ID A0A2K6K549_RHIBE Unreviewed; 885 AA.
AC A0A2K6K549;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
GN Name=ITIH3 {ECO:0000313|Ensembl:ENSRBIP00000006369.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000006369.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000006369.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000006369.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or
CC two heavy chains (HC) and one light chain, bikunin. Pre-alpha-inhibitor
CC (P-alpha-I) is composed of ITIH3/HC3 and bikunin.
CC {ECO:0000256|ARBA:ARBA00038801}.
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 AlphaFoldDB; A0A2K6K549; -.
DR Ensembl; ENSRBIT00000029348.1; ENSRBIP00000006369.1; ENSRBIG00000026208.1.
DR GeneTree; ENSGT00940000154554; -.
DR Proteomes; UP000233180; Unplaced.
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:UP000233180};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..885
FT /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014434837"
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 885 AA; 98850 MW; 2392CF0DFA2F5B44 CRC64;
MASAWWPCLI LALLSGLAAS GFPRSPFQLL GKRSLPEGVA DGVEVYSTKI NSKVTSRFAH
NVVTTRAVNR ADTAKEVSFD VELPKTAFIT NFTLTIDGVT YPGNVKEKEV AKKQYEKAVS
QGKTAGLVKA SGRKLEKFTV SVNVAAGSKV TFELTYEELL KRHKGKYEMY LKVQPKQLVK
HFEIDVDIFE PQGISMLDAE ASFITNDLLG SALTKSFSGK KGHVSFKPSL DQQRSCPTCT
DSLLNGDFTI TYDVNRESPG NVQIVNGYFV HFFAPQGLPV VPKNVAFVID ISGSMAGRKL
EQTKEALLRI LEDMKEEDYL NFILFSGDVS TWKEHLVQAT PENLQEARTF VKSMEDKGMT
NINDGLLRGI SMLNKAREEH RVPERSTAIV IMLTDGDANV GESRPEKIQE NVRNAIGGKF
PLYNLGFGNN LNYNFLENMA LENHGFARRI YEDSDADLQL QGFYEEVANP LLTGVEMDYP
ENAILGLTQN TYQHFYDGSE IVVAGHLVGE DVNSFKADVK GHGATNDLTF TEEVDMKEME
KALQERDYIF GNYIERLWAY LTIEQLLEKR KNAHGEEKEN LTAQALDLSL KYHFVTPLTS
MVVTKPEDNE DERAIADKPG EAPSPFVSAA SYQPPQNPYY HVDGDPHFII QVPEKDDALC
FNINEAPGTI LRLIQDPVTG LTVNGQIIGD KRGSPDSKTR KTYFGKLGIA NAQMDFQVEV
TTEKITLWNR AVPSTFSWLD TVTVTQDGLS MMINRKKNMV VSFGDGVTFV VVLHQVWKKH
PVHHDFLGFY VVDSHRMSAQ THGLLGQFFQ PFDFKVSDIR PGSDPTKPDA TLVVKTHQLT
VTRGSQKDYR KDANIGTKVV CWFVHNNGEG LIDGVHTDYI VPNLF
//
