ID V9K8F1_CALMI Unreviewed; 1222 AA.
AC V9K8F1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Laminin subunit gamma-1 {ECO:0000313|EMBL:AFO94111.1};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO94111.1};
RN [1] {ECO:0000313|EMBL:AFO94111.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Intestine {ECO:0000313|EMBL:AFO94111.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; JW861594; AFO94111.1; -; mRNA.
DR AlphaFoldDB; V9K8F1; -.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00055; EGF_Lam; 8.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF270; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 9.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00180; EGF_Lam; 9.
DR SMART; SM00281; LamB; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 8.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 6.
DR PROSITE; PS51115; LAMININ_IVA; 1.
PE 2: Evidence at transcript level;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Secreted {ECO:0000256|ARBA:ARBA00022869}.
FT DOMAIN 11..57
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 58..107
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 134..302
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 337..385
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 497..547
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 548..595
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 596..643
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 648..708
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 793..862
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 913..968
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 997..1191
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 11..23
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 31..40
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 78..87
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 355..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 520..529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 548..560
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 550..567
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 569..578
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 596..608
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 616..625
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFO94111.1"
SQ SEQUENCE 1222 AA; 134807 MW; 51E5B9555EFA5F41 CRC64;
RQGPNARCLS CDCSLVGSLS TQCDNYGRCS CKPGVMGDKC DRCQPGYHSL TEAGCRPCAC
NPAGSTAECS LDTGRCICKD NVEGFNCERC KPGFFNLEPS NPHGCTACFC FGHSSVCSKA
EDYSVHRITA SFDTGLDGWR AEQRDGGEVP LQWSPMSHDI SVTSNNYLPV YYVAPGNFLG
NQLMSYGQNL SFTFYMDRRD TRLSAEDLIL EGAGLRVTVP LIAQGNQYPT ETPQIYTFRL
HEVSSYPWRP LLSSFEFQRL LHNLTGIKIR GTYSENTPGH LDDVALLTAR PGPGSPALWV
ERCTCPTAYQ GQFCEQCAPG YRRENPSLGP FSPCVPCMCN AHSDSCDPET GECYCRDYTA
GPNCERCMDG YYGDSTYGSS VDCKPCPCPS GSSCAVGPRL KEVVCTSCPA GTTGKRCELC
DDGYYGDPLG EEGPVRPCRV CQCSDNIDPN AVGNCNRQTG ECLKCIYNTA GFYCDRCKED
FYGHALTPNP AEKCKPCNCS PYGTVNQQRS CNQVTGLCEC LPHVIDRDCS QCEQGFYNIL
SGQGCQSCDC NSIGSTDGQC DIRSGQCECQ PGIVGQRCDR CESYHFGFGL DGCKPCDCDH
EGSRTPQCKE DGRCDCKEGF VGTHCDQCEE NYFYNRTRPG CQECPTCYRL VKDKVNEQRQ
KLKDLEDLIA NLGTSQDTVS DKAFEERLKE AEKTIMDLLR DAQNMQEVDN SLMDRLAEIN
NTLSIQWGRL QNIKDTVDIT DDLASRSTNR VRDVEQMISN SRRELEKGKT LLGNLSIATP
DSSGDPNNMT LLAEEARKLA EMHQKEADSI EQTAKDANDT STKAYDLLQK TLAGESEITN
NINDLNRKYN EAKAMSWELE KQATKVHSDA QEAGNKALEI YANLTSLPAV DTKALENKAD
KIMKEAMDLD DVIDNKLKNY NDMRDDLKAK ETEVKSLLDK GKTEQQTADQ LLARADAAKA
LAEDAAKKGK ATLQEAQDIL TNLQDFDKRV NDNKTAAEEA LKKISSIQDT IDAASAKTKQ
AEDALGTARM DASAAKKTAE EAERIATKLQ TNAAKTKQDA DDTFDKAMKL ANEVNDMKQQ
MNEVEDELTA KQTEADQDMM MANMASQAAQ EADENARKAK KAVQNVLNTV NKLLGELGQL
DNVDVSKLKE IEETLNKAKD QMKNSDLEQK LEDLDKAAKE QENAINAYGQ DIIDIIKDIE
NLDDIKKTLP PGCYNTQSLE TP
//
