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Database: UniProt
Entry: A0A2K6DLK0_MACNE
LinkDB: A0A2K6DLK0_MACNE
Original site: A0A2K6DLK0_MACNE 
ID   A0A2K6DLK0_MACNE        Unreviewed;       699 AA.
AC   A0A2K6DLK0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
GN   Name=ITIH3 {ECO:0000313|Ensembl:ENSMNEP00000036787.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000036787.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000036787.1}
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; A0A2K6DLK0; -.
DR   Ensembl; ENSMNET00000061253.1; ENSMNEP00000036787.1; ENSMNEG00000041402.1.
DR   GeneTree; ENSGT00940000154554; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000041402; 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:UP000233120};
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..699
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014353906"
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   699 AA;  77857 MW;  156F1AD42B29D706 CRC64;
     MASAWWPCLI LALLSGLAAS GFPRGPFLLL GKRSLPEGVA NGVEVYSTKI NSKVTSRFAH
     NVVTTRAVNR ADTAKEVSFD VELPKTAFIT NFTLTIDGVT YPGNVKEKEV AKKQYEKAVS
     QGKTAGLVKA SGRKLEKFTV SVNVAAGSKV TFELTYEELL KRHKGKYEMY LKVQPKQLIK
     HFEIDVDIFE PQGISMLDAE ASFITNDLLG SALTKSFSGK KGHVSFKPSL DQQRSCPTCT
     DSLLNGDFTI TYDVNRESPG NVQIVNGYFV HFFAPQGLPV VPKNVAFVID ISGSMAGRKL
     EQTKEALLRI LEDMKEEDYL NFILFSGDVS TWKEHLVQAT PENLQEARTF VKSMEDKGMT
     NINDGLLRGI SMLNKAREEH RVPERSTSIV IMLTDGDANV GESRPEKIQE NVRNAIGGKF
     PLYNLGFGNN LNYNFLENMA LENHGFARRI YEDSDADLQL QGFYEEVANP LLTGVEMEYP
     ENAILGLTQN TYQHFYDGSE IVVAGRLVGE DMNSFKADVK GHGAANDLTF TEEVTTEKIT
     LWNRAVPSTF SWLDTVTVTQ DGLSMMINRK KNMVVSFGDG VTFVVVLHQV WKKHPVHRDF
     LGFYVVDSDR MSAQTHGLLG QFFQPFDFKV SDIRPGSDPT KPDATLVVKN HQLTVTRGSQ
     KDYRKDASIG TKVVCWFVHN NGEGLIDGVH TDYIVPNLF
//
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