UniProt: H0VFV6

Database: UniProt
Entry: H0VFV6_CAVPO

LinkDB:  H0VFV6_CAVPO 
Original site:  H0VFV6_CAVPO

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Ontology (14)   
   GO (14)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (4)   
   Pfam (3)   
   PROSITE (5)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (37)   

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ID   H0VFV6_CAVPO            Unreviewed;      1800 AA.
AC   H0VFV6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Laminin subunit beta 2 {ECO:0000313|Ensembl:ENSCPOP00000008968.3};
GN   Name=LAMB2 {ECO:0000313|Ensembl:ENSCPOP00000008968.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000008968.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000008968.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000008968.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; AAKN02012891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003476714.1; XM_003476666.3.
DR   STRING; 10141.ENSCPOP00000008968; -.
DR   Ensembl; ENSCPOT00000010083.3; ENSCPOP00000008968.3; ENSCPOG00000009993.4.
DR   GeneID; 100732418; -.
DR   KEGG; cpoc:100732418; -.
DR   CTD; 3913; -.
DR   VEuPathDB; HostDB:ENSCPOG00000009993; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   GeneTree; ENSGT00940000156060; -.
DR   HOGENOM; CLU_001560_1_0_1; -.
DR   InParanoid; H0VFV6; -.
DR   OMA; SCRDHTG; -.
DR   OrthoDB; 90222at2759; -.
DR   TreeFam; TF312903; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000009993; Expressed in heart left ventricle and 12 other cell types or tissues.
DR   GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR   GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0150043; F:structural constituent of synapse-associated extracellular matrix; IEA:Ensembl.
DR   GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR   GO; GO:0048677; P:axon extension involved in regeneration; IEA:Ensembl.
DR   GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR   GO; GO:0072274; P:metanephric glomerular basement membrane development; IEA:Ensembl.
DR   GO; GO:0072249; P:metanephric podocyte development; IEA:Ensembl.
DR   GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR   CDD; cd22299; cc_LAMB2_C; 1.
DR   CDD; cd00055; EGF_Lam; 13.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 9.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013015; Laminin_IV_B.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00053; Laminin_EGF; 13.
DR   Pfam; PF21199; LAMININ_IV_B; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00180; EGF_Lam; 13.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 13.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 6.
DR   PROSITE; PS50027; EGF_LAM_2; 12.
DR   PROSITE; PS51116; LAMININ_IVB; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..1800
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011665890"
FT   DOMAIN          46..284
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          285..348
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          349..411
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          412..471
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          472..523
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          524..569
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          563..779
FT                   /note="Laminin IV type B"
FT                   /evidence="ECO:0000259|PROSITE:PS51116"
FT   DOMAIN          785..832
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          833..878
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          879..928
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          929..987
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          988..1039
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1040..1096
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1145..1191
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   REGION          1343..1367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1257..1298
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1479..1527
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1582..1619
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1733..1788
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1344..1367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        314..323
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        379..388
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        442..451
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        495..504
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        507..521
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        524..536
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        526..543
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        545..554
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        785..797
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        787..804
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        806..815
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        833..845
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        835..852
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        854..863
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        898..907
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        958..967
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1012..1021
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1069..1078
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1145..1157
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1147..1164
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1166..1175
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1800 AA;  197014 MW;  673799E755FCF268 CRC64;
     MEWAAGDQGR GRQGQPVSWD LRLGLLLSVL ATTLAQAPSL DVPGCSQGSC YPATGDLLVG
     RADRLTASST CGLRGPQPYC IVSHLQDEKK CFLCDSRRPF SPDNPHSHRI QNVVTSFAPQ
     RRAAWWQSEN GVRMVTIQLD LEAEFHFTHL IMTFKTFRPA AMLVERSADF GRTWHVYRYF
     SYNCGADFPG VPLAPPRHWD DVVCESRYSE IEPSTEGEVI YRVLDPAIPI PDPYSPRIQN
     LLKITNLRVN LTRLHTLGDN LLDPRREIRE KYYYALYELV VRGNCFCYGH ASQCAPAPGA
     PAHAEGMVHG ACVCKHNTQG LNCEQCQDFY HDLPWHPAED GHSHACRKCE CHGHTHSCHF
     DMAIYLASGN VSGGVCDRCQ HNTVGHHCEL CRPFFYRDPM KDLRDPAVCR PCDCDPMGSQ
     DGGLCDSHDD AALGLVSGQC RCKEHVMGPR CQRCRSGFFG LSASDPLGCR RCQCNTRGTV
     PGDTPCDANS GTCFCKRLVT GHGCDHCLPG HWGLSHDLLG CRPCNCDVGG ALDPQCDETT
     GQCHCRQHMV GRRCEQVQPG YFRPYLDHLT WEAEDARGQV LSVVERLAAT QETPSWTGPG
     FVQLREGQTL EFLVTSLPKA MDYDVLLRLE PQVPEQWAEI EFTVERPDFV AAYSLCGHVL
     PSDDHIQKTL QADSRYMVLP KPVCLEPGTS YRLHLKLVRT GGSAQPETPY SGPVLLIDSL
     VLLPRVLALE MFSAGDASAL ERRATFEHYR CHEEGLMPSK TPPTEACAPL LISLSTLIYN
     GALSCQCDPE GSLSSECNPH GGQCRCKPGV VGRRCNICAT GYYGFGPAGC QACQCSPEGA
     LSGLCEGTTG QCPCRTGAFG LRCDHCQRGQ WGFPNCRPCI CNGHADECDT HTGICLNCRD
     HTGGEHCERC IAGFYGDPQL PYGGQCRPCP CPEGPESQRN FATSCHRDGY SQQIVCHCRS
     GYTGLRCDTC APGHFGDPSR PGGRCLPCEC SGNIDPMDPD ACDPRTGQCL RCLYHTEGPH
     CAYCKPGFHG QATRQSCHRC TCNLLGTNPQ QCPSTDQCQC DLSSGQCPCL PNVQGLSCDR
     CAPNFWNFTS GRGCQPCACH LTRARSPTCN EFTGQCNCHA GFGGRSCSEC QELHWGDPGL
     QCRACDCDPR GIDTPQCHRS TGHCSCRPGV SGVRCDQCAR GFSGVFPACH PCHVCFGDWD
     RIVQDLAART QRLEQWAQEL QQTGVLGAFE SSFRHIQEKL GMVQAIVGAR NTSAASTAQL
     VEAIEDLRSE IGEATEQLTR LEAELTNVQD ENFNANHALS SLERDGLALN LTLRQLDQHL
     DLLKHSNFLG AYDSIRHAYS QSAEAERRAN TSTLSVPSPV SNSADTRHRT EALMGAQRED
     FNRRHLANQR ALSELSAHTH TLSLTDINEL VCGAPGDEPC ATSPCGGASC RDEDGQPRCG
     GLGCSGAAAT ADLALARARH TQAELQRALV EGGGILSQVA ETRRQADEAQ QRAQAALDKA
     NASRGQVEQA NQELRELIQS VKDFLSQEGA DPDSIEMVAM RVLELSIPAS PEQIQHLASE
     IAERVQNLED VDTILAHTVG DVRRAEQLLQ DAQRARSWAE AEKQKAETVQ KALEEALRAQ
     GVAQGAIQGA VIDTKNIEQT LHQVQERMTG TEQALSSAGE RAQQLDALLE GLKLKWAGNS
     LAASTAEETA GSAHTRAQEA EQLLQGPVGD QYQTVKALAE RKAEGVLAAQ TRAEQLRDEA
     RGLLQVAQDK LQRLQELEGT YKENERALED KAAQLDGLEA RMRDVLQAIN LQVQIYNTCQ
//

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