ID H0UTK8_CAVPO Unreviewed; 906 AA.
AC H0UTK8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H1 {ECO:0000256|ARBA:ARBA00039925};
GN Name=ITIH1 {ECO:0000313|Ensembl:ENSCPOP00000000250.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000000250.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000000250.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000000250.3};
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; AAKN02001397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0UTK8; -.
DR STRING; 10141.ENSCPOP00000000250; -.
DR Ensembl; ENSCPOT00000000288.3; ENSCPOP00000000250.3; ENSCPOG00000000285.4.
DR VEuPathDB; HostDB:ENSCPOG00000000285; -.
DR eggNOG; ENOG502RXR2; Eukaryota.
DR GeneTree; ENSGT00940000162180; -.
DR HOGENOM; CLU_008101_0_0_1; -.
DR InParanoid; H0UTK8; -.
DR OMA; QEFRTTC; -.
DR TreeFam; TF328982; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000000285; Expressed in liver and 2 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:Ensembl.
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:SF106; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H1; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..906
FT /note="Inter-alpha-trypsin inhibitor heavy chain H1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012406935"
FT DOMAIN 36..165
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 291..474
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
SQ SEQUENCE 906 AA; 101202 MW; 3730DD93B7A3F8C0 CRC64;
MDGAMGLQTL LCVYLVSLLT LQAMPVLGLA TGRSKSSEKR QAVDTIVNGV FIRSLKVNCK
VTSRFAHYVI TSQVENSADT AREVAFEVEI PKTAFISDFA ITANRNTFIG DIKDKVTAWK
QYRKAAISGE NAGLVRASGR NMEQFTIHIT VGPQSKAIFR LTYEEVLKRK LTQYNIIIKV
KPKQLVHHFE IDVDIFEPQG ISKLDAQASF LTKELAAQTI KKSFSGKKGH VLFRPTVSQQ
QSCPTCSTSL LNGDFTVTYD VNRNKLCDLL VANNYFAHFF APQNLTNMRK NLVFVIDISG
SMEGQKVKQT KEALLKILQD MRPEDYFDLV LFGSNVQSWK GSLVQASKAN LQAAGDFVRR
FSLHGATNLN GGLLRGIEIL NKAQERLPEL NKHASIVIML TDGEPTEGVT DRAQIQKNIR
NAIQGRFPLY NLGFGNDVDF TFLEVMSMEN NGWAQRIYED HDAAQQLQGF YNQVSSPLLV
DVDMQYPPDA VSALTQHRHK QYYDGSEIVV AGRIADNKLG VFKADVKAQG EGQEFRTTCL
VDEEEMKKLL QERGHLLENH VERLWAYLTI QQLLAKRMKA EGEEKANLSA QVLKMSLDYQ
FVTPLTSMTI RGMEDEDGLE PTIDKSPEGM TTKGLQTFVL SALQPAPTQP SSSFQQLPNR
VTGVDTDPHF IIHVPQKEDT LCFNINEEPG VILSLVQDPD TGFSVNGQLI GSKARSPGKH
EGTYFGRLGI TNPATDFQLE VTPQNITLSP GSGGLMFSWR DQAVLRQDGM VVTINKKRNL
VLSMDGKATF EVVLHRVWRG SAVHQDFLGF YVLDGRWMSP RTHGLLGQFL HPFDFEVLDL
RPGSDPTKPD ATLVVKNRRL TVTRGLQKDY SKDPRHGAEV SCWFVHNNGA GLIHGIHTDY
IVPDIF
//
