ID M3WFU5_FELCA Unreviewed; 556 AA.
AC M3WFU5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Hyaluronan binding protein 2 {ECO:0000313|Ensembl:ENSFCAP00000010975.4};
GN Name=HABP2 {ECO:0000313|Ensembl:ENSFCAP00000010975.4,
GN ECO:0000313|VGNC:VGNC:67531};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000010975.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000010975.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010975.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000010975.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010975.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000010975.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010975.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AANG04000273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006938246.2; XM_006938184.3.
DR AlphaFoldDB; M3WFU5; -.
DR PaxDb; 9685-ENSFCAP00000010975; -.
DR Ensembl; ENSFCAT00000011832.6; ENSFCAP00000010975.4; ENSFCAG00000011829.6.
DR GeneID; 101080665; -.
DR KEGG; fca:101080665; -.
DR CTD; 3026; -.
DR VGNC; VGNC:67531; HABP2.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157814; -.
DR HOGENOM; CLU_006842_18_2_1; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000011712; Chromosome D2.
DR Bgee; ENSFCAG00000011829; Expressed in liver and 4 other cell types or tissues.
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; 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; 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; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
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:UP000011712};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 71..107
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 109..146
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 148..186
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 191..274
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 310..551
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 97..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 113..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 136..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 157..174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 176..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 556 AA; 62039 MW; 39623B678F27923B CRC64;
MLARMCHLHI VLVTALVGKA AIGFSLMSLL VDPDPDWTPD YYESSYEYYN HEENSSDTLA
YQENPNWYYT EEDPCLDHPC KRNGDCLVSG DTFTCSCPAP FSGHRCQNVQ NTCKNKPCGR
GECLITQSPP YYRCVCKHPY SGSDCSTAVP ACRPNPCQNG GICSRHKRRT KFVCTCPEQF
KGKFCEIGPD DCYVGDGYSY RGKVSKTVNQ HSCLYWNSHL LLHENYNMFM EDADTHGIGE
HNFCRNPDGD EKPWCFIKVN NAKVKWEYCD IPACSALDIA DPEGSPTEPL SKLPGFDSCG
KTEMGKVKRI YGGFKSTAGK HPWQASLQTS LPLTASMPQG HFCGGSLIHP CWVLTAAHCT
DIKTKHLKVV LGDQDLKKTE FHEQRFGVEK IFKYSHYNER DEIPHNDIAL LKLKPVDGHC
ALESKYVKTV CLPDGAFPSG TECHISGWGV TETGEGSRQL LDAKVKLIAS TLCNSHRLYD
HMIDNSMICA GNLQKPGKDS CQGDSGGPLT CEKNGTYYVY GIVSWGLECG KKPGVYTLVT
KFLNWIKATI QRETSF
//
