ID A0A2R9A3A7_PANPA Unreviewed; 878 AA.
AC A0A2R9A3A7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
GN Name=ITIH3 {ECO:0000313|Ensembl:ENSPPAP00000011792.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000011792.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000011792.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000011792.1}
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 -!- 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 EMBL; AJFE02064119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9A3A7; -.
DR Ensembl; ENSPPAT00000034453.1; ENSPPAP00000011792.1; ENSPPAG00000029064.1.
DR GeneTree; ENSGT00940000154554; -.
DR Proteomes; UP000240080; Chromosome 3.
DR Bgee; ENSPPAG00000029064; Expressed in liver and 6 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:UP000240080};
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..878
FT /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015330770"
FT DOMAIN 29..158
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 278..461
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 196..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 98330 MW; BB0685D32DDB52CD CRC64;
MASAWWPCLI LALLSSLAAS GFPRSPIRLL GKRSLPEGVA NGIEVYSTKI NSKVTSRFAH
NVVTTRAINR ADTAKEVSFD VELPKTAFIT NFTLTIDGVT YPGNVKEKEV AKKQYEKAVS
QGKTAGLVKA SGRKLEKFTV SVTVAAGSKV TFELTYEELL KRHKGKYEMY LKVQPKQLVK
HFEVINRPCR PGGTAAGWVK NKSSASRHPP SLAGKGHVSF KPSLDQQRSC PTCTDSLLNG
DFTITYDVNR ESPGNVQIVN GYFVHFFAPQ GLPVVPKNVA FVIDISGSMA GRKLEQTKEA
LLRILEDMKE EDYLNFILFS GDVSTWKEHL VQATPENLQE ARTFVKSMED KGMTNINDGL
LRGISMLNKA REEHRIPERS TSIVIMLTDG DANVGESRPE KIQENVRNAI GGKFPLYNLG
FGNNLNYNFL ENMALENHGF ARRIYEDSDA DLQLQGFYEE VANPLLTGVE MEYPENAILD
LTQNTYQHFY DGSEIVVAGR LVDEDMNSFK ADVKGHGATN DLTFTEEVDM KEMEKALQER
DYIFGNYIER LWAYLTIEQL LEKRKNAHGE EKENLTAWAL DLSLKYHFVT PLTSMVVTKP
EDNEDERAIA DKPGEDAEGK PLATSYQPPQ NPYYYVDGDP HFIIQIPEKD DALCFNIDEA
PGTVLRLIQD PVTGLTVNGQ IIGDKRGSPD SKTRKTYFGK LGIANAQMDF QVEVTTGKIT
LWNRAMPSTF SWLDTVTVTQ DGLSMMINRK NMVVSFGDGV TFVVVLHQVW KKHPVHRDFL
GFYVVDSHRM SAQTHGLLGQ FFQPFDFKVS DIRPGSDPTK PDATLVVKNH QLIVTRGSQK
DYRKDASIGT KVVCWFVHNN GEGLIDGVHT DYIVPNLF
//
