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Database: UniProt
Entry: A0A2R9A8R1_PANPA
LinkDB: A0A2R9A8R1_PANPA
Original site: A0A2R9A8R1_PANPA 
ID   A0A2R9A8R1_PANPA        Unreviewed;       698 AA.
AC   A0A2R9A8R1;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
GN   Name=ITIH3 {ECO:0000313|Ensembl:ENSPPAP00000011796.1};
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:ENSPPAP00000011796.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000011796.1, 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:ENSPPAP00000011796.1}
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; A0A2R9A8R1; -.
DR   Ensembl; ENSPPAT00000034457.1; ENSPPAP00000011796.1; 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..698
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015315185"
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   698 AA;  77967 MW;  7EECC45E0C32EB44 CRC64;
     MASAWWPCLI LALLSSLAAS GFPRSPIRLL GKRSLPEGVA NGIEVYSTKI NSKVTSRFAH
     NVVTTRAINR ADTAKEVSFD VELPKTAFIT NFTLTIDGVT YPGNVKEKEV AKKQYEKAVS
     QGKTAGLVKA SGRKLEKFTV SVTVAAGSKV TFELTYEELL KRHKGKYEMY LKVQPKQLVK
     HFEIEVDIFE PQGISMLDAE ASFITNDLLG SALTKSFSGK KGHVSFKPSL DQQRSCPTCT
     DSLLNGDFTI TYDVNRESPG NVQIVNGYFV HFFAPQGLPV VPKNVAFVID ISGSMAGRKL
     EQTKEALLRI LEDMKEEDYL NFILFSGDVS TWKEHLVQAT PENLQEARTF VKSMEDKGMT
     NINDGLLRGI SMLNKAREEH RIPERSTSIV IMLTDGDANV GESRPEKIQE NVRNAIGGKF
     PLYNLGFGNN LNYNFLENMA LENHGFARRI YEDSDADLQL QGFYEEVANP LLTGVEMEYP
     ENAILDLTQN TYQHFYDGSE IVVAGRLVDE DMNSFKADVK GHGATNDLTF TEEVTTGKIT
     LWNRAMPSTF SWLDTVTVTQ DGLSMMINRK NMVVSFGDGV TFVVVLHQVW KKHPVHRDFL
     GFYVVDSHRM SAQTHGLLGQ FFQPFDFKVS DIRPGSDPTK PDATLVVKNH QLIVTRGSQK
     DYRKDASIGT KVVCWFVHNN GEGLIDGVHT DYIVPNLF
//
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