ID A0A401NGS8_SCYTO Unreviewed; 1610 AA.
AC A0A401NGS8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
GN ORFNames=scyTo_0011073 {ECO:0000313|EMBL:GCB60120.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB60120.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB60120.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB60120.1}.
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DR EMBL; BFAA01004914; GCB60120.1; -; Genomic_DNA.
DR STRING; 75743.A0A401NGS8; -.
DR OMA; TEMITIY; -.
DR Proteomes; UP000288216; 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; 2.
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; 2.
DR Pfam; PF08487; VIT; 2.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00609; VIT; 2.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF53300; vWA-like; 2.
DR PROSITE; PS51468; VIT; 2.
DR PROSITE; PS50234; VWFA; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000288216};
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..1610
FT /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019023415"
FT DOMAIN 31..165
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 87..274
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 756..885
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 1011..1194
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 431..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1291..1318
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 433..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1610 AA; 181660 MW; 524B0D05395E8B93 CRC64;
MRPMLVHLLL LSLPTLISAD FIIAESEDHG KRITRGLKYK DREKIEVYSL KIDSKITSRF
AHNVITSRVV NRATQSREAL FEIELPKTAF ITNFTMTIDG VKYSGDVKEK EAARQQYNAA
VSRGQTAGLV NFDSTVEKWR DSLVQATPEN VLQAKRYIIY LQLGAETNIN DSLLLAVSLL
DTAHKQKQLP ERSASMIILL TDGDPNVGEK DPAKIQINVK NAIRARYNLY CLGFGFDVDY
SFLEKMALDN GGVARLIYDD SDAALQLQGF YNEVANPLLL DVELQYQENA ISELTEVNFR
QYYDGSEIVV AGKISNNSLD VFMVEIRART ANTDLSLEGK VNVSEAGNIL QYQQYIFGDF
TERLWAYLTI KQLLKQRISA TGGEMEKLTD RALALSLKYS FVTPLTSMVV TKPEEEKMEV
IILADKPIAK PQTEQSGRHS PRLQGFARSE SSRTLQDSST SQGLSNAREL NPRFSFISSA
ARKIISVDGD PHFIIQLPRQ SDAICFNIGG KPGSIVNLVL DPYTGIKVNG QLIGDKKTEN
NQKLNTYFGK FGLENRKTNM KITVTTEMIT IYYSEENIIL PWSTTATLTY ESFSVSMMQE
KNLTVTMGDG ATFVIVLHRV WKHHPLHRDF LGFYTLDSHR LSNRTHGLLG QFYHDLDYKV
YNIRPGSDPE KTDATMVVKG RNLIVTRGWQ KDYRLDPKQV SNISCFCKMK AMLSFLLLIS
IPALISSDFI ITEAEQHKSD NANTVSNVLK QAGRTLKKRS TEEHGKKRDL EIHAMKIESK
VSSRFAHTVV ISQVLNRANV SKEAFFEIEL PKTAFITNFS MTLDGVTHVG VVKEKEVAQK
QYQQAVSRGQ TAGLVKVSGR KMEKFKVSVN IGPNKKVIFE LTYEELLKRH LGAYEMQIRV
KPQQLVNHFQ IDVHIFEPQG IAFLNVDANF LTNNLTSIVK KTLTGTKAHV SFKPTLEQQR
KCPDCHETIL DGDFIIKYDV NRDLSAGSVQ VVNGYFVHHF APANLARIPK NVIFVIDHSG
SMSGTKMRQT NEALVKILGD MDTKDHFGII IFDDNIDTWK DTIFQATLEN VFEAKKFVKT
ISARGGTNIN DAMVKAVRLL DKAYQDKQLP ERSVSMIILL TDGHPNSGES NPTRIQQNVK
NVADGKYNVY CLGFGYDVNY NFLEIMALEN NGVARRIYED SDAPLQLQGF YDEVANPLLL
DIEFQYPENA ISESTQANFK HLFAGSEIVV AGKIVDNSLD YLRADVIAKT ANENLTLQAE
VKISGAENIT QQQQYIFGDF TERLWAYLTI QQLLEKRISA ETDEKKNLTD RILELSLKYS
FVTPLTSMVV TKPEENKNDT FVADKPSEDE KVARPSFPGH SMVDSDPHFI ISINDRSDAI
CFNIDGKPGA ILNVVTDPST DFVVNGELIG EKKIEKNVKM NTYFGKFGIV NNQMDMKVEV
STKMITVFHG EDKIIFPWSS TASLTKESFS ISIAKEKNLT LTMGDDATFV IVLHRVWKNH
PLHRDFLGFY TLDSHRLSNR THGLLGQFYR EVNAEIYNIR PGLDQGKPDA TMIVKGHKLR
VTRGYQKDYR LDPKRGTNIP CWFVHYNGKG FIDGIPTDYV VTSLFDTLYS
//