ID   G3TD90_LOXAF            Unreviewed;       946 AA.
AC   G3TD90;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Inter-alpha-trypsin inhibitor heavy chain 2 {ECO:0000313|Ensembl:ENSLAFP00000012097.3};
GN   Name=ITIH2 {ECO:0000313|Ensembl:ENSLAFP00000012097.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000012097.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000012097.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012097.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000012097.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012097.3};
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   AlphaFoldDB; G3TD90; -.
DR   STRING; 9785.ENSLAFP00000012097; -.
DR   Ensembl; ENSLAFT00000014441.3; ENSLAFP00000012097.3; ENSLAFG00000014439.3.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   GeneTree; ENSGT00940000157945; -.
DR   HOGENOM; CLU_008101_0_1_1; -.
DR   InParanoid; G3TD90; -.
DR   OMA; AKQMWAY; -.
DR   TreeFam; TF328982; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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:UP000007646};
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_5003454914"
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;  106252 MW;  6136BDC08159AF3C CRC64;
     MKRLMCFLLW LFLSEAQGLE IPTNGLPEFA EYGDLVELAP GKFQFVPENR RYQRSVPGES
     GEETKDDDQV TLYSYKVQST ITSRMANTII QSKVVNNSPL PQDVVFDVQI PKGAFITNFT
     MTVDGTRFTS SIKEKTVGRA LYSQARAKGK AAALVRSKAL DMENFKTEVN ILPGSKVQFE
     LHYQEVKWRK LGSYEHRIHL QPGRLAKHLE VDIWVIEPQG LRFLHVPDTF EGHFEGVPVI
     SKGNQKAHVS FRPTVPQQRK CSNCSETAVD GELVVVYDVN REEKAGELEV FNGYFVQFFA
     PDNLEPIPKN ILFVIDVSGS MWGIKMKQTV EAMKTILDDL RAEDQFSVVD FNHNVRTWRN
     DLVSATKTQV TDAKKYIEKI QPNGGTNINE ALLRAIFILN EADNLGLLDP NSVSLIILVS
     DGDPTVGELK LSKIQKNVKQ NIRDNISLFS LGIGFDVDYD FLKRLSNDNR GIAQRIYGNQ
     DTSSQLRKFY NQVSTPLLRN IQFNYPDTAV TDVTQNSFHN YFGGSEIVVA GKADPTKLEQ
     IQSIITATSA STDLVLEKAA ETGGLEDFLS KDKHADPDFT KKLWAYLTIN QLLAERSLAP
     TAAAKKEITK TILEMSLEHH IVTPFTAMVI ENDAGDERML ADSPQHDHSC CSGALYYGSK
     TAASSIPPWA SASPTPEIPL HARGAPVLET TPLHVIRVEN DPHFIIYLPK SQKNICFNID
     SEPGKILSLV SDPESVGILV NGQLIGAKKP KNNKLNTYFG KLGFYFQSED MKIEISTENI
     TLTRGSHVSI LSWADTVHVI NQRVLVSVRK EKTVTITLDK EMSFSVLLHR VWKKHPINVD
     FLGIYIPPTN KFSPNAHGLI GQFMHEPEIH IFNERPGKNP KKPEASMEVK GQKLTVTRGL
     QKDYRTDTVF GTDVPCWFVH NSGKGFIDGH YKDYLVPQLY SYLKWP
//