ID G1KH79_ANOCA Unreviewed; 900 AA.
AC G1KH79;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000007772.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000007772.4, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000007772.4,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000007772.4}
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 AlphaFoldDB; G1KH79; -.
DR STRING; 28377.ENSACAP00000007772; -.
DR Ensembl; ENSACAT00000007938.4; ENSACAP00000007772.4; ENSACAG00000007499.4.
DR eggNOG; ENOG502QPS2; Eukaryota.
DR GeneTree; ENSGT00940000154554; -.
DR HOGENOM; CLU_008101_0_0_1; -.
DR InParanoid; G1KH79; -.
DR TreeFam; TF328982; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000007499; Expressed in liver and 8 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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 900 AA; 101584 MW; 1EC17F9C8408BA96 CRC64;
MGRHLPFYIW LAFIPVLVSS DFLVEQLRNV KKRNTIDGHP KGIEIYWVKI DCSVTSRFSR
NVITSRAVNR ANVSKEAFFD VELPKTAFIT NFTMTIDGVT YPGTIKEKEV AQKQYQKAVS
SGRTAGLVKA SGRKTEKFSV SVNVAAASKI TFELTYEELL KRSFGKYELF IKVNPKQLVN
KFEIEANIFE PQGISDLEVE GTFLNNELLP LVQKSYSGKK AHVLFSPTID QQRTCDNCTT
SLLQGDFLIK YDVNRDIPSN LQIVNGYFVH FFAPKNLAHL PKNVAFVIDV SGSMWGSKIR
QAKEAMIKIV EDLKEDDHFN IILFESEVRK WKDGIIKATP ENVQEAKYFI GNITESGLTN
FNGGLMAGIE MLNNAHKLKI VPERSASLTI MLSDGEANVG ETDQFRIQEN AKNASQGKYP
LYSLGFGYNL DYGFLERLSK VNNGVARRIY DDSDAALQLQ GFYDEVANPL LTDVALEYPE
NVISDVTENN FKHYYDGSEL VVAGRITDND LNSITAEVKA HGALKDLTFT EQADVEETAK
AFEEQKYIFG EYIERLWAYL TIRQLLEKSS IATGYEKGNL TAKALEMSLK YKFVTPLTSM
IVTKPEDDEE PEVVADKPIE GRNFFLFVME KYPITNTPAI QIKSYPAGDL PHFGKIDGDP
HFIIAVPQKE DALCFNINED PGAVLSLISD PVTGIVVNGQ LIGEKKSNND VREQNTYFGK
LGIANIHRNI KIEITTEQII LHNGVKRTAF SWLDEVILQQ PSLTLVIKRK KSMEVSMDNG
AKFVVILHQV WKKHPLHRDF LGFYTLDSHR LSQQTHGLLG QFFRPIDFDI LEVHPGSDPE
KPDATMVVKN NWLTVTRGWQ KDYTEDTRHG LNVPCWFVHN NGEGLIDGVH TDYIVPSIFG
//
