ID G3WVD4_SARHA Unreviewed; 557 AA.
AC G3WVD4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Hyaluronan binding protein 2 {ECO:0000313|Ensembl:ENSSHAP00000019389.2};
GN Name=HABP2 {ECO:0000313|Ensembl:ENSSHAP00000019389.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000019389.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000019389.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000019389.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; G3WVD4; -.
DR STRING; 9305.ENSSHAP00000019389; -.
DR Ensembl; ENSSHAT00000019546.2; ENSSHAP00000019389.2; ENSSHAG00000016467.2.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157814; -.
DR HOGENOM; CLU_006842_18_2_1; -.
DR InParanoid; G3WVD4; -.
DR TreeFam; TF329901; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264:SF40; HYALURONAN-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 73..109
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 150..188
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 193..276
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 313..551
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 99..108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 159..176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 178..187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 557 AA; 62460 MW; EAFB81253F269326 CRC64;
MITRASRLRI LPLIILVGHG ALGFFSLTSP LASIDKDWTP YDYEYSAEYY DHEINNISDY
EEYIDWTFIE NDTTDLCQPN PCMHGGDCVI NGDNFKCNCP APFTGGKCQA VRNACRKNPC
VRGECLIIQT PPYYKCACNH PYGNPHCSKV FTACRPNPCK NGGICKRNRR RSKFTCSCPD
GFRGKFCEIG PEDCYEDKGL NYRGKVSKTI NHNTCLHWNS HLLLREAYNV FMEDAELHGI
GEHNYCRNPD GDKSPWCFIQ LDKRTLSWEF CDVTSCSSSD VVESLWKPTE PSASSEMFGT
CGLPEIESKI KRIYGGFKST PGKHPWQASL QAISPLTVSS PNGHLCGGTL IEPCWVLTAA
HCVMLKAKQI RVVLGVQDLL KSESHEQSFR VEKIFVHPDY QEEDDIPYND IALLKLKAVK
GQCAQESKYV KTACLSEVPF PSQTECYISG WGETSTGRGS RYLLDAKVQL ISKSHCNAPN
QYNNLIDETM FCAGGQGIDS CQGDSGGPLT CERDGKYYLY GIVSWGFKCG KKPGVYTLVT
KYHNWIKDTI QEESGSY
//
