SVH1_CAEEL
ID SVH1_CAEEL Reviewed; 951 AA.
AC Q17800; H1AGA0;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine protease svh-1 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
DE AltName: Full=HGF/MSP/plasminogen-like protein svh-1 {ECO:0000303|PubMed:22388962};
DE AltName: Full=Suppressor of vhp-1 deletion lethality protein svh-1 {ECO:0000312|WormBase:C07G1.1};
DE Flags: Precursor;
GN Name=svh-1 {ECO:0000312|WormBase:C07G1.1};
GN ORFNames=C07G1.1 {ECO:0000312|WormBase:C07G1.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:BAL45941.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF 2-TYR--PHE-17 AND HIS-755.
RX PubMed=22388962; DOI=10.1038/nn.3052;
RA Li C., Hisamoto N., Nix P., Kanao S., Mizuno T., Bastiani M., Matsumoto K.;
RT "The growth factor SVH-1 regulates axon regeneration in C. elegans via the
RT JNK MAPK cascade.";
RL Nat. Neurosci. 15:551-557(2012).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, DOMAIN, ACTIVE SITE, AND MUTAGENESIS OF 2-TYR--PHE-17 AND
RP HIS-755.
RX PubMed=25464847; DOI=10.1016/j.celrep.2014.10.056;
RA Hisamoto N., Li C., Yoshida M., Matsumoto K.;
RT "The C. elegans HGF/plasminogen-like protein SVH-1 has protease-dependent
RT and -independent functions.";
RL Cell Rep. 9:1628-1634(2014).
CC -!- FUNCTION: Serine protease which ensures proper pharyngeal pumping
CC during larval growth by regulating the levels of extracellular matrix
CC component fbl-1 (PubMed:25464847). Independently of its enzymatic
CC activity and probably by acting as a ligand for tyrosine-protein kinase
CC receptor svh-2, involved in axon regeneration after injury by promoting
CC the generation of productive and stable growth cones (PubMed:22388962,
CC PubMed:25464847). May play a role in gonad development
CC (PubMed:25464847). {ECO:0000269|PubMed:22388962,
CC ECO:0000269|PubMed:25464847}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22388962}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in ADL sensory neurons.
CC {ECO:0000269|PubMed:22388962}.
CC -!- DOMAIN: The Kringle domain is dispensable for larval growth and axon
CC regeneration after injury. {ECO:0000269|PubMed:25464847}.
CC -!- DOMAIN: The PAN domain is required to maintain gonad structure and thus
CC fertility. Dispensable for larval growth.
CC {ECO:0000269|PubMed:25464847}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB693146; BAL45941.1; -; mRNA.
DR EMBL; BX284604; CCD61391.2; -; Genomic_DNA.
DR PIR; T15451; T15451.
DR RefSeq; NP_501379.2; NM_068978.3.
DR AlphaFoldDB; Q17800; -.
DR SMR; Q17800; -.
DR STRING; 6239.C07G1.1; -.
DR MEROPS; S01.B69; -.
DR PaxDb; Q17800; -.
DR EnsemblMetazoa; C07G1.1.1; C07G1.1.1; WBGene00006620.
DR GeneID; 182375; -.
DR KEGG; cel:CELE_C07G1.1; -.
DR UCSC; C07G1.1; c. elegans.
DR CTD; 182375; -.
DR WormBase; C07G1.1; CE47478; WBGene00006620; svh-1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000172378; -.
DR HOGENOM; CLU_315286_0_0_1; -.
DR InParanoid; Q17800; -.
DR OMA; FQCDYEV; -.
DR OrthoDB; 158600at2759; -.
DR PhylomeDB; Q17800; -.
DR PRO; PR:Q17800; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006620; Expressed in larva and 2 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:WormBase.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0031103; P:axon regeneration; IMP:UniProtKB.
DR GO; GO:0002164; P:larval development; IMP:UniProtKB.
DR GO; GO:1905941; P:positive regulation of gonad development; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:WormBase.
DR GO; GO:1903746; P:positive regulation of pharyngeal pumping; IMP:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00108; KR; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 4.10.400.10; -; 2.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00130; KR; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 2.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50287; SRCR_2; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Kringle; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..951
FT /note="Serine protease svh-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448587"
FT DOMAIN 234..304
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 319..356
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 355..435
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 433..585
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 557..594
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 598..694
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 713..947
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 490..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 755
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:25464847"
FT ACT_SITE 803
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 898
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 320..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 327..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 340..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 387..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 391..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 461..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 474..584
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 545..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 558..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 566..584
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 578..593
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 622..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 635..693
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 661..673
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 740..756
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 838..904
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 867..883
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 894..923
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MUTAGEN 2..17
FT /note="Missing: Probably prevents secretion. Impaired axon
FT regeneration following injury. Impaired larval growth."
FT /evidence="ECO:0000269|PubMed:22388962,
FT ECO:0000269|PubMed:25464847"
FT MUTAGEN 755
FT /note="H->A: In h755a: Impaired larval growth. No defect in
FT axon regeneration following injury."
FT /evidence="ECO:0000269|PubMed:22388962,
FT ECO:0000269|PubMed:25464847"
SQ SEQUENCE 951 AA; 105383 MW; 3DA09F6600B7AC45 CRC64;
MYIVIVTMRT ILFFGIFFIF IFQCAKCIEL KIFEDLLEVR SQSGLFFPLC SKSFHQKYGE
QACASISSTF LSYSTVSLQQ YTYSVGCTTS VCFTFLSSFC KTGVKVFCSP SLCASGTLQI
GSKCLSISTV PVQGYSEANY YCNPATLISS LKPTEIESIR DTILPTFADT RLFLTSGLRQ
GATWKWGNGD TVEQEVTGTG RCLALQAGNL VAIDCDSEAY VFCESGRECI ARDKEYSGTA
NRTSDGKMCL MWNDPTVLFR RERDLEILNH NFCRFVNDAD GKKSATPVCY TKPNELSQCY
IPPCPESFND VVPIESGDSC PIGSISCDNG SKCISEKFQC DYEVDCNDGS DEHNCEDYLQ
YYELIGAYRL ADNIIEVWTF IPHVQGCARK CRESLLMCEA FSYEPKSQTC LLTDTSQTFS
SLARKITSLY YRRRFSTKDV EFQVENKVLY ATKSAKKGHV CDDNYSREKL SSICRVLGFG
DPIYTVESHQ SESSLGPLQP TTLHPTNPSF DSPSSVSQMR RTSPSATLAP RLPAWNLSCL
REPNCTSTVI STCEPIRCSH CQQAACGDGS CIRFDQLCNG QIDCQSGEDE DYCRANSFRL
TNGSDTSGYL EVLFRSRWEP ICADHLNGKI SNSICDAMRL GEHGFILSTN ATISSGYNVN
CDVDCSIRRS SSCTRHARIS CISQNGMSSA SQCGLRYVEV NARDAAKSRI ARVVGGFETV
PGAFPWTAAL RNKATKAHHC GASILDKTHL ITAAHCFEED ERVSSYEVVV GDWDNNQTDG
NEQIFYLQRI HFYPLYKDIF SHDIAILEIP YPGIEFNEYA QPICLPSKDF VYTPGRQCVV
SGWGSMGLRY AERLQAALIP IINRFDCVNS SQIYSSMSRS AFCAGYLEGG IDSCQGDSGG
PFACRREDGA FVLAGVISWG DGCAQKKQPG IYTMVAPYLS WISAIINGQP V
