ID H3CM48_TETNG Unreviewed; 715 AA.
AC H3CM48;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Macrophage stimulating 1 {ECO:0000313|Ensembl:ENSTNIP00000009328.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000009328.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000009328.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000256|PIRNR:PIRNR001152}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR AlphaFoldDB; H3CM48; -.
DR STRING; 99883.ENSTNIP00000009328; -.
DR Ensembl; ENSTNIT00000009499.1; ENSTNIP00000009328.1; ENSTNIG00000014761.1.
DR GeneTree; ENSGT00940000159461; -.
DR InParanoid; H3CM48; -.
DR OMA; YQIPRCT; -.
DR TreeFam; TF329901; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00108; KR; 4.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR024174; HGF/MST1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24261:SF12; HEPATOCYTE GROWTH FACTOR-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF00051; Kringle; 4.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001152; HGF_MST1; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 4.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00021; KRINGLE_1; 3.
DR PROSITE; PS50070; KRINGLE_2; 4.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152}.
FT DOMAIN 18..102
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 106..183
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 187..265
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 289..368
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 376..454
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 488..713
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 188..265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 209..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 237..260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 311..350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 339..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 377..454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 398..437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 715 AA; 81725 MW; 5BC21B68AFACCA77 CRC64;
LPFLLLTLRL SSETGYHSPL NDFQRSEGRE LVPTSWNSAR VTLLSGLNLE ECAQRCAQSL
DCRAFNYETR PVVTCKHLPW VGDGSNAEVK RNVNCDLYEK KVYVRKCIVG KGEDYRGKVF
TTRSGLTCQQ WWSKFPHDHR WTPTNTNGLE LNYCRNPDGD RIGPWCYTTD PERRYESCNI
PQCKDEVCIT CNGEEYRGQV DHTVSNRECQ RWDQQHPHQH IYQPEKYPDK SLDDNYCRNP
DASPVPWCYT TDPEVERENC EIRKCKSPDL ICQCRGAGGE APASSFTTHC FRGRGEDYRG
KVNETPSGIP CQRWDAQSPH EHPFYPNTYE CKGLEENYCR NPDGSEAPWC FTSVPEMRTA
LCLQIKRCAD DIEAEDCYQE NGKNYRGTVR KTRKGITCQK WNNTPHRTKI NPRTHPEANL
TENYCRNPDG DQHGPWCYTT DPKTEFDYCA IKQCAQLGEV PINEPVEKVE FNKCGKREDR
FQPTRLRIVN GIPGNSPWTV SLRDRKGNHF CGGSMVDSRW VISTKQCFSS CYVDLPGYSA
MMGTLFRDPK EGEPGVQTIP LTKIVCGPSE SQLVMLQLEY PAQFNERVSQ ICLPPERYIV
PEDTTCEIAG WGETRGTGDE TVLNVAHVPV LSNKACNTYF RGRVRENEMC TQSFQGGVGA
CERDYGGPLA CQNRDCWVLE GVIIPMRRCG HPGQPNIFIR VSTYVDWIKK VMEMA
//
