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Database: UniProt
Entry: K7FNL1_PELSI
LinkDB: K7FNL1_PELSI
Original site: K7FNL1_PELSI 
ID   K7FNL1_PELSI            Unreviewed;       899 AA.
AC   K7FNL1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000009621.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000009621.1}
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   -!- 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; AGCU01116377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01116378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01116379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K7FNL1; -.
DR   STRING; 13735.ENSPSIP00000009621; -.
DR   Ensembl; ENSPSIT00000009668.1; ENSPSIP00000009621.1; ENSPSIG00000008164.1.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   GeneTree; ENSGT00940000154554; -.
DR   OMA; FNVIRFD; -.
DR   TreeFam; TF328982; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
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:UP000007267};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..899
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003901979"
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"
FT   REGION          605..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  100680 MW;  071761E06E2B45F3 CRC64;
     MANHLLFYIL LALIPALGTS DFLITQFRNI KKRSADDLIV NGIEIYSMKI DSKVTSRFAH
     NVITSRAVNR ANVSKEVVFD VDLPKTAFIT NFSMIIDGVT YPGTIKEKEV AKKQYEKAVS
     RGQTAGLVKA SGRKTEKFTV SVNIAAASKV TFELVYEELL KRNFGKYEMF IKVKPKQLVK
     NFEIEVNIFE PQGISELDAQ GSFVTNDLSQ VLTKSFSGKK GHVSFKPTLD QQRTCATCST
     SLLDGDFIIK YDVKRDSPGD LQIVNGYFVH FFAPTNLPRF PKNVIFVIDI SGSMDGIGIQ
     QTRQALLKIL EDIKEEDYFN FILFGTDVHV WKDKLVQATP ENLKEAKEFA QAISTRGMTN
     LHGGLMKGIE MLNTAYETNS VPKRSASIII MLTDGQPNQG VSDPQQIQAN VKTAIQGKYP
     LYNLAFGYGI DYNFLEKMAL ENKGVARRIY PDSDSAIQME GFYDEVANPM LTEVELNYPE
     NAIADLTQNN FKHYYDGSEI VVAGRITDND LNSLTADVKA QGALNDVTYI EQADVNEMAK
     ALQEQEYIFG DYIERLWAYL TIQQLLEKRT VAQGEEKDNL TAEALELSLK YKFVTPLTSM
     VVTKPEDNED QSAIADKPVE GKAKAAPGTY SAPTHSFLYS RPASPSVYTS VDGDPHFIIS
     VPQKEDAICF NINEETGTVL SLIKDPVTGI TVNGQLIGDK RVNNDAKIQN TYFGKLGIEN
     KKLELKLEVT PEKIIIQNGR KKTVFSWLDT VTLRQESLTL IINRKKNLVL SMGDGASFVI
     VLHQVWEKHP LHQNFLGLYT LDSHKLSEHT HGLLGQFFHH IDFDILEIHP GADSKKPDAT
     MMVKNNKLTV TRGWQKDFRK DSQHGVDIPC WFVHNNGAGL IDGVHTNYIV SSIFDTTIN
//
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