ID A0A151MD85_ALLMI Unreviewed; 936 AA.
AC A0A151MD85;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Suppressor of tumorigenicity 14 protein-like {ECO:0000313|EMBL:KYO22478.1};
GN Name=TMPRSS7 {ECO:0000313|EMBL:KYO22478.1};
GN ORFNames=Y1Q_0003045 {ECO:0000313|EMBL:KYO22478.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO22478.1};
RN [1] {ECO:0000313|EMBL:KYO22478.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO22478.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO22478.1}.
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DR EMBL; AKHW03006231; KYO22478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151MD85; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.30.70.960; SEA domain; 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; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50024; SEA; 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:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..863
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..207
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 343..452
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 552..786
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 803..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 464..482
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 476..491
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 505..517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 525..540
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 936 AA; 104989 MW; F56BE8CADE5B9EDA CRC64;
MIQSVASKRV SVVYSIPSPD DCECVSGQSP NLYWVQSSEE ESSFLKYSFL KRLRWHLGIL
PIISLAVTVF VLVLHYSLSP AFSFIYIGGS VEIPNLTYTS DLTDPKSQKF ILQAEMIQSY
FAEFYESSTL GKYYLNSVVA AFSEGEDGLK VYCWSIFWAP QDITGSFKKL ISLKQKEIIR
KQVPWDVNSS AESFLVEENF DLFTMDLFVT DATEYDVTLK SVSFDLYAKP GNNRSLTLVN
PKKSFYQWRL RVPSNYVVRL VILTLHGVTP GSCASHRLSA YDFLLPLQNK IITRWCGVPG
AWNPPIVRLT SSSNVMLVTF SLDKRKENSI LKAYFQAVPK IVCGGRYISW NGTVSSPYYP
SYYPPSIDCS WIIRAPLPGY KLSLKILVIQ IQEKTPGSSK CDKDWLEIDG VRYCKAIAEG
QRNKDYGYSV AISFHSDELV THRGFYIEYK AFSYMDLCPR QFKCTDGTCI PLNNQCDGRQ
DCSDGSNELD CGCSPEESNC ASKNCSPYAY KCSNGKCSMK PNPECDGIRD CADGSDEVNC
ACGKSQFKKN RIVGGEDARS GKWPWQASLQ MGTYGHICGA SVISNRWLIS AAHCFLDSDS
IRYSVPSGWK AYMGIRIMSK NSNHVAMRSI KRIVVHPRYD QYISDYDVAL LEMETPVFFS
ELVQPICLPS SPRIFFYGTV CYVTGWGAIK ENSQLAKTLQ EARVKIINRS VCSKLYDDLI
TSRMLCAGNL NGGIDACQGD SGGPLACIGK ENRWYLAGIQ EVSFFSGLAL KSVSHRDMET
VNGHVPEQGY QVIELQEARE ELNEDEDEAK SKDPLKPEES TKSKERIWRP CSKVVFWKCK
LWMLILAVFL VILLLITLSL ILYSEVYIDE DEYWDPDLVS SGNHHNFSGT LKVQCSAGTA
YSEDLTKKGG QNVALGPDVA CQTILSSPGP LKNLEN
//
