ID H2N9Q3_PONAB Unreviewed; 946 AA.
AC H2N9Q3; A0A2J8VK78;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=ITIH2 isoform 1 {ECO:0000313|EMBL:PNJ57914.1};
DE SubName: Full=Inter-alpha-trypsin inhibitor heavy chain 2 {ECO:0000313|Ensembl:ENSPPYP00000002402.3};
GN Name=ITIH2 {ECO:0000313|Ensembl:ENSPPYP00000002402.3};
GN ORFNames=CR201_G0018235 {ECO:0000313|EMBL:PNJ57914.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000002402.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000002402.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ57914.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ57914.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000002402.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; NDHI03003418; PNJ57914.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000003279; -.
DR Ensembl; ENSPPYT00000002475.3; ENSPPYP00000002402.3; ENSPPYG00000002074.3.
DR eggNOG; ENOG502QPS2; Eukaryota.
DR GeneTree; ENSGT00940000157945; -.
DR HOGENOM; CLU_008101_0_0_1; -.
DR OMA; AKQMWAY; -.
DR OrthoDB; 608326at2759; -.
DR TreeFam; TF328982; -.
DR Proteomes; UP000001595; Chromosome 10.
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:SF14; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H2; 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 Reference proteome {ECO:0000313|Proteomes:UP000001595};
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..946
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041158021"
FT DOMAIN 56..185
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 310..493
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
SQ SEQUENCE 946 AA; 106422 MW; BC5E666E878F5236 CRC64;
MKRLTCFFIC FFLSEVSGFE IPINGLSEFV DYEDLVELAP GKFQLVAENR RYQRSLPGES
EEMTEEADQV TLYSYKVQST ITSRMATTMI QSKVVNNSPQ PQNVVFDVQI PKGAFISNFS
MTVDGKTFRS SIKEKTVGRA LYAQARAKGK TAGLVRSRGL DMENFRTEVN VLPGAKAQFE
LHYQEVKWRK LGSYEHRIYL QPGRLAKHLE VDVWVIEPQG LRFLHVPDTF EGHFDGVPVI
SKGQQKAHVS FKPTVAQQRI CPSCRETAVD GELVVLYDVK REEKAGELEV FNGYFVHFFA
PDNLDPIPKN ILFVIDVSGS MWGVKMKQTV EAMKTILDDL RAEDHFSVID FNQNVRTWRN
DLISATKTQV ADAKRYIEKI QPSGGTNINE ALLRAIFILN EASNLGLLDP NSVSLIILVS
DGDPTVGELK LSKIQKNVKE NIQDNISLFS LGMGFDVDYD FLKRLSSENR GIAQRIYGNQ
DTSSQLKKFY NQVSTPLLRN VQFNYPHTSV TDITQNNFHN YFGGSEIVVA GKFDPAKLDQ
IESVITATSA NTQLVLETLA QMDDLQDFLS KDKHADPDFT RKLWAYLTIN QLLAERSLAP
TAATKRRITR SILQMSLDHH IVTPLTSLVI ENEAGDERML ADAPPQDPSC CSGALYYGSK
VAPDSTPSWA NPSPTPVISM LAQGSQVLES TPPPHVMRVE NDPHFIIYLP KSQKNICFNI
DSEPGKILNL VSDPESGIVV NGQLVGAKKP NNGKLSTYFG KLGFYFQSED IKIEISTETI
TLSRGSSTFA LSWSDTAQVM NQRVQISVKK EKVVTITLDK EMSFSVLLHR VWKKHPVNVD
FLGIYIPPTN KFSPKAHGLI GQFMQEPKIH IFNERPGKNP EKPEASMEVK GQKLIVTRGL
QKDYRTDLVF GTDVTCWFVH NSGKGFIDGH YKDYFMPQLY SFLKRP
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