ID F7DHC5_MONDO Unreviewed; 728 AA.
AC F7DHC5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Mannan binding lectin serine peptidase 1 {ECO:0000313|Ensembl:ENSMODP00000010610.4};
GN Name=MASP1 {ECO:0000313|Ensembl:ENSMODP00000010610.4};
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000010610.4, ECO:0000313|Proteomes:UP000002280};
RN [1] {ECO:0000313|Ensembl:ENSMODP00000010610.4, ECO:0000313|Proteomes:UP000002280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17495919; DOI=10.1038/nature05805;
RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT coding sequences.";
RL Nature 447:167-177(2007).
RN [2] {ECO:0000313|Ensembl:ENSMODP00000010610.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000256|PIRSR:PIRSR001155-3}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR AlphaFoldDB; F7DHC5; -.
DR STRING; 13616.ENSMODP00000010610; -.
DR MEROPS; S01.132; -.
DR Ensembl; ENSMODT00000010817.4; ENSMODP00000010610.4; ENSMODG00000008535.4.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00950000183084; -.
DR HOGENOM; CLU_006842_14_1_1; -.
DR InParanoid; F7DHC5; -.
DR OMA; QHWVAQG; -.
DR TreeFam; TF330373; -.
DR Proteomes; UP000002280; Chromosome 7.
DR Bgee; ENSMODG00000008535; Expressed in liver and 16 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF13; MANNAN-BINDING LECTIN SERINE PROTEASE 1; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001155; C1r_C1s_MASP; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR001155-4};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001155-2};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278,
KW ECO:0000256|PIRSR:PIRSR001155-3}; Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001155-4};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..728
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023945374"
FT DOMAIN 8..136
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 183..295
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 297..362
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 363..432
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 448..714
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 551
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 662
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT MOD_RES 157
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT DISULFID 73..89
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 141..155
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 151..164
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 166..179
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 183..210
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 240..258
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 299..347
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 327..360
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 365..412
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 395..430
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 434..571
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 628..647
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 658..690
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
SQ SEQUENCE 728 AA; 80934 MW; 996CE104A51A8036 CRC64;
FRAFLLCCSL YVSLLRTSAN MVELNDMFGE IQSPNFPDSY PSDSEVTWNI TVPEGFRIKL
YFMHFDLESS YLCEYDYVEA EDQVLALFCG RETTDTEQAP GQQAVLSPGP FMALTFRSDF
SNEERFTGFD AHYMAVDVDE CTEKSDEELA CDHYCHNYIG GYYCSCRIGY ILHTDNRTCR
VECSDNLFTQ RTGVITSPDF PGPYPKSSDC LYRIELEDGF LITLQFEDSF DVEDHPEVSC
PYDYIKIKAG QKEFGPYCGE KSPARIVTQS NSVQILFHSD NSGENGGWRL SYSSSGNPCP
ALQPPIRGKI DPAQAQYTFR DQVLISCAAG YKVVKDNLEL DTFQIECLKD GTWSNRVPAC
KIVDCGTPKE LEHGQVTFAT KSNLTLYKSE VHYSCQQPYY QLFPNITGTY ACEAQGTWMN
GELGEKLPTC LPVCGQPSHS LPALVKRIIG GRNAEPGFFP WQALIVVEDT SRVPNDKWFG
SGALLSESWV LTAAHVLRSQ RRDNTVIPVS REHVTVYLGL HDVRDKSGAV NRTAARVILH
PDFDIQNYNH DIALVQLKEP VPLGPHVLPV CLPAPEPEGP LPNTLGLVAG WGISNPNVTV
DEIIGGGMRT LSDVLQYVKL PVVLHAECKA SYESRSGNYS VTENMFCAGY YEGGKDTCLG
DSGGAFVIQD APSRRWVAQG LVSWGGPEEC GSKQVYGVYT KVSNYVRWLW SQLGSPGGRG
EVEAEAER
//
