR013694; VIT.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10338; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10338:SF115; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H3; 1.
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; vWA-like; 1.
DR PROSITE; PS51468; VIT; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..891
FT /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004868255"
FT DOMAIN 29..158
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 284..467
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
SQ SEQUENCE 891 AA; 99394 MW; B89F323D2E15887B CRC64;
MALARWLCLI LALLSGLAVS GFPRNPSRLL GKRSLPEGAV DGIEVYSTKV NCKVTSRFAH
NVVTTRAVNH ANTAKEVSFD VELPKTAFIT NFTLTIDGVT YPGNVKEKEV AKKQYEKAVS
QGKTAGLVKA SGRKLEKFTV SVNVAAGSKV TFELTYEELL KRHKGKYEMY LKVQPKQLVK
HFEITVDIFE PQGISTLDAE ASFITNDLLG SAFTKSFSGK KGHVSFKPSL DQQRSCPTCT
DSLLKGDFII TYDVNRESPA NVQIVNGYFV HFFAPQGLPV VPKSVVFVID VSGSMHGRKM
EQTKDALLKI LEDVKQDDYL NFILFSGDVT TWKDSLVPAT PENIQEARKF VMDIHDRGMT
NINDALLRGI SMLNKAREEH TVPERSTSII IMLTDGDANV GESRPEKIQE NVRNAIGGKF
PLYNLGFGNN LNYNFLENMA LENHGLARRI YEDSDASLQL QGFYEEVANP LLTGVEAEYP
QNAILDLTQN SYQHFYDGSE IVVAGRLADE DMNSFKAAVK GHGAINDLTF TEEVDMKEME
KALQEQDYIF GDYIERLWAY LTIEQLLEKR KNAWGEEKEN LTAQALELSL KYHFVTPLTS
MVVTKPEDNE NQTAIANKPG EGPLDAEVIP SMAYLTSYQG PKTPYYYVDG DPHFIIQIPE
KDDAICFNID EDPGTVLRLI QDPVTGLTVN GQIIGEKRGS SDSQNRRTYF GKLGIASAQM
DFRIEVTPEN ITLWNGDSLS TFSWLDTVMV TQDGLSVMIN RKKSMVVSFG DGVAFVVVLH
QVWKKEPAHH DFLGFYVVDS RGMSAQTHGL LGQFFHPFDF QVSDVHPGSD PTKPDATMVV
KNHQLTVTRG SQKDYGKDIS VGRNVACWFV HNNGQGLIDG IHRDYIVPNL F
//
