ID   U3K2V4_FICAL            Unreviewed;       891 AA.
AC   U3K2V4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
GN   Name=ITIH3 {ECO:0000313|Ensembl:ENSFALP00000009358.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000009358.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000009358.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000009358.2}
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   -!- 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; U3K2V4; -.
DR   STRING; 59894.ENSFALP00000009358; -.
DR   Ensembl; ENSFALT00000009398.2; ENSFALP00000009358.2; ENSFALG00000008971.2.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   GeneTree; ENSGT00940000154554; -.
DR   HOGENOM; CLU_008101_0_0_1; -.
DR   Proteomes; UP000016665; Chromosome 12.
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   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:UP000016665};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..891
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5032856275"
FT   DOMAIN          29..158
FT                   /note="VIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51468"
FT   DOMAIN          283..466
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
SQ   SEQUENCE   891 AA;  100030 MW;  0E0AA54AF5BB72AD CRC64;
     MENKLLLCIL LLIPAFASSD FLLTHVRNIK KRSADNDLVV NGIEIYSMKI DSKVTSRFAH
     NVITSRAVNQ GNVSKEVFFD VELPKTAFIT KFSMTIDGVT YPGTIKEKEA AKKQYEKAVS
     RGQTAGLVRA SGRKTEKFTV SVNIKAASKV TFELTYEELL KRQFGKYEMF IKVKPKQLVK
     DFEIEVDIFE PQGIAELEAE GTFITNELQN IIKKTFSGKK GHISFKPTLD QQRTCANCSQ
     SALDGDFTVR YDVKRTTPDN LQIVNGYFVH FFAPTNLPKL SKNIIFVLDT SGSMYGREME
     QTKEALLKIL DDIKEDDFFN FILFDSEIST WKETLIKATP ENLDEARKFV QHISAQGMTN
     LHGGLMRGID ILNAAHEQNL VPKRSASIII MLTDGQPNVG VSNTHEIEKA VKKAIDGRYT
     LYNLGFGSGV DYGFLEKMAL ENKGLARRIY PDSDAALQLQ GFYDEVSNPM LIDVELNYPE
     NEISDLTTNS FKHFYDGSEI VVAGRFVDSN QNHLSVDVRG EGADDALLYT TQQDAEQTAQ
     AFQEQQYIFG EYIERLWAYL TIEQLLEKRI TATGEEKENL TAQALALSLM YKFVTPLTSM
     VVTKPEEDDN EEGIADKPTE GVGMFTSLLQ ASPVYHTYAS PPTWYTSVDG DPHFIISVPQ
     KKDAICFNIN ENPGMILNLI NDPVTGITVN GELIGDKRAN SDAKIQNSYF GKLGIANKHL
     DVKLTVTPET ITIQNGDEKT GFTWLDSVTL HQADLTLIIN RKKNLVLSMG SGVSFVVVLH
     QVWKKHPLHQ DFLGLYTLKS DELSEQTHGL LGQFFRPIDF TIIEIHPGSD PKKPDATMIV
     KNNELTVTRG WQKDYRRDPK HGVDIPCWFV HDNGAGLIDG VHTDYIVSSL F
//