ID A0A444UJX6_ACIRT Unreviewed; 2708 AA.
AC A0A444UJX6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Secretory phospholipase A2 receptor {ECO:0000313|EMBL:RXM35471.1};
GN ORFNames=EOD39_12902 {ECO:0000313|EMBL:RXM35471.1};
OS Acipenser ruthenus (Sterlet sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7906 {ECO:0000313|EMBL:RXM35471.1, ECO:0000313|Proteomes:UP000289886};
RN [1] {ECO:0000313|EMBL:RXM35471.1, ECO:0000313|Proteomes:UP000289886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WHYD16114868_AA {ECO:0000313|EMBL:RXM35471.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RXM35471.1};
RA Wei Q.;
RT "Draft Genome and Complete Hox-Cluster Characterization of the Sterlet
RT Sturgeon (Acipenser ruthenus).";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449}.
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:RXM35471.1}.
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DR EMBL; SCEB01214413; RXM35471.1; -; Genomic_DNA.
DR Proteomes; UP000289886; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 8.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR CDD; cd12474; RRM2_MSSP2; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1240.30; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 8.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR22803:SF65; LYMPHOCYTE ANTIGEN 75; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00034; CLECT; 9.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00458; RICIN; 2.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 10.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:RXM35471.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000289886};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 162..247
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 1223..1271
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 1238..1310
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1339..1456
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1480..1593
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1636..1756
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1779..1898
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1924..2050
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2084..2189
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2219..2281
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2426..2528
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2550..2633
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 94..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1228..1254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 1242..1269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2708 AA; 306842 MW; 0A1ADEDD9FD1A3F8 CRC64;
MSKSFCGISD SNNTVPITSA STEICLICSI NCHLDTCAVL LGKNPWFPVT FISPTGKAYI
SVFMGKVWKQ QMYPQYTYYY PQYLQAKQPF ALNPHPMAPP SPSTNSSTNH SSSSSNAGWD
QLSKTNLYIR GLPPATTDHD LVKLCQPNLS FCVRKQQEQD PTNLYISNLP LSMDEQELES
MLKPFGQVIS TRILRDSNGA SRGVGFARME STEKCEAVIS HFNGKFIKTP PGILVPNEPL
LCKFADGGQK KRQNQNKYVQ NGRAWPREGE AGMTLTYDPT TAAMQNGFYP SPYSIANRMI
AQTSITPYIS PVSTYQGYFN CLAPKDHSPY LSLNLIKLDV LQVQTPSWMT HQPYIMQHPG
AVLSPSMDHT MSLQPASMLN PLTQQMSHLS LGNTGTFMPA TTAMQGAYIP QYAHMQTAAV
QVENFTDSLS NSKRCDNLTN LLMKGCPEDL IEFPVTKVVI QKNEFLGGGG GQKNNRNVTQ
IAPQKITLKL RPANEVTFQV DVQQAEDYPV DVYYLMDLSA SMVDDLEMIK ELGTTLSKEM
AKLTSKFRLG FGSFVEKPVL PFIRKTPEEL KNPCKGVDQF CLPTFGYKHV LPLTDSAERF
NEIITDQQVS ANIDIPECGF DAVMQAAVCG DKIGWRNDSM HLLVFVSDAD SHFGMDSKMS
GIVIPNDGQC HLDSNNEYSK STVLEYPTLG QLIDKLVENN ILLIFAVTED QRNNYENYAK
LIPGATVGIL QSDSRNILQL IMTAYKELRS EIELEVEGDT EDIQISFTAI CHDGTVLPGQ
KKCSHLQVGD TVSFNVTVGL TDCLKKPKHF TIKPVGFQDV LKVEIEAMCS CVCHHEAELN
SSRCSAGKGT FQCGMCVCNP GHMGPHCHGN CDCGECVCHS GWIGEYCNCT TSTDACVSDD
GVLCNGRGEC VCGKCVCTNP GASGSNCERC PTCGDACSSK RSCVECHLYA KEQSPEECYE
KCKAIHTTVI DTEDFKDNRS IPCTLQSDNE CIISFHMSVD EYRLTYVYNL KQADCPKPPN
IPLIIWGVSM SVLTIGIILL IIWKLFVSVH DRKEVAKFEA ERANAKWQTG CQINFAMSHQ
ILDLTTKGVF ILESEHLNRC IRADKTKLTL ENCDQPSKHM LWKWVSRHRL FNIGSSMCLG
LNTTSLQQPL NMFKCDSTLK TLWWRCSGNT LFGAAQLKLT GKGRLVVATK QRVSSQRWKI
YLTSGEGPCA HPYEEIHTVQ GNAHGMPCVL PFKYNNKWYS ECTTEGREDN YRWCATTSLY
DQDEKWGFCP NPGLSPMSAL ASTHCGVFNS AVGNEWQNLD CGSGLPFICK KYPNFTRRAE
PFDTWQYYPT VCSPGWFPHN KFCYKLQSQE QSWKDSLTVC RSSNADLISV HSLADVELLL
TLFQNVSETV SGAWIGLSNK TQGSFEWSDG SPVTFTYWHK YEPNVTYVEG PLCVRVTTDS
TWQVKTCDER LPSVCKKPGN LEEQKSGLGD KGCSEGWKRR GHFCYKVTGH LQNYEDATKS
YYCNSPMVTV GNRFEQAFIN SLIQNVTNGS SLYFWTALQD RNKTGEYSWL TQKGSFQHVR
YTNWNKYQPA SSGGCVAISG GKYLGRWEVK DCNTFRAMSI CKQAISSYKE TESSDITINQ
QASCAPGWES KPDLLYCYKV FHREKVLMKR SWEDADFFCQ ALGSNLVSFS HYEEENFLNG
ILQNMFNSEE RLFWAGFNKR NPLSGAAWEW SDGTAVVSSF IEDRNNEDDQ RNCAAYKAGN
MIIPLRCDAK LEWICKMPKG AKLKGLYWYT EQNEPWVFYQ KSEYLFHNIS FPWNAVAFAC
KMLGADLVSI HSSDQLDFIQ SKIEKLFQNE VKWWIGLFAE YSNTELRWID GSAVDYENWE
GTNSRRSEVK NERCVYMSSQ TGRWSEGKCN GHHPYICERK TVSVVEIPRE PHLIGGCPER
WLYFGHKCFL MHVPNNPQDL KNWNDAQAFC KSHEGSLVSV ENEIEQAYLT MLLLGSQTSV
WIGLQNDNRQ KWVNGKPVTY ANWSPIEPEN SFSDGDDLNA SNAQQDDPLC TLLSNNHNYH
LTGKWYNEKC LDNGYGFICQ KQQDPSKPPS HQSFFHPLPN TIEYGNRSYR IIHGNMTWYE
ALNKCLENET ELVSITDEFH QAFLTVVVNR LDHAHWIGLY SQDQDGINYQ WSDGSDAFFT
HWDDADEVHL LGDCVYMDIN GNWKSADCET PLQGAVCHVP PESKPISYKG ECPKTWLKFQ
SSCYSFEPVI RRLDLEESRE YCKQKANMSD VLTIKDEEEH RFVLEELQSF GPSHQTIWLG
IIFDTDRHAS FTIHHNHKDS CLEVKDSQLS VVQCKNSPSM QWKWGTRHRL YNIQSMQCLG
LDLSENAVGM FECDTAHVML WWRCAQNFLF GASQYRLSAT SGSVTASLNS NDTWTKENFA
DSICHQPYED SWKYKITRCE SDWLPYNGYC YMMGKEPDTQ EMAVKTCEGK GGVLISIHSL
EDIELIITKL HNNTEIDVWT GLINNQSPAL FEWTDGTPVT FTYWSQHEPS VPFNKTPNCV
AYTGQDWKRH GDSCYKVDKN EVFFQESFNL SITNRFEQAF INSLITKYSK DDTKYFWTSL
QDKNGNGQYE WITTEGMQPV TFTNWNIYQP DGLGGCVVMS AGKSLGKWEV KDCTNFKAMA
IYKKVIGNRK NPEPEINPNT TCQDGWFSTM KDYLEKEHGR KQKGFVNHWV PIFQAFKILM
KCNLFIMC
//
