ID A0A2U9BBW5_SCOMX Unreviewed; 3983 AA.
AC A0A2U9BBW5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative lymphocyte antigen 75-like {ECO:0000313|EMBL:AWP01299.1};
GN ORFNames=SMAX5B_012449 {ECO:0000313|EMBL:AWP01299.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP01299.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP01299.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) 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}.
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DR EMBL; CP026247; AWP01299.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000020198; -.
DR Proteomes; UP000246464; Chromosome 5.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; 17.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 18.
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; IPR033760; Integrin_beta_N.
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; IPR016201; PSI.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF00059; Lectin_C; 17.
DR Pfam; PF17205; PSI_integrin; 1.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00034; CLECT; 18.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 18.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 17.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
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, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2134..2157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3932..3953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 896..944
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 962..1076
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1105..1226
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1250..1362
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1407..1528
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1551..1670
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1696..1821
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1852..1958
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1990..2113
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2400..2448
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 2461..2579
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2607..2731
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2751..2858
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2899..3038
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 3201..3326
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 3352..3456
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 3491..3599
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 3639..3749
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 3796..3921
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 2201..2222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3768..3788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 901..927
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 915..942
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 2405..2431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 2419..2446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 3983 AA; 445492 MW; 0B7F7F491325B24F CRC64;
MVSEDAPEGS CSAGSAVTCD QCLRLSPHCA WCTQENFTDW FSVGERCDTL EILVEKGCAA
SLLEFPVSNG QILRDRPLGK KTGSANSTQI SPQKMALKLR AGSQLTFQVR IQHTEDYPVD
MYYLMDLSAS MIDDLETIKD LGSSLSREMA DLTSKFRMGF GSFVEKPVLP FIRITEEELA
NPCSGVGSTC LPAFGYKHVL SLTSSTDKFN AIITKQRVSA NIDVPECGFD AVMQAAVCGD
KIGWRNDSMR LLVFVSDADS HFGMDSKMAG IVIPNDGQCH LDVNNEYSMS TVQEYPTLGQ
LIDKVVENNV LLIFAVTEKQ IHNYKNYANL IPGATVGVLA TDSRNILELI VTAYKEMRSE
IELEVLGDTE ELQMSFTAIC PNGTVLPDQK RCSNIKPGET VVFNVSVELP GCLSGVRHFS
LKPVGLQDSL EVELESLCSC DCRQPPEANS SQCAAGQGAF HCGVCVCQPG FLGAQCECNE
DSALLSNCLA SNESGICSGQ GQCYCGQCVC HASSFGSIYG PYCECDDYSC VRFRGELCGG
HGACDCGECH CQSGWTGEYC NCSTSTEACV SEDGAVCGGR GKCECGHCVC TVPGASGDKC
EKCPTCGDAC SSARTCVECH LQDKDEAESC EQTCSVPKIS INTTGDYDKG SSMPCALMTE
NECWISFNVV DSETGTTAYN LQMYGCPEPP NIPMIILGVS LSVVCIGLIL LGVWKVLVSV
HDRKEVAKFE AERAKAKWQS EQDDDGDDEL LDRAQLRDFY KKGVFILECE PLKRCVTVDR
SNLVLEDCGR PTRRMLWKWV SQHRLFNVGT SMCLGLNTSD ATQPLGLFEC DTAAPALWWR
CSGKMLYGAS QWKVAVAGRL VVVKRNSYHE WKRHNTNGEG PCSYPYEDIH TLLGNAHGMP
CALPFKYNNK WFSECTSEGR EDYLQWCSTT TRYDEAEKWG FCPVQDSSCE HFWESNQELH
ACYQFNLYTI LTWSQALSTC QAQGGNLLSI TSLAEYRYIR DRLASVGVMV WIGLNHLKNG
RGWQWADGAP LSLVNLTTAL PASPLQVNRQ CGVYNSASDG RWQSLSCESA LPYICKKTPN
HTRRAEPLEN WQYIRTECAN GWWPHNGFCY AVLPETEGGS WEESARACGS RGANLTSLSS
LSEVEMLLNL LANFSDDGTE AWIGLWKRPS SPSVEWSDGS PVTLTLWHQY QPPHNLTDAT
LCAKVDGKKG NWLLASCDKR LPAVCRRESQ NPVHPPGTWD EGCPEGWKRH GPSCYTVTSH
EQSYGDALMG YYCKASLLTV ENRFEQAFVN SLLSERGANS SMYYWISLTD QKEMREYSWL
LHNGSSQPVT FTNWNKHQPV SAGGCVAMSG GPALGHWEVK DCKSFKALSV CKQSVSSYHD
LQLPEHHVDA HAPCPPGWES RSGLLDCFKV FHDEKVLMKR SWVEADFFCQ ALGAQLASFY
HYEEQVFVKQ LLSTMFEGAQ GRWFWVGLNK RDPESPGAWE WSDGSLVVTS FIEDKNEEDD
RRDCAVYSDL TNAVTPQPCD TKHEWICKVP RGEKLKKPYW YTEESEPWVF YRGAEYLLAK
QPFDWDAVSL ACQMMGAYLL SLHSRDELHF VKDRLRRLSL GPTDWWIGLS TGQPGEEVRW
SDKTAVDFQN WANGNAGGGL RKNGLCVTMS SSTGKWSTNR CGDLHGYVCK RKTASVVETP
REPHYIGGCP EKWLYFGHKC LLFHLPDSPK EGKSWKDAQS ICSSFEGSLV AIEDEIEQAY
ITMLLQGSSV GVWIGLGDGD IMKWTNGRTV SYTNWSPIEP KSYLTDDEWL SGFAKEPLCI
VLSNNHNFHL TGKWYDEKCS ETGYGFICQK PQDTSKPPTH SYHHPLPDNI EYRSRSYKVV
SGNMSWYDAM HLCIENDSDL VSITDAYHQA FLTVLVNRLA VPHWIGLYSQ DSGINYQWSD
GSDTVYTHWD AADDDDDSVI GECVYVDVNG GWRRADCETP LPGALCQVST PSNKPFTSHK
VVCPSTWVKF GAGCYNFEPV VEKLTFEESR EHCRQKVNTS DVLTVESETE NRFVLEQLWS
SGLRHQAVWL GMHFNIDTDS MAWVDGSPVD YTNWLDKAPD PELLTTDACV TTSVVDGVWH
LSRCNERLGF VCKILTGDVA EVEVEPLNGS HHGVIAEAVL VAVLFFALLA GVMWFVYKRN
PARFRGVPMF GRAYYRQTGS HSLESDGNFF LSLRPPSLSI SPSAARRSSP FMKETTTTTT
TTTAAAAAEP LSAAGTMLTS TAATLRLCLL TALLWGTCPP ARSVQGFDED AFAIQHAGTG
KCLATGASTH LNLTTCDPNS RSQMWKWGSG HRLFHVSTSH CLALDVQAKT LSLVDCGTNI
LLWWRCLDGA VYTVYQMGLA VSEGKVAARR DTNDTWVRGG SRDNICHRPY RVVHTVSGNS
AGKPCDFPFK YNGSWHHGCL PDADFPELSW CATSSDYDQD REKGLCLTPE EGCKTLFAGP
EGEFCYEFAS SAAVTWQAAL DSCRSQGADL FSLSGPEDLH SKTFLDGLGS MPERMWIGLH
QLDTSQGWQW SDGSPLSVLR WETGMPSPSA ILASGCGVLN SKQNFESEAC NKQLPYVCKK
SVNASCTATT ESSVYKETVC ADGWVPWNGW CYKLEKDEPR NFTDALQHCN TTVGGRDGFL
ASLHSIDSKE MISTNFHADG QFLDVWIGLT GINMNPTTVF KWINQAPVTF TFWGPNEPVQ
PTQDTSCVFY SGESHGWRVG TCTLRLPFMC QTKGEVRESA TQTGCRFEDG WRRHGNSCYQ
VNTKQVSFKD RCNITIRNRF EQAFINRLLG EHISQEPQYF WTGVQDIKNT GEYQWLSQDG
SPGLVTYTNW AWFEPGQHGG CAVLSTNQPL GKWEVKNCTI FKAGTICRAD LSPLPSPEPE
PNPNTTCPNG WVSRENIRYC YKVFHEERLS RKRSWEEAER FCQALGASLP SFTNVAEMRA
LHSIMRETIS NNRYFWVGLN RRNPSDRSWQ WSDGRPVSME VLQDDFHEDD AYSRDCSAFK
TTKSTLKHLF VFLNHHLPPT PFYNTPFHCD SRLEWACQIP RGKTPKNPDW YNPGGHHETS
VFVDGAEFWF VHEPKLTFEE ARLFCSTNDS KMAAPTTSTA AMQIHQYLKN ISSTPKQNWW
IDLTEPGRIF PMTYTQMFFY HSVFLGRCIS ISPESIFPNH ELSCRQQLSF VCERHNITSV
EIKPLEPQPG GLPCGNESLS FRNKCYTLMR SKKPVPFRYA NENCQSVRGT LVTISDQVEQ
DFITTLMPGM RNMDRIWIGL KIKRNDPEWV DQSPVDYLNF NPLLLGMHKA IHINTWDPDS
IDFCVFLINN PDSAMLGTWD YSSCTQYQNV AVCQHYADKV EEPHVRAEPF HIGNHTVQLV
AKNLTWFEAL EQCRSKNMDL ASVADTLFQS TLTVHVSRAR TPMWIGLFSE DDGIHYRWTD
HSHTVFNRWS SDVTSGSCVY LDTDGFWKAT ECEQKLGGAI CHKPHKETIT TPEDVAAKCP
HKMNGPNWIP FKNNCYSFQL VSSRWEEFNQ GQIHETCKKL HPDADILTIR NAEENEFIKL
QLLPFQSLAQ FVWLGLFKDD NDDQMKWYDG TKVQYSNWAK GRPNVDEPFM AGLTTQGNWL
LVSNQNLFSE FKQRTIVTCK LDHEPKQEYN TSSADFQRYG NLTYDVVTRK LSWFQALEEC
GQRGGHLASV HDLQHSAHVE LIAKSDGFPL WIGLSNQDVS DSAFEWSDGT RFDYKAAISD
SKDGSGSDQQ EASCVLVTPA GAWVKTGCNT LVDGAICYTT TITTTSQRAR MRSAPEANRC
PQSNGAPSGM SKWVRHQDHC YAFDMSFYNY SVYSKEQAGG ICQSMDAQLL TIKTKEENDF
VSKYITDDSL ITGRVWLGID LDTQGKPVSW QDGSALAYSN WKPEASDAGK KSAPHCAVMV
AGDEGIWSFV SCQASYSRVV CKTEAKSAGS PVALGLFIII VIILVAVIGF IVYRKKRAHF
PSTVRYKRTY DESDATSIIT DAD
//
